Scholars@Duke
Michael T Forrester

Michael T Forrester

Medical Instructor in the Department of Medicine
Medicine, Pulmonary, Allergy, and Critical Care Medicine
michael.forrester@duke.edu
303 Research Drive, Sands 455,, Durham, NC 27710

Selected Publications

Topology-driven discovery of transmembrane protein S-palmitoylation.

Journal Article J Biol Chem · March 2025 Protein S-palmitoylation is a reversible lipophilic posttranslational modification regulating diverse signaling pathways. Within transmembrane proteins (TMPs), S-palmitoylation is implicated in conditions from inflammatory disorders to respiratory viral in ... Full text Link to item Cite

Analysis of Protein Cysteine Acylation Using a Modified Suspension Trap (Acyl-Trap).

Journal Article J Proteome Res · August 2, 2024 Proteins undergo reversible S-acylation via a thioester linkage in vivo. S-palmitoylation, modification by C16:0 fatty acid, is a common S-acylation that mediates critical protein-membrane and protein-protein interactions. The most widely used S-acylation ... Full text Link to item Cite

Ischemic priapism due to coagulopathy of severe COVID-19 infection

Journal Article Journal of Clinical Urology · November 1, 2023 Initially thought to be a primarily respiratory disease process, the hypercoagulable state associated with COVID-19 has been associated with myriad clinical sequelae. We report a case of stuttering ischemic priapism associated with COVID-19, and describe a ... Full text Cite

ERK-dependent proteasome degradation of Txnip regulates thioredoxin oxidoreductase activity.

Journal Article J Biol Chem · September 6, 2019 Dynamic control of thioredoxin (Trx) oxidoreductase activity is essential for balancing the need of cells to rapidly respond to oxidative/nitrosative stress and to temporally regulate thiol-based redox signaling. We have previously shown that cytokine stim ... Full text Link to item Cite

Thioredoxin-mediated denitrosylation regulates cytokine-induced nuclear factor κB (NF-κB) activation.

Journal Article J Biol Chem · January 31, 2014 S-nitrosylation of nuclear factor κB (NF-κB) on the p65 subunit of the p50/p65 heterodimer inhibits NF-κB DNA binding activity. We have recently shown that p65 is constitutively S-nitrosylated in the lung and that LPS-induced injury elicits a decrease in S ... Full text Link to item Cite

Proteomic analysis of the NOS2 interactome in human airway epithelial cells.

Journal Article Nitric Oxide · November 1, 2013 The cytokine-inducible isoform of nitric oxide synthase (NOS2) is constitutively expressed in human respiratory epithelia and is upregulated in inflammatory lung disease. Here, we sought to better define the protein interactions that may be important for N ... Full text Link to item Cite

Solid-phase capture for the detection and relative quantification of S-nitrosoproteins by mass spectrometry.

Journal Article Methods · August 1, 2013 The proteomic analysis of S-nitrosylated protein (SNO-proteins) has long depended on the biotin switch technique (BST), which requires blocking of free thiols, ascorbate-based denitrosylation of SNO-Cys, biotinylation of nascent thiol and avidin-based affi ... Full text Link to item Cite

Response to "is flavohemoglobin a nitric oxide dioxygenase?"

Journal Article Free Radical Biology and Medicine · September 1, 2012 Full text Cite

Protection from nitrosative stress: a central role for microbial flavohemoglobin.

Journal Article Free Radic Biol Med · May 1, 2012 Nitric oxide (NO) is an inevitable product of life in an oxygen- and nitrogen-rich environment. This reactive diatomic molecule exhibits microbial cytotoxicity, in large part by facilitating nitrosative stress and inhibiting heme-containing proteins within ... Full text Link to item Cite

Glioma stem cell proliferation and tumor growth are promoted by nitric oxide synthase-2.

Journal Article Cell · July 8, 2011 Malignant gliomas are aggressive brain tumors with limited therapeutic options, and improvements in treatment require a deeper molecular understanding of this disease. As in other cancers, recent studies have identified highly tumorigenic subpopulations wi ... Full text Link to item Cite

Site-specific analysis of protein S-acylation by resin-assisted capture.

Journal Article J Lipid Res · February 2011 Protein S-acylation is a major posttranslational modification whereby a cysteine thiol is converted to a thioester. A prototype is S-palmitoylation (fatty acylation), in which a protein undergoes acylation with a hydrophobic 16 carbon lipid chain. Although ... Full text Link to item Cite

Bacterial flavohemoglobin: a molecular tool to probe mammalian nitric oxide biology.

