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- Publications
- Influence
Identification, purification, and partial characterization of a novel Mr 28,000 integral membrane protein from erythrocytes and renal tubules.
- B. Denker, B. Smith, F. Kuhajda, P. Agre
- Medicine, Biology
- The Journal of biological chemistry
- 25 October 1988
A novel Mr 28,000 integral membrane protein ("28kDa") was identified in human erythrocytes and found entirely associated with the Triton X-100 insoluble membrane skeletons. Antibodies to 28kDa… Expand
α-Actinin-4-Mediated FSGS: An Inherited Kidney Disease Caused by an Aggregated and Rapidly Degraded Cytoskeletal Protein
Focal segmental glomerulosclerosis (FSGS) is a common pattern of renal injury, seen as both a primary disorder and as a consequence of underlying insults such as diabetes, HIV infection, and… Expand
Zonula Occludens-1 Is a Scaffolding Protein for Signaling Molecules
- T. Meyer, C. Schwesinger, B. Denker
- Biology, Medicine
- The Journal of Biological Chemistry
- 12 July 2002
Zonula occludens proteins are multidomain proteins usually localized at sites of intercellular junctions, yet little is known about their role in regulating junctional properties. Multiple signaling… Expand
Primary Care Management of Chronic Kidney Disease
- Adrienne S. Allen, J. Forman, E. Orav, D. Bates, B. Denker, T. Sequist
- Medicine
- Journal of General Internal Medicine
- 1 April 2011
BackgroundChronic kidney disease (CKD) causes substantial morbidity and mortality; however, there are limited data to comprehensively assess quality of care in this area.ObjectiveTo assess quality of… Expand
Disease-associated mutant α-actinin-4 reveals a mechanism for regulating its F-actin-binding affinity
- A. Weins, J. Schlondorff, +4 authors M. Pollak
- Biology, Medicine
- Proceedings of the National Academy of Sciences
- 9 October 2007
α-Actinin-4 is a widely expressed protein that employs an actin-binding site with two calponin homology domains to crosslink actin filaments (F-actin) in a Ca2+-sensitive manner in vitro. An… Expand
Renal Pathophysiology: The Essentials
This text offers medical students a case-based approach to learning the mechanisms of renal disease. Each chapter covers a disease, beginning with a patient case and followed by a discussion of the… Expand
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Molecular structure and assembly of the tight junction.
Polarized epithelial cells separate two extremely different cellular milieus. The tight junction (TJ) is the most apical component of the junctional complex and serves as the permeability barrier… Expand
Reassembly of the Tight Junction after Oxidative Stress Depends on Tyrosine Kinase Activity*
- T. Meyer, C. Schwesinger, J. Ye, B. Denker, S. Nigam
- Medicine, Biology
- The Journal of Biological Chemistry
- 22 June 2001
Oxidative stress compromises the tight junction, but the mechanisms underlying its recovery remain unclear. We developed a model in which oxidative stress reversibly disrupts the tight junction.… Expand
Molecular structure and assembly of the tight junction.
Polarized epithelial cells separate two extremely different cellular milieus. The tight junction (TJ) is the most apical component of the junctional complex and serves as the permeability barrier… Expand
H2O2 activates G protein, α 12 to disrupt the junctional complex and enhance ischemia reperfusion injury
- Wanfeng Yu, S. Beaudry, +4 authors B. Denker
- Biology, Medicine
- Proceedings of the National Academy of Sciences
- 9 April 2012
The epithelial cell tight junction separates apical and basolateral domains and is essential for barrier function. Disruption of the tight junction is a hallmark of epithelial cell damage and can… Expand