Timothy Arthur James Haystead

Timothy Arthur James Haystead
Professor of Pharmacology and Cancer Biology

Haystead, Timothy. Using chemical biology approaches to define novel drug targets for the treatment of hypertension, obesity, cancer, inflammatory and infectious disease.

Research Interests

The major focus of my laboratory is the discovery and development of novel small molecule inhibitors targeting purine-utilizing proteins involved in various aspects of human disease. Specific targets of interest include heat shock protein 90 (Hsp90), heat shock protein 70 (Hsp70), fatty acid synthase, acetyl CoA Carboxylase, DAPK3 (ZIPK), PIM kinases, dengue fever non-structural protein 5 (NS5) and TAK1 (haysteadlab.com). Hsp90, Hsp70 and fatty acid synthase all have cancer and antiviral therapeutic indications and we are actively developing a series molecules specifically targeting these proteins that were scratch discovered in our laboratory. We have also developed a series of novel imaging molecules based on our Hsp90 inhibitor series that have utility as both diagnostics and potentially curative strategies for a number human cancers and viral infections. Our DAPK(ZIPK) and PIMK inhibitors have shown indications as anti-hypertensive agents as well as having utility in preventing reperfusion injury after stroke. Our TAK1 inhibitor program (discovered with the Derbyshire Laboratory, Department of Chemistry, Duke) has defined a highly potent and selective inhibitor of TAK1 kinase an important protein kinases thought to mediate the actions of proinflammatory cytokines such as TNFa, IL1 and TGFb. The foundations of these programs are based on the development a chemoproteomic strategy utilizing affinity methods combined with in house organic synthetic chemistry.

Current Appointments & Affiliations

Professor of Pharmacology and Cancer Biology, Pharmacology & Cancer Biology, Basic Science Departments 2015
Associate Professor in Pathology, Pathology, Clinical Science Departments 2002
Member of the Duke Cancer Institute, Duke Cancer Institute, Institutes and Centers 2000

Contact Information

C 118 LSRC, Durham, NC 27708
Duke Box 3813, Durham, NC 27710
timothy.haystead@dm.duke.edu (919) 613-8609
haystead lab

Background
Education, Training, & Certifications
- Ph.D., University of Dundee (United Kingdom) 1988
Duke Appointment History
- Associate Professor of Pharmacology & Cancer Biology, Pharmacology & Cancer Biology, Basic Science Departments 2001 - 2015
- Instructor, Temporary in the Department of Pharmacology & Cancer Biology, Pharmacology & Cancer Biology, Basic Science Departments 2000 - 2001
Recognition
In the News
- DEC 13, 2017 Duke Health News
  
  Lyme Study Uses Drug Discovery Methods That Have Fueled Cancer Breakthroughs
- AUG 17, 2017 Duke Health News
  
  Lab Tests Show Molecule Appears to Spur Cell Death in Tumors, Inflammation
- MAY 27, 2014
  
  Making Room for Luck
Research
Selected Grants
- Pharmacological Sciences Training Grant awarded by National Institutes of Health 2020 - 2025
- Targeting Borrelia specific immune cell populations in vivo through expression of ectopically expressed Hsp90 awarded by Bill & Marian Cook Foundation 2019 - 2021
- Improving the Oral Bioavailability and In vivo Efficacy of the TAK 1 Inhibitor, Takinib. awarded by Eydis Bio Inc. 2019 - 2021
- Co-crystalization of inducible Heat shock Protein 70 with the inhibitor HS-72 and structural analogs. awarded by Open Philanthropy Project 2018 - 2021
- Improving the Oral Bioavailability and in vivo efficacy of the TAK 1 inhibitor, Takinib. awarded by North Carolina Biotechnology Center 2019 - 2021
- Detection and Elimination of Oncogenic Signaling Networks in Pre-malignant and Malignant Cells with Magnetic Resonance Imaging awarded by Department of Defense 2012 - 2020
- Interdisciplinary Training Program in Lung Disease awarded by National Institutes of Health 2009 - 2020
- Organization and Function of Cellular Structure awarded by National Institutes of Health 1975 - 2020
- Pharmacological Sciences Training Program awarded by National Institutes of Health 1975 - 2020
- Pharmacology Industry Internships for Ph.D. Students awarded by American Society for Pharmacology and Experimental Therapeutics 2017 - 2019
- A novel strategy to see and treat breast cancer: translation to intra-operative breast margin assessment awarded by National Institutes of Health 2017 - 2019
- Development of Tethered Hsp90 Inhibitors Carrying Radioiodinated Probes to Specifically Descriminate and Kill Malignant Breast Tumor Cells awarded by Department of Defense 2015 - 2019
- Discovery of novel liver host targets for malaria treatment awarded by National Institutes of Health 2016 - 2019
- Literature search of clinical trials studies on Hsp90 inhibitors awarded by Open Philanthropy Project 2017 - 2018
- Co-crystallization of Hsp70i and the inhibitor HS-72 awarded by Open Philanthropy Project 2017 - 2018
- Targeting the synthetic essential kinases of breast cancers awarded by Department of Defense 2015 - 2018
- Preclinical Development of Novel HSP90 Inhibitors for the Prevention and Treatment of Chikungunya Virus Infections awarded by National University of Singapore 2014 - 2016
- The Duke Multidisciplinary Training Program in Pediatric Lung Disease awarded by National Institutes of Health 2010 - 2016
- Discovery and development of broad spectrum anti-flaviviral drugs awarded by National Institutes of Health 2010 - 2016
- A Novel Method to Stop HIV Replication: Inhibition of Human Purine-Utilizing Proteins awarded by Ohio State University 2010 - 2014
- Molecular mechanisms of chemoresistance in breast cancer awarded by National Institutes of Health 2010 - 2012
- Calcium desensitization in Smooth Muscle. awarded by National Institutes of Health 2010 - 2011
- Maturation of Normal & Sensitized Airway Contractility awarded by National Institutes of Health 2006 - 2011
- Proteome Mining as a Predictive Tool of Drug Toxicity awarded by National Institutes of Health 2005 - 2010
- G Protein Involvement in Oncogenesis and Metastasis awarded by National Institutes of Health 2004 - 2009
- Pseudomonas Invasion and the Role of Caveolin-2 awarded by National Institutes of Health 2006 - 2009
- Regulation of smooth muscle-myosin phosphatase 1 kinase awarded by National Institutes of Health 2005 - 2008
- Protein Phosphatase 1 Regulation by Multiple Subunits awarded by National Institutes of Health 2000 - 2006
- Graduate Training Program in Pharmacological Sciences. awarded by National Institutes of Health 1975 - 2005
- Proteomic/Genetic Approaches to Monoamine Transporters awarded by National Institutes of Health 2003 - 2004
- Activation of critical gene sets for spinal axon repair awarded by National Institutes of Health 2001 - 2004
- missing activity
External Relationships
- Eydis
- Open philanthropy.org
Publications & Artistic Works
Selected Publications
- Academic Articles
  - Kaneko, Kensuke, Takuya Osada, Michael A. Morse, William R. Gwin, Joshua D. Ginzel, Joshua C. Snyder, Xiao-Yi Yang, et al. “Heat shock protein 90-targeted photodynamic therapy enables treatment of subcutaneous and visceral tumors.” Commun Biol 3, no. 1 (May 8, 2020): 226. https://doi.org/10.1038/s42003-020-0956-7.
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  - Scarneo, Scott A., Liesl S. Eibschutz, Phillip J. Bendele, Kelly W. Yang, Juliane Totzke, Philip Hughes, David A. Fox, and Timothy A. J. Haystead. “Pharmacological inhibition of TAK1, with the selective inhibitor takinib, alleviates clinical manifestation of arthritis in CIA mice.” Arthritis Res Ther 21, no. 1 (December 17, 2019): 292. https://doi.org/10.1186/s13075-019-2073-x.
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  - Liao, Kuo-Chieh, Christina F. Sandall, David A. Carlson, Annegret Ulke-Lemée, Jaye M. Platnich, Philip F. Hughes, Daniel A. Muruve, Timothy A. J. Haystead, and Justin A. MacDonald. “Application of immobilized ATP to the study of NLRP inflammasomes.” Arch Biochem Biophys 670 (July 30, 2019): 104–15. https://doi.org/10.1016/j.abb.2018.12.031.
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  - Raphemot, Rene, Amber Leigh Eubanks, Maria Toro-Moreno, Rechel Anne Geiger, Philip Floyd Hughes, Kuan-Yi Lu, Timothy Arthur James Haystead, and Emily Rose Derbyshire. “Plasmodium PK9 Inhibitors Promote Growth of Liver-Stage Parasites.” Cell Chem Biol 26, no. 3 (March 21, 2019): 411-419.e7. https://doi.org/10.1016/j.chembiol.2018.11.003.
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  - Crouch, Brian T., Jennifer Gallagher, Roujia Wang, Joy Duer, Allison Hall, Mary Scott Soo, Philip Hughes, Timothy Haystead, and Nirmala Ramanujam. “Exploiting heat shock protein expression to develop a non-invasive diagnostic tool for breast cancer.” Sci Rep 9, no. 1 (March 5, 2019): 3461. https://doi.org/10.1038/s41598-019-40252-y.
