Scholars@Duke
Jennifer Mehlman Carbrey

Jennifer Mehlman Carbrey

Associate Professor of the Practice of Medical Education in Cell Biology
Cell Biology
jennifer.carbrey@duke.edu
Duke Box 3709, Durham, NC 27710
366 Nanaline Duke Bldg, Durham, NC 27710

Selected Publications

Coursera’s Introductory Human Physiology Course: Factors that Characterize Successful Completion of a MOOC

Journal Article International Review of Research in Open and Distributed Learning · April 2015 Since Massive Open Online Courses (MOOCs) are accessible by anyone in the world at no cost, they have large enrollments that are conducive to educational research. This study examines students in the Coursera MOOC, Introductory Human Physiology. Of the 33, ... Open Access Link to item Cite

A comparison of the effectiveness of the team-based learning readiness assessments completed at home to those completed in class.

Journal Article J Educ Eval Health Prof · 2015 PURPOSE: The readiness assurance process (RAP) of team-based learning (TBL) is an important element that ensures that students come prepared to learn. However, the RAP can use a significant amount of class time which could otherwise be used for application ... Full text Open Access Link to item Cite

Reduced arsenic clearance and increased toxicity in aquaglyceroporin-9-null mice.

Journal Article Proc Natl Acad Sci U S A · September 15, 2009 Expressed in liver, aquaglyceroporin-9 (AQP9) is permeated by glycerol, arsenite, and other small, neutral solutes. To evaluate a possible protective role, AQP9-null mice were evaluated for in vivo arsenic toxicity. After injection with NaAsO(2), AQP9-null ... Full text Link to item Cite

Aquaporin 6 binds calmodulin in a calcium-dependent manner.

Journal Article Biochem Biophys Res Commun · May 22, 2009 Featured Publication Aquaporin 6 (AQP6) is an anion channel that is expressed primarily in acid secreting alpha-intercalated cells of the kidney collecting duct. In addition, AQP6 anion channel permeability is gated by low pH. Inspection of the N-terminus of AQP6 revealed a pu ... Full text Link to item Cite

Osteoclast differentiation and function in aquaglyceroporin AQP9-null mice.

Journal Article Biol Cell · March 2009 Featured Publication BACKGROUND INFORMATION: Osteoclasts are cells specialized for bone resorption and play important roles in bone growth and calcium homoeostasis. Differentiation of osteoclasts involves fusion of bone marrow macrophage mononuclear precursors in response to e ... Full text Link to item Cite

Discovery of the aquaporins and development of the field.

Journal Article Handb Exp Pharmacol · 2009 Featured Publication The study of water transport began long before the molecular identification of water channels with studies of water-permeable tissues. The discovery of the first aquaporin, AQP1, occurred during experiments focused on the identity of the Rh blood group ant ... Full text Link to item Cite

Aquaporin 9 is the major pathway for glycerol uptake by mouse erythrocytes, with implications for malarial virulence.

Journal Article Proc Natl Acad Sci U S A · July 24, 2007 Featured Publication Human and rodent erythrocytes are known to be highly permeable to glycerol. Aquaglyceroporin aquaporin (AQP)3 is the major glycerol channel in human and rat erythrocytes. However, AQP3 expression has not been observed in mouse erythrocytes. Here we report ... Full text Link to item Cite

Aquaporin expression and freeze tolerance in Candida albicans.

Journal Article Appl Environ Microbiol · October 2005 Featured Publication Aquaporins are members of the major intrinsic protein superfamily of integral membrane proteins which enable the transport of water, glycerol, and other solutes across membranes in various organisms. In microorganisms, the physiological role of aquaporins ... Full text Link to item Cite

Drug uptake and pharmacological modulation of drug sensitivity in leukemia by AQP9.

Journal Article Biochem Biophys Res Commun · September 24, 2004 Featured Publication Leukemia is the most common childhood cancer. Trisenox, the active ingredient of which is trivalent arsenic, is the first line of treatment for acute promyelocytic leukemia. Since drug action usually requires uptake of the drug, it is of importance to dete ... Full text Link to item Cite

Arsenic trioxide uptake by human and rat aquaglyceroporins.