Journal Article Biotechniques · January 2011 A wide range of mammalian signaling and stress pathways are mediated by nitric oxide (NO), which is synthesized in vivo by the nitric oxide synthase (NOS) family of enzymes. Experimental manipulations of NO are frequently achieved by either inhibition or a ... Full text Link to item Cite

S-nitrosylation in cardiovascular signaling.

Journal Article Circ Res · March 5, 2010 Well over 2 decades have passed since the endothelium-derived relaxation factor was reported to be the gaseous molecule nitric oxide (NO). Although soluble guanylyl cyclase (which generates cyclic guanosine monophosphate, cGMP) was the first identified rec ... Full text Link to item Cite

Thioredoxin-interacting protein (Txnip) is a feedback regulator of S-nitrosylation.

Journal Article J Biol Chem · December 25, 2009 Nitric oxide exerts a plethora of biological effects via protein S-nitrosylation, a redox-based reaction that converts a protein Cys thiol to a S-nitrosothiol. However, although the regulation of protein S-nitrosylation has been the subject of extensive st ... Full text Link to item Cite

A protein microarray-based analysis of S-nitrosylation.

Journal Article Proc Natl Acad Sci U S A · November 10, 2009 The ubiquitous cellular influence of nitric oxide (NO) is exerted substantially through protein S-nitrosylation. Whereas NO is highly promiscuous, physiological S-nitrosylation is typically restricted to one or very few Cys residue(s) in target proteins. T ... Full text Link to item Cite

Protein denitrosylation: enzymatic mechanisms and cellular functions.

Journal Article Nat Rev Mol Cell Biol · October 2009 S-Nitrosylation, the redox-based modification of Cys thiol side chains by nitric oxide, is a common mechanism in signal transduction. Dysregulated S-nitrosylation contributes to a range of human pathologies. New roles for protein denitrosylation in regulat ... Full text Link to item Cite

Oxygen-regulated beta(2)-adrenergic receptor hydroxylation by EGLN3 and ubiquitylation by pVHL.

Journal Article Sci Signal · July 7, 2009 Agonist-induced ubiquitylation and degradation of heterotrimeric guanine nucleotide-binding protein (G protein)-coupled receptors (GPCRs) play an essential role in surface receptor homeostasis, thereby tuning many physiological processes. Although beta-arr ... Full text Link to item Cite

Proteomic analysis of S-nitrosylation and denitrosylation by resin-assisted capture.

Journal Article Nat Biotechnol · June 2009 We have modified the biotin switch assay for protein S-nitrosothiols (SNOs), using resin-assisted capture (SNO-RAC). Compared with existing methodologies, SNO-RAC requires fewer steps, detects high-mass S-nitrosylated proteins more efficiently, and facilit ... Full text Link to item Cite

Detection of protein S-nitrosylation with the biotin-switch technique.

Journal Article Free Radic Biol Med · January 15, 2009 Protein S-nitrosylation, the posttranslational modification of cysteine thiols to form S-nitrosothiols, is a principle mechanism of nitric oxide-based signaling. Studies have demonstrated myriad roles for S-nitrosylation in organisms from bacteria to human ... Full text Link to item Cite

Regulated protein denitrosylation by cytosolic and mitochondrial thioredoxins.

Journal Article Science · May 23, 2008 Nitric oxide acts substantially in cellular signal transduction through stimulus-coupled S-nitrosylation of cysteine residues. The mechanisms that might subserve protein denitrosylation in cellular signaling remain uncharacterized. Our search for denitrosy ... Full text Link to item Cite

Assessment and application of the biotin switch technique for examining protein S-nitrosylation under conditions of pharmacologically induced oxidative stress.

Journal Article J Biol Chem · May 11, 2007 Protein S-nitrosylation has emerged as a principal mechanism by which nitric oxide exerts biological effects. Among methods for studying protein S-nitrosylation, the biotin switch technique (BST) has rapidly gained popularity because of the ease with which ... Full text Link to item Cite

A classification scheme for redox-based modifications of proteins.

Journal Article Am J Respir Cell Mol Biol · February 2007 Full text Link to item Cite

Nitrosative stress in the ER: a new role for S-nitrosylation in neurodegenerative diseases.

Journal Article ACS Chem Biol · July 21, 2006 S-Nitrosylation, the covalent addition of a nitrogen monoxide group to a cysteine thiol, has been shown to modify the function of a broad spectrum of mammalian, plant, and microbial proteins and thereby to convey the ubiquitous influence of nitric oxide on ... Full text Link to item Cite