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  - Sager, Rebecca A., Mark R. Woodford, Sarah J. Backe, Alan M. Makedon, Alexander J. Baker-Williams, Bryanna T. DiGregorio, David R. Loiselle, et al. “Post-translational Regulation of FNIP1 Creates a Rheostat for the Molecular Chaperone Hsp90.” Cell Rep 26, no. 5 (January 29, 2019): 1344-1356.e5. https://doi.org/10.1016/j.celrep.2019.01.018.
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  - Turner, Sara R., Mona Chappellaz, Brittany Popowich, Anne A. Wooldridge, Timothy A. J. Haystead, William C. Cole, and Justin A. MacDonald. “Smoothelin-like 1 deletion enhances myogenic reactivity of mesenteric arteries with alterations in PKC and myosin phosphatase signaling.” Sci Rep 9, no. 1 (January 24, 2019): 481. https://doi.org/10.1038/s41598-018-36564-0.
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  - Scarneo, Scott A., Antoine Mansourati, Liesl S. Eibschutz, Juliane Totzke, Jose R. Roques, David Loiselle, David Carlson, Philip Hughes, and Timothy A. J. Haystead. “Genetic and pharmacological validation of TAK1 inhibition in macrophages as a therapeutic strategy to effectively inhibit TNF secretion.” Sci Rep 8, no. 1 (November 19, 2018): 17058. https://doi.org/10.1038/s41598-018-35189-7.
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  - Carlson, David A., Miriam R. Singer, Cindy Sutherland, Clara Redondo, Leila T. Alexander, Philip F. Hughes, Stefan Knapp, et al. “Targeting Pim Kinases and DAPK3 to Control Hypertension.” Cell Chem Biol 25, no. 10 (October 18, 2018): 1195-1207.e32. https://doi.org/10.1016/j.chembiol.2018.06.006.
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  - Neckers, Len, Brian Blagg, Timothy Haystead, Jane B. Trepel, Luke Whitesell, and Didier Picard. “Methods to validate Hsp90 inhibitor specificity, to identify off-target effects, and to rethink approaches for further clinical development.” Cell Stress Chaperones 23, no. 4 (July 2018): 467–82. https://doi.org/10.1007/s12192-018-0877-2.
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  - Posfai, Dora, Amber L. Eubanks, Allison I. Keim, Kuan-Yi Lu, Grace Z. Wang, Philip F. Hughes, Nobutaka Kato, Timothy A. Haystead, and Emily R. Derbyshire. “Identification of Hsp90 Inhibitors with Anti-Plasmodium Activity.” Antimicrob Agents Chemother 62, no. 4 (April 2018). https://doi.org/10.1128/AAC.01799-17.
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  - Bellaye, Pierre-Simon, Chiko Shimbori, Toyoshi Yanagihara, David A. Carlson, Philip Hughes, Chandak Upagupta, Seidai Sato, et al. “Synergistic role of HSP90α and HSP90β to promote myofibroblast persistence in lung fibrosis.” Eur Respir J 51, no. 2 (February 2018). https://doi.org/10.1183/13993003.00386-2017.
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  - Haystead, T. A. J. “Fluorescent-Linked Enzyme Chemoproteomic Strategy (FLECS) for Identifying HSP70 Inhibitors.” Methods Mol Biol 1709 (2018): 75–86. https://doi.org/10.1007/978-1-4939-7477-1_6.
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  - Osada, Takuya, Kensuke Kaneko, William R. Gwin, Michael A. Morse, Amy Hobeika, Brian W. Pogue, Zachary C. Hartman, Philip F. Hughes, Timothy Haystead, and H Kim Lyerly. “In Vivo Detection of HSP90 Identifies Breast Cancers with Aggressive Behavior.” Clin Cancer Res 23, no. 24 (December 15, 2017): 7531–42. https://doi.org/10.1158/1078-0432.CCR-17-1453.
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  - Crouch, Brian, Helen Murphy, Stella Belonwu, Amy Martinez, Jennifer Gallagher, Allison Hall, Mary Scott Soo, et al. “Leveraging ectopic Hsp90 expression to assay the presence of tumor cells and aggressive tumor phenotypes in breast specimens.” Sci Rep 7, no. 1 (December 13, 2017): 17487. https://doi.org/10.1038/s41598-017-17832-x.
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  - Dushukyan, Natela, Diana M. Dunn, Rebecca A. Sager, Mark R. Woodford, David R. Loiselle, Michael Daneshvar, Alexander J. Baker-Williams, et al. “Phosphorylation and Ubiquitination Regulate Protein Phosphatase 5 Activity and Its Prosurvival Role in Kidney Cancer.” Cell Rep 21, no. 7 (November 14, 2017): 1883–95. https://doi.org/10.1016/j.celrep.2017.10.074.
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  - Zhu, Caigang, Amy F. Martinez, Hannah L. Martin, Martin Li, Brian T. Crouch, David A. Carlson, Timothy A. J. Haystead, and Nimmi Ramanujam. “Near-simultaneous intravital microscopy of glucose uptake and mitochondrial membrane potential, key endpoints that reflect major metabolic axes in cancer.” Sci Rep 7, no. 1 (October 23, 2017): 13772. https://doi.org/10.1038/s41598-017-14226-x.
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  - Kulkarni, Manjusha M., Annette N. Ratcliff, Menakshi Bhat, Yazan Alwarawrah, Philip Hughes, Jesus Arcos, David Loiselle, et al. “Cellular fatty acid synthase is required for late stages of HIV-1 replication.” Retrovirology 14, no. 1 (September 29, 2017): 45. https://doi.org/10.1186/s12977-017-0368-z.
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  - Totzke, Juliane, Deepak Gurbani, Rene Raphemot, Philip F. Hughes, Khaldon Bodoor, David A. Carlson, David R. Loiselle, et al. “Takinib, a Selective TAK1 Inhibitor, Broadens the Therapeutic Efficacy of TNF-α Inhibition for Cancer and Autoimmune Disease.” Cell Chem Biol 24, no. 8 (August 17, 2017): 1029-1039.e7. https://doi.org/10.1016/j.chembiol.2017.07.011.
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  - Crowe, Lauren B., Philip F. Hughes, David A. Alcorta, Takuya Osada, Aaron P. Smith, Juliane Totzke, David R. Loiselle, et al. “A Fluorescent Hsp90 Probe Demonstrates the Unique Association between Extracellular Hsp90 and Malignancy in Vivo.” Acs Chem Biol 12, no. 4 (April 21, 2017): 1047–55. https://doi.org/10.1021/acschembio.7b00006.
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  - Ogawa, Mikako, Yusuke Tomita, Yuko Nakamura, Min-Jung Lee, Sunmin Lee, Saori Tomita, Tadanobu Nagaya, et al. “Immunogenic cancer cell death selectively induced by near infrared photoimmunotherapy initiates host tumor immunity.” Oncotarget 8, no. 6 (February 7, 2017): 10425–36. https://doi.org/10.18632/oncotarget.14425.
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  - Smith, A. P., and T. A. J. Haystead. “Hsp90: A key target in HIV infection.” Future Virology 12, no. 2 (February 1, 2017): 55–59. https://doi.org/10.2217/fvl-2016-0122.
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  - Martin, Mackenzie D., Jeremy D. Baker, Amirthaa Suntharalingam, Bryce A. Nordhues, Lindsey B. Shelton, Dali Zheng, Jonathan J. Sabbagh, Timothy A. J. Haystead, Jason E. Gestwicki, and Chad A. Dickey. “Inhibition of Both Hsp70 Activity and Tau Aggregation in Vitro Best Predicts Tau Lowering Activity of Small Molecules.” Acs Chem Biol 11, no. 7 (July 15, 2016): 2041–48. https://doi.org/10.1021/acschembio.6b00223.
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  - Woodford, Mark R., Diana M. Dunn, Adam R. Blanden, Dante Capriotti, David Loiselle, Chrisostomos Prodromou, Barry Panaretou, et al. “The FNIP co-chaperones decelerate the Hsp90 chaperone cycle and enhance drug binding.” Nature Communications 7 (June 29, 2016): 12037. https://doi.org/10.1038/ncomms12037.
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  - Alwarawrah, Yazan, Philip Hughes, David Loiselle, David A. Carlson, David B. Darr, Jamie L. Jordan, Jessie Xiong, et al. “Fasnall, a Selective FASN Inhibitor, Shows Potent Anti-tumor Activity in the MMTV-Neu Model of HER2(+) Breast Cancer.” Cell Chem Biol 23, no. 6 (June 23, 2016): 678–88. https://doi.org/10.1016/j.chembiol.2016.04.011.
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  - Howe, Matthew K., Brittany L. Speer, Philip F. Hughes, David R. Loiselle, Subhash Vasudevan, and Timothy A. J. Haystead. “An inducible heat shock protein 70 small molecule inhibitor demonstrates anti-dengue virus activity, validating Hsp70 as a host antiviral target.” Antiviral Res 130 (June 2016): 81–92. https://doi.org/10.1016/j.antiviral.2016.03.017.
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  - MacDonald, Justin A., Cindy Sutherland, David A. Carlson, Sabreena Bhaidani, Abdulhameed Al-Ghabkari, Karl Swärd, Timothy A. J. Haystead, and Michael P. Walsh. “A Small Molecule Pyrazolo[3,4-d]Pyrimidinone Inhibitor of Zipper-Interacting Protein Kinase Suppresses Calcium Sensitization of Vascular Smooth Muscle.” Mol Pharmacol 89, no. 1 (January 2016): 105–17. https://doi.org/10.1124/mol.115.100529.