Journal Article Biochem Biophys Res Commun · April 16, 2004 Featured Publication Aquaglyceroporins are channels that allow downhill movement of uncharged solutes such as glycerol and urea. Arsenic trioxide has recently been shown to be translocated by mouse mAQP7 and rat rAQP9. In this study we examined the ability of the four known hu ... Full text Link to item Cite

A role for aquaporin-9 in metabolism

Conference FASEB JOURNAL · March 14, 2003 Link to item Cite

Aquaglyceroporin AQP9: solute permeation and metabolic control of expression in liver.

Journal Article Proc Natl Acad Sci U S A · March 4, 2003 Featured Publication Aquaglyceroporins form the subset of the aquaporin water channel family that is permeable to glycerol and certain small, uncharged solutes. AQP9 has unusually broad solute permeability and is expressed in hepatocyte plasma membranes. Proteoliposomes recons ... Full text Link to item Cite

Organization of carboxysome genes in the thiobacilli.

Journal Article Curr Microbiol · February 2003 The order of genes in the carboxysome gene clusters of four thiobacilli was examined and the possibility of the cluster forming an operon evaluated. Furthermore, carboxysome peptide homologs were compared with respect to similarities in primary sequence, a ... Full text Link to item Cite

Arsenite transport by mammalian aquaglyceroporins AQP7 and AQP9.

Journal Article Proc Natl Acad Sci U S A · April 30, 2002 Featured Publication Much is known about the transport of arsenite and antimonite into microbes, but the identities of mammalian transport proteins are unknown. The Saccharomyces cerevisiae FPS1 gene encodes a membrane protein homologous to the bacterial aquaglyceroporin GlpF ... Full text Link to item Cite

Aquaporin in Candida: characterization of a functional water channel protein.

Journal Article Yeast · November 2001 Featured Publication The Candida albicans genome database contains one ORF with homology to aquaporins, AQY1. Xenopus oocytes injected with cRNA encoding C. albicans Aqy1p displayed a coefficient of water permeability (P(f)) that was equivalent to the P(f) for oocytes injected ... Full text Link to item Cite

Aquaporins in Saccharomyces: Characterization of a second functional water channel protein.

Journal Article Proc Natl Acad Sci U S A · January 30, 2001 Featured Publication The Saccharomyces cerevisiae genome database contains two ORFs with homology to aquaporins, AQY1 and AQY2. Aqy1p has been shown to be a functional aquaporin in some strains, such as Sigma1278b. AQY2 is disrupted by a stop codon in most strains; however, Si ... Full text Link to item Cite

Functional analysis of a second aquaporin homolog from Saccharomyces cerevisiae

Journal Article MOLECULAR BIOLOGY OF THE CELL · November 1, 1999 Link to item Cite

Aquaporins in Saccharomyces. Genetic and functional distinctions between laboratory and wild-type strains.

Journal Article J Biol Chem · October 16, 1998 Featured Publication Aquaporin water channel proteins mediate the transport of water across cell membranes in numerous species. The Saccharomyces genome data base contains an open reading frame (here designated AQY1) that encodes a protein with strong homology to aquaporins. A ... Full text Link to item Cite

Sequence homologs of the carboxysomal polypeptide CsoS1 of the thiobacilli are present in cyanobacteria and enteric bacteria that form carboxysomes - Polyhedral bodies

Journal Article Canadian Journal of Botany · January 1, 1998 Carboxysomes containing the Calvin cycle enzyme ribulose-1,5-bisphosphate carboxylase-oxygenase (Rubisco) have been demonstrated in a variety of chemoautotrophic prokaryotes and cyanobacteria. The genes in the ccm and cso operon in Synechococcus sp. PCC794 ... Full text Cite

Functional analysis of an aquaporin homolog from Saccharomyces cerevisiae.

Journal Article MOLECULAR BIOLOGY OF THE CELL · November 1, 1997 Link to item Cite