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  - Dunn, Diana M., Mark R. Woodford, Andrew W. Truman, Sandra M. Jensen, Jacqualyn Schulman, Tiffany Caza, Taylor C. Remillard, et al. “c-Abl Mediated Tyrosine Phosphorylation of Aha1 Activates Its Co-chaperone Function in Cancer Cells.” Cell Rep 12, no. 6 (August 11, 2015): 1006–18. https://doi.org/10.1016/j.celrep.2015.07.004.
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  - Lontay, Beata, Khaldon Bodoor, Adrienn Sipos, Douglas H. Weitzel, David Loiselle, Rachid Safi, Donghai Zheng, et al. “Pregnancy and Smoothelin-like Protein 1 (SMTNL1) Deletion Promote the Switching of Skeletal Muscle to a Glycolytic Phenotype in Human and Mice.” J Biol Chem 290, no. 29 (July 17, 2015): 17985–98. https://doi.org/10.1074/jbc.M115.658120.
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  - Howe, Matthew K., Khaldon Bodoor, David A. Carlson, Philip F. Hughes, Yazan Alwarawrah, David R. Loiselle, Alex M. Jaeger, et al. “Identification of an allosteric small-molecule inhibitor selective for the inducible form of heat shock protein 70.” Chem Biol 21, no. 12 (December 18, 2014): 1648–59. https://doi.org/10.1016/j.chembiol.2014.10.016.
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  - Rathore, Abhay P. S., Timothy Haystead, Pratyush K. Das, Andres Merits, Mah-Lee Ng, and Subhash G. Vasudevan. “Chikungunya virus nsP3 & nsP4 interacts with HSP-90 to promote virus replication: HSP-90 inhibitors reduce CHIKV infection and inflammation in vivo.” Antiviral Res 103 (March 2014): 7–16. https://doi.org/10.1016/j.antiviral.2013.12.010.
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  - Carlson, David A., Aaron S. Franke, Douglas H. Weitzel, Brittany L. Speer, Philip F. Hughes, Laura Hagerty, Christopher N. Fortner, et al. “Fluorescence linked enzyme chemoproteomic strategy for discovery of a potent and selective DAPK1 and ZIPK inhibitor.” Acs Chem Biol 8, no. 12 (December 20, 2013): 2715–23. https://doi.org/10.1021/cb400407c.
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  - Yasuda, K., H. Zhang, D. Loiselle, T. Haystead, I. G. Macara, and S. Mili. “The RNA-binding protein Fus directs translation of localized mrnas in APC-RNP granules.” Journal of Cell Biology 203, no. 5 (December 9, 2013): 737–46. https://doi.org/10.1083/jcb.201306058.
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  - Barrott, Jared J., Philip F. Hughes, Takuya Osada, Xiao-Yi Yang, Zachary C. Hartman, David R. Loiselle, Neil L. Spector, et al. “Optical and radioiodinated tethered Hsp90 inhibitors reveal selective internalization of ectopic Hsp90 in malignant breast tumor cells.” Chem Biol 20, no. 9 (September 19, 2013): 1187–97. https://doi.org/10.1016/j.chembiol.2013.08.004.
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  - Barrott, Jared J., and Timothy A. J. Haystead. “Hsp90, an unlikely ally in the war on cancer.” Febs J 280, no. 6 (March 2013): 1381–96. https://doi.org/10.1111/febs.12147.
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  - LaMonte, Gregory, Nisha Philip, Joseph Reardon, Joshua R. Lacsina, William Majoros, Lesley Chapman, Courtney D. Thornburg, et al. “Translocation of sickle cell erythrocyte microRNAs into Plasmodium falciparum inhibits parasite translation and contributes to malaria resistance.” Cell Host Microbe 12, no. 2 (August 16, 2012): 187–99. https://doi.org/10.1016/j.chom.2012.06.007.
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  - Hughes, Philip F., Jared J. Barrott, David A. Carlson, David R. Loiselle, Brittany L. Speer, Khaldon Bodoor, Lauretta A. Rund, and Timothy A. J. Haystead. “A highly selective Hsp90 affinity chromatography resin with a cleavable linker.” Bioorg Med Chem 20, no. 10 (May 15, 2012): 3298–3305. https://doi.org/10.1016/j.bmc.2012.03.043.
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  - Cheng, Qing, Jeffrey T. Chang, Joseph Geradts, Leonard M. Neckers, Timothy Haystead, Neil L. Spector, and H Kim Lyerly. “Amplification and high-level expression of heat shock protein 90 marks aggressive phenotypes of human epidermal growth factor receptor 2 negative breast cancer.” Breast Cancer Res 14, no. 2 (April 17, 2012): R62. https://doi.org/10.1186/bcr3168.
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  - Duncan, James S., Timothy A. J. Haystead, and David W. Litchfield. “Chemoproteomic characterization of protein kinase inhibitors using immobilized ATP.” Methods Mol Biol 795 (2012): 119–34. https://doi.org/10.1007/978-1-61779-337-0_8.
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  - Bodoor, Khaldon, Beata Lontay, Rachid Safi, Douglas H. Weitzel, David Loiselle, Zhengzheng Wei, Szabolcs Lengyel, Donald P. McDonnell, and Timothy A. Haystead. “Smoothelin-like 1 protein is a bifunctional regulator of the progesterone receptor during pregnancy.” J Biol Chem 286, no. 36 (September 9, 2011): 31839–51. https://doi.org/10.1074/jbc.M111.270397.
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  - Iioka, Hidekazu, David Loiselle, Timothy A. Haystead, and Ian G. Macara. “Efficient detection of RNA-protein interactions using tethered RNAs.” Nucleic Acids Res 39, no. 8 (April 2011): e53. https://doi.org/10.1093/nar/gkq1316.
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  - Sparks, Matthew A., Kelly K. Parsons, Johannes Stegbauer, Susan B. Gurley, Anuradha Vivekanandan-Giri, Christopher N. Fortner, Jay Snouwaert, et al. “Angiotensin II type 1A receptors in vascular smooth muscle cells do not influence aortic remodeling in hypertension.” Hypertension 57, no. 3 (March 2011): 577–85. https://doi.org/10.1161/HYPERTENSIONAHA.110.165274.
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  - Weitzel, Douglas H., Jenica Chambers, and Timothy A. J. Haystead. “Phosphorylation-dependent control of ZIPK nuclear import is species specific.” Cell Signal 23, no. 1 (January 2011): 297–303. https://doi.org/10.1016/j.cellsig.2010.09.016.
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  - Haystead, T. A. J. “Rapid characterization of in vivo phosphorylation sites and the protein kinases and phosphatases that regulate them by affinity capture” 2 (December 1, 2010): 1247–51. https://doi.org/10.1016/B978-0-12-374145-5.00154-6.
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  - Lontay, Beata, Khaldon Bodoor, Douglas H. Weitzel, David Loiselle, Christopher Fortner, Szabolcs Lengyel, Donghai Zheng, James Devente, Robert Hickner, and Timothy A. J. Haystead. “Smoothelin-like 1 protein regulates myosin phosphatase-targeting subunit 1 expression during sexual development and pregnancy.” J Biol Chem 285, no. 38 (September 17, 2010): 29357–66. https://doi.org/10.1074/jbc.M110.143966.
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  - Fadden, Patrick, Kenneth H. Huang, James M. Veal, Paul M. Steed, Amy F. Barabasz, Briana Foley, Mei Hu, et al. “Application of chemoproteomics to drug discovery: identification of a clinical candidate targeting hsp90.” Chem Biol 17, no. 7 (July 30, 2010): 686–94. https://doi.org/10.1016/j.chembiol.2010.04.015.
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  - Borman, Meredith A., Tiffany A. Freed, Timothy A. J. Haystead, and Justin A. Macdonald. “The role of the calponin homology domain of smoothelin-like 1 (SMTNL1) in myosin phosphatase inhibition and smooth muscle contraction.” Mol Cell Biochem 327, no. 1–2 (July 2009): 93–100. https://doi.org/10.1007/s11010-009-0047-z.
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  - Okamura, Tatsunori, Simendra Singh, John Buolamwini, Timothy Haystead, Henry Friedman, Darell Bigner, and Francis Ali-Osman. “Tyrosine phosphorylation of the human glutathione S-transferase P1 by epidermal growth factor receptor.” J Biol Chem 284, no. 25 (June 19, 2009): 16979–89. https://doi.org/10.1074/jbc.M808153200.
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  - Doerig, Christian, Oliver Billker, Timothy Haystead, Pushkar Sharma, Andrew B. Tobin, and Norman C. Waters. “Protein kinases of malaria parasites: an update.” Trends Parasitol 24, no. 12 (December 2008): 570–77. https://doi.org/10.1016/j.pt.2008.08.007.
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  - Duncan, James S., Laszlo Gyenis, John Lenehan, Maria Bretner, Lee M. Graves, Timothy A. Haystead, and David W. Litchfield. “An unbiased evaluation of CK2 inhibitors by chemoproteomics: characterization of inhibitor effects on CK2 and identification of novel inhibitor targets.” Mol Cell Proteomics 7, no. 6 (June 2008): 1077–88. https://doi.org/10.1074/mcp.M700559-MCP200.
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  - Higgins, M. J., D. Loiselle, T. A. Haystead, and L. M. Graves. “Human cytidine triphosphate synthetase 1 interacting proteins.” Nucleosides Nucleotides Nucleic Acids 27, no. 6 (June 2008): 850–57. https://doi.org/10.1080/15257770802146502.
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  - Wooldridge, Anne A., Christopher N. Fortner, Beata Lontay, Takayuki Akimoto, Ronald L. Neppl, Carie Facemire, Michael B. Datto, et al. “Deletion of the protein kinase A/protein kinase G target SMTNL1 promotes an exercise-adapted phenotype in vascular smooth muscle.” J Biol Chem 283, no. 17 (April 25, 2008): 11850–59. https://doi.org/10.1074/jbc.M708628200.
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  - Howard, Brandon A., Gregory D. Sempowski, Richard M. Scearce, Hua-Xin Liao, David M. Lee, Gordon K. Lam, Haiyen Chen, Patrick Fadden, Timothy Haystead, and Barton F. Haynes. “Murine CD7 shares antigenic cross-reactivity with HSP-60.” Hybridoma (Larchmt) 27, no. 2 (April 2008): 81–89. https://doi.org/10.1089/hyb.2007.0553.
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  - Hilder, Thomas L., Michael H. Malone, Sompop Bencharit, John Colicelli, Timothy A. Haystead, Gary L. Johnson, and Christine C. Wu. “Proteomic identification of the cerebral cavernous malformation signaling complex.” J Proteome Res 6, no. 11 (November 2007): 4343–55. https://doi.org/10.1021/pr0704276.
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  - Philip, Nisha, and Timothy A. Haystead. “Characterization of a UBC13 kinase in Plasmodium falciparum.” Proc Natl Acad Sci U S A 104, no. 19 (May 8, 2007): 7845–50. https://doi.org/10.1073/pnas.0611601104.
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  - Mulugu, Sashidhar, Wenli Bai, Peter C. Fridy, Robert J. Bastidas, James C. Otto, D Eric Dollins, Timothy A. Haystead, Anthony A. Ribeiro, and John D. York. “A conserved family of enzymes that phosphorylate inositol hexakisphosphate.” Science 316, no. 5821 (April 6, 2007): 106–9. https://doi.org/10.1126/science.1139099.
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  - Kwiek, Nicole C., Drew F. Thacker, and Timothy A. J. Haystead. “Dual kinase-mediated regulation of PITK by CaMKII and GSK3.” Cell Signal 19, no. 3 (March 2007): 593–99. https://doi.org/10.1016/j.cellsig.2006.08.009.
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  - Hagerty, Laura, Douglas H. Weitzel, Jenica Chambers, Christopher N. Fortner, Matthew H. Brush, David Loiselle, Hiroshi Hosoya, and Timothy A. J. Haystead. “ROCK1 phosphorylates and activates zipper-interacting protein kinase.” J Biol Chem 282, no. 7 (February 16, 2007): 4884–93. https://doi.org/10.1074/jbc.M609990200.
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  - Borman, Meredith A., Justin A. MacDonald, and Timothy A. J. Haystead. “Staurosporine inhibition of zipper-interacting protein kinase contractile effects in gastrointestinal smooth muscle.” Biochem Cell Biol 85, no. 1 (February 2007): 111–20. https://doi.org/10.1139/o06-209.
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  - Walker, James R., Annie J. Gnanam, Alexandra L. Blinkova, Mary Jo Hermandson, Mikhail A. Karymov, Yuri L. Lyubchenko, Paul R. Graves, Timothy A. Haystead, and Klaus D. Linse. “Clostridium taeniosporum spore ribbon-like appendage structure, composition and genes.” Mol Microbiol 63, no. 3 (February 2007): 629–43. https://doi.org/10.1111/j.1365-2958.2006.05494.x.
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  - Moorhead, Greg B. G., Timothy A. J. Haystead, and Carol MacKintosh. “Synthesis and use of the protein phosphatase affinity matrices microcystin-sepharose and microcystin-biotin-sepharose.” Methods Mol Biol 365 (2007): 39–45. https://doi.org/10.1385/1-59745-267-X:39.
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  - Wooldridge, Anne A., and Timothy A. Haystead. “Real-time in vivo proteomic identification of novel kinase substrates in smooth muscle.” Methods Mol Biol 357 (2007): 235–52. https://doi.org/10.1385/1-59745-214-9:235.
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  - Philip, N., and T. A. Haystead. “Affinity Purification with Natural Immobilized Ligands” 4 (December 1, 2006): 265–67. https://doi.org/10.1016/B978-012164730-8/50218-5.
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  - Kwiek, Nicole C., Drew F. Thacker, Michael B. Datto, Heather B. Megosh, and Timothy A. J. Haystead. “PITK, a PP1 targeting subunit that modulates the phosphorylation of the transcriptional regulator hnRNP K.” Cell Signal 18, no. 10 (October 2006): 1769–78. https://doi.org/10.1016/j.cellsig.2006.01.019.
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  - Gurley, Susan B., Alicia Allred, Thu H. Le, Robert Griffiths, Lan Mao, Nisha Philip, Timothy A. Haystead, et al. “Altered blood pressure responses and normal cardiac phenotype in ACE2-null mice.” J Clin Invest 116, no. 8 (August 2006): 2218–25. https://doi.org/10.1172/JCI16980.
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  - Margolis, Seth S., Jennifer A. Perry, Douglas H. Weitzel, Christopher D. Freel, Minoru Yoshida, Timothy A. Haystead, and Sally Kornbluth. “A role for PP1 in the Cdc2/Cyclin B-mediated positive feedback activation of Cdc25.” Mol Biol Cell 17, no. 4 (April 2006): 1779–89. https://doi.org/10.1091/mbc.e05-08-0751.
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  - Hagerty, Laura, and Timothy A. J. Haystead. “Delineating signal transduction pathways in smooth muscle through focused proteomics.” Expert Rev Proteomics 3, no. 1 (February 2006): 75–85. https://doi.org/10.1586/14789450.3.1.75.
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  - Haystead, Timothy A. J. “The purinome, a complex mix of drug and toxicity targets.” Curr Top Med Chem 6, no. 11 (2006): 1117–27. https://doi.org/10.2174/156802606777812059.
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  - Haystead, Timothy A. J. “ZIP kinase, a key regulator of myosin protein phosphatase 1.” Cell Signal 17, no. 11 (November 2005): 1313–22. https://doi.org/10.1016/j.cellsig.2005.05.008.
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  - Kremer, Brandon E., Timothy Haystead, and Ian G. Macara. “Mammalian septins regulate microtubule stability through interaction with the microtubule-binding protein MAP4.” Mol Biol Cell 16, no. 10 (October 2005): 4648–59. https://doi.org/10.1091/mbc.e05-03-0267.
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  - Hilder, Thomas L., Gerald M. Carlson, Timothy A. J. Haystead, Edwin G. Krebs, and Lee M. Graves. “Caspase-3 dependent cleavage and activation of skeletal muscle phosphorylase b kinase.” Mol Cell Biochem 275, no. 1–2 (July 2005): 233–42. https://doi.org/10.1007/s11010-005-2411-y.
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  - Graves, P. R., K. M. Winkfield, and T. A. J. Haystead. “Erratum: Regulation of zipper-interacting protein kinase activity in vitro and in vivo by multisite phosphorylation (Journal of Biological Chemistry (2005) 280 (9363-9374)).” Journal of Biological Chemistry 280, no. 24 (June 17, 2005): 23424.
  - Graves, P. R., K. M. Winkfield, and T. A. J. Haystead. “Regulation of zipper-interacting protein kinase activity in vitro and in vivo by multisite phosphorylation (vol 280, pg 9363, 2005).” Journal of Biological Chemistry 280, no. 24 (June 17, 2005): 23424–23424.
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  - Graves, Paul R., Karen M. Winkfield, and Timothy A. J. Haystead. “Regulation of zipper-interacting protein kinase activity in vitro and in vivo by multisite phosphorylation.” J Biol Chem 280, no. 10 (March 11, 2005): 9363–74. https://doi.org/10.1074/jbc.M412538200.
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  - Datto, M. B., and T. A. J. Haystead. “The proteome,” December 20, 2004, 153–78.
  - Lascola, Christopher D., Allen W. Song, Timothy A. Haystead, David S. Warner, Katleen Verleysen, Tiffany A. Freed, and James M. Provenzale. “Changes in magnetization transfer MRI correlate with spreading depression-induced astroglial reactivity and increased protein expression in mice.” Ajr Am J Roentgenol 183, no. 6 (December 2004): 1791–97. https://doi.org/10.2214/ajr.183.6.01831791.
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  - Cao, Heping, Wi S. Lai, Leesa J. Deterding, John Venable, Elizabeth A. Kennington, Timothy A. J. Haystead, John R. Yates, Kenneth B. Tomer, and Perry J. Blackshear. “Identification of phosphorylation sites in human tristetraprolin that affect its electrophoretic mobility.” Molecular & Cellular Proteomics 3, no. 10 (October 1, 2004): S66–S66.
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  - Borman, Meredith A., Justin A. MacDonald, and Timothy A. J. Haystead. “Modulation of smooth muscle contractility by CHASM, a novel member of the smoothelin family of proteins.” Febs Lett 573, no. 1–3 (August 27, 2004): 207–13. https://doi.org/10.1016/j.febslet.2004.08.002.
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  - Wooldridge, Anne A., Justin A. MacDonald, Ferenc Erdodi, Chaoyu Ma, Meredith A. Borman, David J. Hartshorne, and Timothy A. J. Haystead. “Smooth muscle phosphatase is regulated in vivo by exclusion of phosphorylation of threonine 696 of MYPT1 by phosphorylation of Serine 695 in response to cyclic nucleotides.” J Biol Chem 279, no. 33 (August 13, 2004): 34496–504. https://doi.org/10.1074/jbc.M405957200.
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  - Erikson, Eleanor, Timothy A. J. Haystead, Yue-Wei Qian, and James L. Maller. “A feedback loop in the polo-like kinase activation pathway.” J Biol Chem 279, no. 31 (July 30, 2004): 32219–24. https://doi.org/10.1074/jbc.M403840200.
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  - Jones, Janice C., Hemali P. Phatnani, Timothy A. Haystead, Justin A. MacDonald, S Munir Alam, and Arno L. Greenleaf. “C-terminal repeat domain kinase I phosphorylates Ser2 and Ser5 of RNA polymerase II C-terminal domain repeats.” J Biol Chem 279, no. 24 (June 11, 2004): 24957–64. https://doi.org/10.1074/jbc.M402218200.
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  - Kwiek, Jesse J., Timothy A. J. Haystead, and Johannes Rudolph. “Kinetic mechanism of quinone oxidoreductase 2 and its inhibition by the antimalarial quinolines.” Biochemistry 43, no. 15 (April 20, 2004): 4538–47. https://doi.org/10.1021/bi035923w.
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  - Graves, P. R., and T. A. J. Haystead. “Proteomics, Fluorescence, and Binding Affinity” 2–3 (November 7, 2003): 301–3. https://doi.org/10.1016/B978-012124546-7/50534-9.
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  - Mackey, Aaron J., Timothy A. J. Haystead, and William R. Pearson. “CRP: Cleavage of Radiolabeled Phosphoproteins.” Nucleic Acids Res 31, no. 13 (July 1, 2003): 3859–61. https://doi.org/10.1093/nar/gkg513.
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  - Soti, Csaba, Akos Vermes, Timothy A. J. Haystead, and Péter Csermely. “Comparative analysis of the ATP-binding sites of Hsp90 by nucleotide affinity cleavage: a distinct nucleotide specificity of the C-terminal ATP-binding site.” Eur J Biochem 270, no. 11 (June 2003): 2421–28. https://doi.org/10.1046/j.1432-1033.2003.03610.x.
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  - Haystead, T. A. J. “Response to Petri: Can a proteomics strategy be used to identify the anti-malarial activity of chloroquine?” Trends in Pharmacological Sciences 24, no. 5 (May 1, 2003): 212–13. https://doi.org/10.1016/S0165-6147(03)00072-5.
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  - Mandal, Arabinda, Kenneth L. Klotz, Jagathpala Shetty, Friederike L. Jayes, Michael J. Wolkowicz, Laura C. Bolling, Scott A. Coonrod, et al. “SLLP1, a unique, intra-acrosomal, non-bacteriolytic, c lysozyme-like protein of human spermatozoa.” Biol Reprod 68, no. 5 (May 2003): 1525–37. https://doi.org/10.1095/biolreprod.102.010108.
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  - Corcoran, Ethan E., James D. Joseph, Justin A. MacDonald, Christopher D. Kane, Timothy A. J. Haystead, and Anthony R. Means. “Proteomic analysis of calcium/calmodulin-dependent protein kinase I and IV in vitro substrates reveals distinct catalytic preferences.” J Biol Chem 278, no. 12 (March 21, 2003): 10516–22. https://doi.org/10.1074/jbc.M210642200.
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  - Graves, Paul R., and Timothy A. J. Haystead. “A functional proteomics approach to signal transduction.” Recent Prog Horm Res 58 (2003): 1–24. https://doi.org/10.1210/rp.58.1.1.
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  - Ray, Rupa, and Timothy A. Haystead. “Phosphoproteome analysis in yeast.” Methods Enzymol 366 (2003): 95–103. https://doi.org/10.1016/s0076-6879(03)66008-8.
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  - Ray, Rupa, and Timothy A. Haystead. “Mixed peptide sequencing and the FASTF/FASTS algorithms.” Methods Enzymol 366 (2003): 84–95. https://doi.org/10.1016/s0076-6879(03)66007-6.
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  - Graves, Paul R., Jesse J. Kwiek, Patrick Fadden, Rupa Ray, Klaas Hardeman, Andrew M. Coley, Michael Foley, and Timothy A. J. Haystead. “Discovery of novel targets of quinoline drugs in the human purine binding proteome.” Mol Pharmacol 62, no. 6 (December 2002): 1364–72. https://doi.org/10.1124/mol.62.6.1364.
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  - Murányi, Andrea, Justin A. MacDonald, Jing Ti Deng, David P. Wilson, Timothy A. J. Haystead, Michael P. Walsh, Ferenc Erdodi, Eniko Kiss, Yue Wu, and David J. Hartshorne. “Phosphorylation of the myosin phosphatase target subunit by integrin-linked kinase.” Biochem J 366, no. Pt 1 (August 15, 2002): 211–16. https://doi.org/10.1042/BJ20020401.
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  - Borman, Meredith A., Justin A. MacDonald, Andrea Murányi, David J. Hartshorne, and Timothy A. J. Haystead. “Smooth muscle myosin phosphatase-associated kinase induces Ca2+ sensitization via myosin phosphatase inhibition.” J Biol Chem 277, no. 26 (June 28, 2002): 23441–46. https://doi.org/10.1074/jbc.M201597200.
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  - MacDonald, Justin A., Aaron J. Mackey, William R. Pearson, and Timothy A. J. Haystead. “A strategy for the rapid identification of phosphorylation sites in the phosphoproteome.” Mol Cell Proteomics 1, no. 4 (April 2002): 314–22. https://doi.org/10.1074/mcp.m200002-mcp200.
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  - Graves, Paul R., and Timothy A. J. Haystead. “Molecular biologist's guide to proteomics.” Microbiol Mol Biol Rev 66, no. 1 (March 2002): 39–63. https://doi.org/10.1128/mmbr.66.1.39-63.2002.
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  - Huang, Min, Piotr Kozlowski, Matthew Collins, Yanhong Wang, Timothy A. Haystead, and Lee M. Graves. “Caspase-dependent cleavage of carbamoyl phosphate synthetase II during apoptosis.” Mol Pharmacol 61, no. 3 (March 2002): 569–77. https://doi.org/10.1124/mol.61.3.569.
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  - Mackey, Aaron J., Timothy A. J. Haystead, and William R. Pearson. “Getting more from less: algorithms for rapid protein identification with multiple short peptide sequences.” Mol Cell Proteomics 1, no. 2 (February 2002): 139–47. https://doi.org/10.1074/mcp.m100004-mcp200.
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  - Mandal, A., K. L. Klotz, J. Shetty, F. L. Jayes, M. J. Wolkowicz, L. C. Bolling, S. A. Coonrod, et al. “SLLP1, a novel non-bacteriolytic c lysozyme-like protein in the acrosome of human spermatozoa.” Biology of Reproduction 66 (January 1, 2002): 113–14.
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  - Joberty, G., R. R. Perlungher, P. J. Sheffield, M. Kinoshita, M. Noda, T. Haystead, and I. G. Macara. “Borg proteins control septin organization and are negatively regulated by Cdc42.” Nat Cell Biol 3, no. 10 (October 2001): 861–66. https://doi.org/10.1038/ncb1001-861.
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  - Walker, L. A., J. A. MacDonald, X. Liu, R. K. Nakamoto, T. A. Haystead, A. V. Somlyo, and A. P. Somlyo. “Site-specific phosphorylation and point mutations of telokin modulate its Ca2+-desensitizing effect in smooth muscle.” J Biol Chem 276, no. 27 (July 6, 2001): 24519–24. https://doi.org/10.1074/jbc.M103560200.
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  - Nadal, E. de, R. P. Fadden, A. Ruiz, T. Haystead, and J. Ariño. “A role for the Ppz Ser/Thr protein phosphatases in the regulation of translation elongation factor 1Balpha.” J Biol Chem 276, no. 18 (May 4, 2001): 14829–34. https://doi.org/10.1074/jbc.M010824200.
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  - Lin, C. H., S. Ficarro, T. A. J. Haystead, D. F. Hunt, and G. K. Owens. “Angiotensin II upregulation of rRNA transcription in vascular smooth muscle cells: Identification of Upstream Binding Factor (UBF) phosphorylation sites.” Arteriosclerosis Thrombosis and Vascular Biology 21, no. 4 (April 1, 2001): 684–684.
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  - MacDonald, J. A., M. Eto, M. A. Borman, D. L. Brautigan, and T. A. Haystead. “Dual Ser and Thr phosphorylation of CPI-17, an inhibitor of myosin phosphatase, by MYPT-associated kinase.” Febs Lett 493, no. 2–3 (March 30, 2001): 91–94. https://doi.org/10.1016/s0014-5793(01)02277-3.
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  - Graves, L. M., M. Huang, P. Kozlowski, M. Collins, and T. A. J. Haystead. “Caspase-dependent cleavage of the pyrimidine biosynthetic enzyme CAD during apoptosis.” Faseb Journal 15, no. 4 (March 7, 2001): A25–A25.
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  - MacDonald, J. A., M. A. Borman, A. Murányi, A. V. Somlyo, D. J. Hartshorne, and T. A. Haystead. “Identification of the endogenous smooth muscle myosin phosphatase-associated kinase.” Proc Natl Acad Sci U S A 98, no. 5 (February 27, 2001): 2419–24. https://doi.org/10.1073/pnas.041331498.
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  - MacDonald, J. A., L. A. Walker, R. K. Nakamoto, I. Gorenne, A. V. Somlyo, A. P. Somlyo, and T. A. Haystead. “Phosphorylation of telokin by cyclic nucleotide kinases and the identification of in vivo phosphorylation sites in smooth muscle.” Febs Lett 479, no. 3 (August 18, 2000): 83–88. https://doi.org/10.1016/s0014-5793(00)01884-6.
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  - Mothe-Satney, I., D. Yang, P. Fadden, T. A. Haystead, and J. C. Lawrence. “Multiple mechanisms control phosphorylation of PHAS-I in five (S/T)P sites that govern translational repression.” Mol Cell Biol 20, no. 10 (May 2000): 3558–67. https://doi.org/10.1128/mcb.20.10.3558-3567.2000.
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  - Sanz, P., G. R. Alms, T. A. Haystead, and M. Carlson. “Regulatory interactions between the Reg1-Glc7 protein phosphatase and the Snf1 protein kinase.” Mol Cell Biol 20, no. 4 (February 2000): 1321–28. https://doi.org/10.1128/mcb.20.4.1321-1328.2000.
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  - Terry-Lorenzo, R. T., M. Inoue, J. H. Connor, T. A. Haystead, B. N. Armbruster, R. P. Gupta, C. J. Oliver, and S. Shenolikar. “Neurofilament-L is a protein phosphatase-1-binding protein associated with neuronal plasma membrane and post-synaptic density.” J Biol Chem 275, no. 4 (January 28, 2000): 2439–46. https://doi.org/10.1074/jbc.275.4.2439.
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  - Walker, L. A., J. A. MacDonald, A. V. Somlyo, R. K. Nakamoto, T. A. J. Haystead, and A. P. Somlyo. “Site-specific phosphorylation of telokin modulates its relaxant effect on smooth muscle.” Biophysical Journal 78, no. 1 (January 1, 2000): 23A-23A.
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  - Gorenne, I., T. A. J. Haystead, A. S. Somlyo, and A. P. Somlyo. “An inhibitor of p160 Rho-kinase blocks MARCKS phosphorylation in vascular smooth muscle.” Molecular Biology of the Cell 10 (November 1, 1999): 247A-247A.
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  - Alms, G. R., P. Sanz, M. Carlson, and T. A. Haystead. “Reg1p targets protein phosphatase 1 to dephosphorylate hexokinase II in Saccharomyces cerevisiae: characterizing the effects of a phosphatase subunit on the yeast proteome.” Embo J 18, no. 15 (August 2, 1999): 4157–68. https://doi.org/10.1093/emboj/18.15.4157.
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  - Kihm, A. J., T. A. J. Haystead, and G. K. Owens. “Identification of kinases involved in the growth factor-induced increases in phosphorylation of the rRNA transcription factor Upstream Binding Factor (UBF).” Faseb Journal 13, no. 4 (March 12, 1999): A388–A388.
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  - Kihm, A. J., J. C. Hershey, T. A. Haystead, C. S. Madsen, and G. K. Owens. “Phosphorylation of the rRNA transcription factor upstream binding factor promotes its association with TATA binding protein.” Proc Natl Acad Sci U S A 95, no. 25 (December 8, 1998): 14816–20. https://doi.org/10.1073/pnas.95.25.14816.
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  - Damer, C. K., J. Partridge, W. R. Pearson, and T. A. Haystead. “Rapid identification of protein phosphatase 1-binding proteins by mixed peptide sequencing and data base searching. Characterization of a novel holoenzymic form of protein phosphatase 1.” J Biol Chem 273, no. 38 (September 18, 1998): 24396–405. https://doi.org/10.1074/jbc.273.38.24396.
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  - Fadden, P., T. A. Haystead, and J. C. Lawrence. “Phosphorylation of the translational regulator, PHAS-I, by protein kinase CK2.” Febs Lett 435, no. 1 (September 11, 1998): 105–9. https://doi.org/10.1016/s0014-5793(98)01047-3.
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  - Wu, X., T. A. Haystead, R. K. Nakamoto, A. V. Somlyo, and A. P. Somlyo. “Acceleration of myosin light chain dephosphorylation and relaxation of smooth muscle by telokin. Synergism with cyclic nucleotide-activated kinase.” J Biol Chem 273, no. 18 (May 1, 1998): 11362–69. https://doi.org/10.1074/jbc.273.18.11362.
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  - Perry, N. B., G. Ellis, J. W. Blunt, T. A. J. Haystead, R. J. Lake, and M. H. G. Munro. “Okadaic acid in New Zealand sponges: Detection by cytotoxicity, protein phosphatase inhibition and immunoassay techniques.” Natural Product Letters 11, no. 4 (January 1, 1998): 305–12. https://doi.org/10.1080/10575639808044964.
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  - Brunn, G. J., P. Fadden, T. A. Haystead, and J. C. Lawrence. “The mammalian target of rapamycin phosphorylates sites having a (Ser/Thr)-Pro motif and is activated by antibodies to a region near its COOH terminus.” J Biol Chem 272, no. 51 (December 19, 1997): 32547–50. https://doi.org/10.1074/jbc.272.51.32547.
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  - Scott, A., B. Erredc, and T. A. J. Haystead. “Activation of MAPK by MEK is enhanced by a thioltransferase.” Faseb Journal 11, no. 9 (December 1, 1997).
  - Grenert, J. P., W. P. Sullivan, P. Fadden, T. A. Haystead, J. Clark, E. Mimnaugh, H. Krutzsch, et al. “The amino-terminal domain of heat shock protein 90 (hsp90) that binds geldanamycin is an ATP/ADP switch domain that regulates hsp90 conformation.” J Biol Chem 272, no. 38 (September 19, 1997): 23843–50. https://doi.org/10.1074/jbc.272.38.23843.
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  - Scott, A., B. Errede, and T. A. J. Haystead. “Activation of MAPK by MEK is enhanced by a thioltransferase.” Faseb Journal 11, no. 9 (July 31, 1997): A1359–A1359.
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  - Long, W., T. A. Hillier, T. A. J. Haystead, and E. J. Barrett. “Fluorescent labeling of phosphoserines in tissue proteins.” Diabetes 46 (May 1, 1997): 766–766.
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  - Fadden, P., T. A. Haystead, and J. C. Lawrence. “Identification of phosphorylation sites in the translational regulator, PHAS-I, that are controlled by insulin and rapamycin in rat adipocytes.” J Biol Chem 272, no. 15 (April 11, 1997): 10240–47. https://doi.org/10.1074/jbc.272.15.10240.
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  - Vernon, S. M., M. J. Campos, T. Haystead, M. M. Thompson, P. E. DiCorleto, and G. K. Owens. “Endothelial cell-conditioned medium downregulates smooth muscle contractile protein expression.” Am J Physiol 272, no. 2 Pt 1 (February 1997): C582–91. https://doi.org/10.1152/ajpcell.1997.272.2.C582.
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  - Wu, X., T. A. J. Haystead, A. V. Somlyo, and A. P. Somlyo. “Telokin relaxes smooth muscle and is phosphorylated, in situ.” Biophysical Journal 72, no. 2 (February 1, 1997): TU228–TU228.
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  - Lawrence, J. C., P. Fadden, T. A. Haystead, and T. A. Lin. “PHAS proteins as mediators of the actions of insulin, growth factors and cAMP on protein synthesis and cell proliferation.” Adv Enzyme Regul 37 (1997): 239–67. https://doi.org/10.1016/s0065-2571(96)00016-7.
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  - Hershev, J. C., C. S. Madsen, J. M. Partridge, G. K. Owens, and T. A. J. Haystead. “Protein phosphatase 2a is involved in regulation of the secondary sustained phase of map kinase activity in response to vascular smooth muscle hypertrophic and mitogenic stimuli.” Faseb Journal 10, no. 3 (December 1, 1996).
  - Jefferson, L. S., S. R. Kimball, P. Fadden, T. A. J. Haystead, and J. C. Lawrence. “Effects of insulin and diabetes on the association of eukaryotic initiation factor 4e and the translational regulator, phas-i, in rat skeletal muscle.” Faseb Journal 10, no. 3 (December 1, 1996).
  - Campos, M., P. Fadden, G. Alms, Z. Qian, and T. A. Haystead. “Identification of protein phosphatase-1-binding proteins by microcystin-biotin affinity chromatography.” J Biol Chem 271, no. 45 (November 8, 1996): 28478–84. https://doi.org/10.1074/jbc.271.45.28478.
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  - Gailly, P., X. Wu, T. A. Haystead, A. P. Somlyo, P. T. Cohen, P. Cohen, and A. V. Somlyo. “Regions of the 110-kDa regulatory subunit M110 required for regulation of myosin-light-chain-phosphatase activity in smooth muscle.” Eur J Biochem 239, no. 2 (July 15, 1996): 326–32. https://doi.org/10.1111/j.1432-1033.1996.0326u.x.
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  - Hershey, J. C., C. S. Madsen, J. M. Partridge, G. K. Owens, and T. A. J. Haystead. “Protein phosphatase 2A is involved in regulation of the secondary sustained phase of MAP kinase activity in response to vascular smooth muscle hypertrophic and mitogenic stimuli.” Faseb Journal 10, no. 3 (March 8, 1996): 419–419.
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  - Jefferson, L. S., S. R. Kimball, P. Fadden, T. A. J. Haystead, and J. C. Lawrence. “Effects of insulin and diabetes on the association of eukaryotic initiation factor 4E and the translational regulator, PHAS-I, in rat skeletal muscle.” Faseb Journal 10, no. 3 (March 8, 1996): 4271–4271.
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  - Gailly, P., D. Johnson, C. M. M. Haystead, Y. H. Chen, X. Wu, T. A. J. Haystead, A. P. Somlyo, P. T. W. Cohen, A. V. Somlyo, and P. Cohen. “Regulation of smooth muscle myosin light chain phosphatase (SMPP1M) by its 110 kDa (M110) subunit.” Biophysical Journal 70, no. 2 (February 1, 1996): WPO26–WPO26.
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  - Kimball, S. R., L. S. Jefferson, P. Fadden, T. A. Haystead, and J. C. Lawrence. “Insulin and diabetes cause reciprocal changes in the association of eIF-4E and PHAS-I in rat skeletal muscle.” Am J Physiol 270, no. 2 Pt 1 (February 1996): C705–9. https://doi.org/10.1152/ajpcell.1996.270.2.C705.
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  - Kimball, S. R., L. S. Jefferson, P. Fadden, T. A. J. Haystead, and J. C. Lawrence. “Insulin and diabetes cause reciprocal changes in the association of eIF-4E and PHAS-I in rat skeletal muscle.” American Journal of Physiology Cell Physiology 270, no. 2 39-2 (February 1, 1996).
  - Kimball, S. R., L. S. Jefferson, P. Fadden, T. A. J. Haystead, and J. C. Lawrence. “Insulin and diabetes cause reciprocal changes in the association of eIF-4E and PHAS-I in rat skeletal muscle.” American Journal of Physiology Cell Physiology 270, no. 2 (February 1, 1996): C705–9.
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  - Haystead, C. M., P. Gailly, A. P. Somlyo, A. V. Somlyo, and T. A. Haystead. “Molecular cloning and functional expression of a recombinant 72.5 kDa fragment of the 110 kDa regulatory subunit of smooth muscle protein phosphatase 1M.” Febs Lett 377, no. 2 (December 18, 1995): 123–27. https://doi.org/10.1016/0014-5793(95)01318-0.
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  - NIXON, G. F., T. A. J. HAYSTEAD, A. P. SOMLYO, and A. V. SOMLYO. “PHOSPHORYLATION OF CALDESMON BY MITOGEN-ACTIVATED PROTEIN-KINASE WITH NO EFFECT ON CALCIUM SENSITIVITY IN SMOOTH-MUSCLE.” British Journal of Pharmacology 116 (December 1, 1995): P279–P279.
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  - Hershey, J. C., M. Hautmann, M. M. Thompson, L. I. Rothblum, T. A. Haystead, and G. K. Owens. “Angiotensin II-induced hypertrophy of rat vascular smooth muscle is associated with increased 18 S rRNA synthesis and phosphorylation of the rRNA transcription factor, upstream binding factor.” J Biol Chem 270, no. 42 (October 20, 1995): 25096–101. https://doi.org/10.1074/jbc.270.42.25096.
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  - Scott, A., C. M. Haystead, and T. A. Haystead. “Purification of a 12,020-dalton protein that enhances the activation of mitogen-activated protein (MAP) kinase by MAP kinase kinase.” J Biol Chem 270, no. 41 (October 13, 1995): 24540–47. https://doi.org/10.1074/jbc.270.41.24540.
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  - Nixon, G. F., K. Iizuka, C. M. Haystead, T. A. Haystead, A. P. Somlyo, and A. V. Somlyo. “Phosphorylation of caldesmon by mitogen-activated protein kinase with no effect on Ca2+ sensitivity in rabbit smooth muscle.” J Physiol 487 ( Pt 2) (September 1, 1995): 283–89. https://doi.org/10.1113/jphysiol.1995.sp020879.
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  - Fadden, P., and T. A. Haystead. “Quantitative and selective fluorophore labeling of phosphoserine on peptides and proteins: characterization at the attomole level by capillary electrophoresis and laser-induced fluorescence.” Anal Biochem 225, no. 1 (February 10, 1995): 81–88. https://doi.org/10.1006/abio.1995.1111.
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  - Haspel, J., P. Dent, T. Haystead, P. W. Brandt-Rauf, D. Chung, I. B. Weinstein, S. Nishimura, Z. Yamaizumi, and M. R. Pincus. “raf-induced kinases may be necessary but are not sufficient for ras-p21-protein induction of oocyte maturation.” Medical Science Research 23, no. 7 (January 1, 1995): 455–57.
  - Shirazi, A., K. Iizuka, P. Fadden, C. Mosse, A. P. Somlyo, A. V. Somlyo, and T. A. Haystead. “Purification and characterization of the mammalian myosin light chain phosphatase holoenzyme. The differential effects of the holoenzyme and its subunits on smooth muscle.” J Biol Chem 269, no. 50 (December 16, 1994): 31598–606.
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  - Lin, T. A., X. Kong, T. A. Haystead, A. Pause, G. Belsham, N. Sonenberg, and J. C. Lawrence. “PHAS-I as a link between mitogen-activated protein kinase and translation initiation.” Science 266, no. 5185 (October 28, 1994): 653–56. https://doi.org/10.1126/science.7939721.
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  - Haystead, T. A., C. M. Haystead, C. Hu, T. A. Lin, and J. C. Lawrence. “Phosphorylation of PHAS-I by mitogen-activated protein (MAP) kinase. Identification of a site phosphorylated by MAP kinase in vitro and in response to insulin in rat adipocytes.” J Biol Chem 269, no. 37 (September 16, 1994): 23185–91.
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  - Davies, S. P., S. A. Hawley, A. Woods, D. Carling, T. A. Haystead, and D. G. Hardie. “Purification of the AMP-activated protein kinase on ATP-gamma-sepharose and analysis of its subunit structure.” Eur J Biochem 223, no. 2 (July 15, 1994): 351–57. https://doi.org/10.1111/j.1432-1033.1994.tb19001.x.
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  - Haystead, C. M., P. Gregory, A. Shirazi, P. Fadden, C. Mosse, P. Dent, and T. A. Haystead. “Insulin activates a novel adipocyte mitogen-activated protein kinase kinase kinase that shows rapid phasic kinetics and is distinct from c-Raf.” J Biol Chem 269, no. 17 (April 29, 1994): 12804–8.
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  - Haystead, C. M., P. Gregory, T. W. Sturgill, and T. A. Haystead. “Gamma-phosphate-linked ATP-sepharose for the affinity purification of protein kinases. Rapid purification to homogeneity of skeletal muscle mitogen-activated protein kinase kinase.” Eur J Biochem 214, no. 2 (June 1, 1993): 459–67. https://doi.org/10.1111/j.1432-1033.1993.tb17942.x.
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  - Haystead, C. M., J. Wu, P. Gregory, T. W. Sturgill, and T. A. Haystead. “Functional expression of a MAP kinase kinase in COS cells and recognition by an anti-STE7/byr1 antibody.” Febs Lett 317, no. 1–2 (February 8, 1993): 12–16. https://doi.org/10.1016/0014-5793(93)81481-e.
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  - HAYSTEAD, T. A. J. “THE ROLE OF PROTEIN PHOSPHATASES IN THE SUPPRESSION OF THE MAP KINASE SIGNAL TRANSDUCTION PATHWAY.” Journal of Cellular Biochemistry, January 9, 1993, 310–310.
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  - Wu, J., H. Michel, P. Dent, T. Haystead, D. F. Hunt, and T. W. Sturgill. “Activation of MAP kinase by a dual specificity Tyr/Thr kinase.” Adv Second Messenger Phosphoprotein Res 28 (1993): 219–25.
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  - Wu, J., J. K. Harrison, L. A. Vincent, C. Haystead, T. A. Haystead, H. Michel, D. F. Hunt, K. R. Lynch, and T. W. Sturgill. “Molecular structure of a protein-tyrosine/threonine kinase activating p42 mitogen-activated protein (MAP) kinase: MAP kinase kinase.” Proc Natl Acad Sci U S A 90, no. 1 (January 1, 1993): 173–77. https://doi.org/10.1073/pnas.90.1.173.
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  - Dent, P., W. Haser, T. A. Haystead, L. A. Vincent, T. M. Roberts, and T. W. Sturgill. “Activation of mitogen-activated protein kinase kinase by v-Raf in NIH 3T3 cells and in vitro.” Science 257, no. 5075 (September 4, 1992): 1404–7. https://doi.org/10.1126/science.1326789.
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  - Wu, J., H. Michel, A. Rossomando, T. Haystead, J. Shabanowitz, D. F. Hunt, and T. W. Sturgill. “Renaturation and partial peptide sequencing of mitogen-activated protein kinase (MAP kinase) activator from rabbit skeletal muscle.” Biochem J 285 ( Pt 3) (August 1, 1992): 701–5. https://doi.org/10.1042/bj2850701.
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  - Haystead, T. A., P. Dent, J. Wu, C. M. Haystead, and T. W. Sturgill. “Ordered phosphorylation of p42mapk by MAP kinase kinase.” Febs Lett 306, no. 1 (July 13, 1992): 17–22. https://doi.org/10.1016/0014-5793(92)80828-5.
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  - Meier, K. E., K. A. Licciardi, T. A. Haystead, and E. G. Krebs. “Activation of messenger-independent protein kinases in wild-type and phorbol ester-resistant EL4 thymoma cells.” J Biol Chem 266, no. 3 (January 25, 1991): 1914–20.
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  - Hardie, D. G., T. A. Haystead, and A. T. Sim. “Use of okadaic acid to inhibit protein phosphatases in intact cells.” Methods Enzymol 201 (1991): 469–76. https://doi.org/10.1016/0076-6879(91)01042-z.
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  - Haystead, T. A., J. E. Weiel, D. W. Litchfield, Y. Tsukitani, E. H. Fischer, and E. G. Krebs. “Okadaic acid mimics the action of insulin in stimulating protein kinase activity in isolated adipocytes. The role of protein phosphatase 2a in attenuation of the signal.” J Biol Chem 265, no. 27 (September 25, 1990): 16571–80.
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  - Haystead, T. A., F. Moore, P. Cohen, and D. G. Hardie. “Roles of the AMP-activated and cyclic-AMP-dependent protein kinases in the adrenaline-induced inactivation of acetyl-CoA carboxylase in rat adipocytes.” Eur J Biochem 187, no. 1 (January 12, 1990): 199–205. https://doi.org/10.1111/j.1432-1033.1990.tb15295.x.
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  - Haystead, T. A., A. T. Sim, D. Carling, R. C. Honnor, Y. Tsukitani, P. Cohen, and D. G. Hardie. “Effects of the tumour promoter okadaic acid on intracellular protein phosphorylation and metabolism.” Nature 337, no. 6202 (January 5, 1989): 78–81. https://doi.org/10.1038/337078a0.
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  - Chepenik, K. P., and T. A. Haystead. “Epidermal growth factor alters metabolism of inositol lipids and activity of protein kinase C in mouse embryo palate mesenchyme cells.” J Craniofac Genet Dev Biol 9, no. 3 (1989): 285–301.
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  - Haystead, T. A., D. G. Campbell, and D. G. Hardie. “Analysis of sites phosphorylated on acetyl-CoA carboxylase in response to insulin in isolated adipocytes. Comparison with sites phosphorylated by casein kinase-2 and the calmodulin-dependent multiprotein kinase.” Eur J Biochem 175, no. 2 (August 1, 1988): 347–54. https://doi.org/10.1111/j.1432-1033.1988.tb14203.x.
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  - Haystead, T. A., and D. G. Hardie. “Insulin and phorbol ester stimulate phosphorylation of acetyl-CoA carboxylase at similar sites in isolated adipocytes. Lack of correspondence with sites phosphorylated on the purified enzyme by protein kinase C.” Eur J Biochem 175, no. 2 (August 1, 1988): 339–45. https://doi.org/10.1111/j.1432-1033.1988.tb14202.x.
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  - HARDIE, D. G., D. CARLING, T. A. J. HAYSTEAD, M. R. MUNDAY, and D. G. CAMPBELL. “REGULATION OF ACETYL-COA CARBOXYLASE AND HMG-COA REDUCTASE BY AMP-ACTIVATED PROTEIN-KINASE.” Faseb Journal 2, no. 6 (March 25, 1988): A1855–A1855.
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  - HAYSTEAD, T. A. J., and D. G. HARDIE. “EVIDENCE FOR CASEIN KINASE-2 MEDIATED PHOSPHORYLATION OF ACETYL-COA CARBOXYLASE IN INSULIN-TREATED ADIPOCYTES.” Faseb Journal 2, no. 5 (March 20, 1988): A993–A993.
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  - HAYSTEAD, T. A. J., and D. G. HARDIE. “ACTIVATION OF ACETYL-COA CARBOXYLASE BY INSULIN-ALLOSTERIC EFFECT OR PROTEIN-PHOSPHORYLATION.” Archives Internationales De Physiologie De Biochimie Et De Biophysique 95, no. 5 (December 1, 1987): B209–B209.
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  - Haystead, T. A., and D. G. Hardie. “Evidence that activation of acetyl-CoA carboxylase by insulin in adipocytes is mediated by a low-Mr effector and not by increased phosphorylation.” Biochem J 240, no. 1 (November 15, 1986): 99–106. https://doi.org/10.1042/bj2400099.
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  - Munday, M. R., T. A. Haystead, R. Holland, D. A. Carling, and D. G. Hardie. “The role of phosphorylation/dephosphorylation of acetyl-CoA carboxylase in the regulation of mammalian fatty acid biosynthesis.” Biochem Soc Trans 14, no. 3 (June 1986): 559–62. https://doi.org/10.1042/bst0140559.
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  - Haystead, T. A., and D. G. Hardie. “Both insulin and epidermal growth factor stimulate lipogenesis and acetyl-CoA carboxylase activity in isolated adipocytes. Importance of homogenization procedure in avoiding artefacts in acetyl-CoA carboxylase assay.” Biochem J 234, no. 2 (March 1, 1986): 279–84. https://doi.org/10.1042/bj2340279.
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  - Baker, H. F., R. M. Ridley, T. A. Haystead, and T. J. Crow. “Further consideration of the learning impairment after aceperone in the marmoset: effects of the drug on shape and colour discrimination and on an alternation task.” Pharmacol Biochem Behav 18, no. 5 (May 1983): 701–4. https://doi.org/10.1016/0091-3057(83)90009-6.
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  - Ridley, R. M., T. A. Haystead, H. F. Baker, and T. J. Crow. “A new approach to the role of noradrenaline in learning: problem-solving in the marmoset after alpha-noradrenergic receptor blockade.” Pharmacol Biochem Behav 14, no. 6 (June 1981): 849–55. https://doi.org/10.1016/0091-3057(81)90373-7.
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  - Ridley, R. M., T. A. J. Haystead, and H. F. Baker. “An involvement of dopamine in higher order choice mechanisms in the monkey.” Psychopharmacology 73, no. 3 (May 1, 1981): 306. https://doi.org/10.1007/BF00422423.
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  - Ridley, R. M., T. A. Haystead, and H. F. Baker. “An analysis of visual object reversal learning in the marmoset after amphetamine and haloperidol.” Pharmacol Biochem Behav 14, no. 3 (March 1981): 345–51. https://doi.org/10.1016/0091-3057(81)90401-9.
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  - Ridley, R. M., H. F. Baker, and T. A. Haystead. “Perseverative behaviour after amphetamine; dissociation of response tendency from reward association.” Psychopharmacology (Berl) 75, no. 3 (1981): 283–86. https://doi.org/10.1007/BF00432439.
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  - Ridley, R. M., T. A. Haystead, and H. F. Baker. “An involvement of dopamine in higher order choice mechanisms in the monkey.” Psychopharmacology (Berl) 72, no. 2 (1981): 173–77. https://doi.org/10.1007/BF00431652.
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  - Ridley, R. M., M. L. Weight, T. A. Haystead, and H. F. Baker. “"Go here-to there" performance after amphetamine: the importance of the response requirement in successive discrimination.” Psychopharmacology (Berl) 69, no. 3 (1980): 271–73. https://doi.org/10.1007/BF00433094.
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- Conference Papers
  - Crouch, B. T., J. Duer, R. Wang, J. Gallagher, A. Hall, M. S. Soo, P. Hughes, T. A. J. Haystead, and N. Ramanujam. “Optimizing fluorescently-tethered Hsp90 inhibitor dose for maximal specific uptake by breast tumors.” In Progress in Biomedical Optics and Imaging Proceedings of Spie, Vol. 10478, 2018. https://doi.org/10.1117/12.2285210.
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  - Haystead, Timothy A. J. “Fluor-tethered Inhibitors of Hsp90 Reveal Secretion and Reinternalization of Hsp90 Is Associated with Metastatic Progression.” In In Vitro Cellular & Developmental Biology Animal, 53:S8–9. SPRINGER, 2017.
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  - Barrott, Jared J., Aaron P. Smith, Takuya Osada, Nimmi Ramanujam, Michael R. Zalutsky, Kim Lyerly, and Timothy A. J. Haystead. “Abstract C86: Tethered Hsp90 inhibitors carrying optical or radioiodinated probes reveal selective internalization of ectopic Hsp90 in malignant breast tumor cells.” In Drug Metabolism, Transport, and Biodistribution. American Association for Cancer Research, 2013. https://doi.org/10.1158/1535-7163.targ-13-c86.
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  - Mandal, A., K. L. Klotz, J. Shetty, S. A. Vemuganti, M. A. Coppola, T. A. J. Haystead, C. J. Flickinger, and J. C. Herr. “SLLP2, a novel non-bacteriolytic lysozyme-like protein of human spermatozoa linked to the X chromosome.” In Biology of Reproduction, 125–125. SOC STUDY REPRODUCTION, 2004.
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  - Lawrence, J. C., T. A. Lin, X. M. Kong, T. A. J. Haystead, and C. B. Hu. “PHAS-I: A new player in the regulation of protein synthesis by insulin and growth factors.” In Diabetes 1994, edited by S. Baba and T. Kaneko, 1100:622–29. ELSEVIER SCIENCE PUBL B V, 1995.
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- Datasets
  - Crowe, Lauren B., Phillip F. Hughes, David A. Acorta, Takuya Osada, Aaron P. Smith, Julaine Totke, David R. Loiselle, et al. “Cryo-sectioned mice for investigating HS-131 uptake,” July 18, 2016. https://doi.org/10.7924/G8G44N63.
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