Search Results - "Frydman, J"
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FOLDING OF NEWLY TRANSLATED PROTEINS IN VIVO: The Role of Molecular Chaperones
Published in Annual review of biochemistry (01-01-2001)“…Recent years have witnessed dramatic advances in our understanding of how newly translated proteins fold in the cell and the contribution of molecular…”
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Pancreatic β-cell death in response to pro-inflammatory cytokines is distinct from genuine apoptosis
Published in PloS one (2011)“…A reduction in functional β-cell mass leads to both major forms of diabetes; pro-inflammatory cytokines, such as interleukin-1beta (IL-1β) and gamma-interferon…”
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Molecular chaperones and the art of recognizing a lost cause
Published in Nature cell biology (01-02-2001)“…Molecular chaperones have long been heralded as machines for folding and salvaging proteins. However, not every attempt to fold or refold a protein can be…”
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Cinnamomum zeylanicum extract on the radiolabelling of blood constituents and the morphometry of red blood cells: In vitro assay
Published in Applied radiation and isotopes (01-02-2008)“…Effects of Cinnamomum zeylanicum (cinnamon) on the labelling of blood constituents with technetium-99 m( 99mTc) and on the morphology of red blood cells were…”
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Function in protein folding of TRiC, a cytosolic ring complex containing TCP‐1 and structurally related subunits
Published in The EMBO journal (01-12-1992)“…T‐complex polypeptide 1 (TCP‐1) was analyzed as a potential chaperonin (GroEL/Hsp60) equivalent of the eukaryotic cytosol. We found TCP‐1 to be part of a…”
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Sucralose sweetener in vivo effects on blood constituents radiolabeling, red blood cell morphology and radiopharmaceutical biodistribution in rats
Published in Applied radiation and isotopes (2011)“…Effects of sucralose sweetener on blood constituents labelled with technetium-99m ( 99mTc) on red blood cell (RBC) morphology, sodium pertechnetate (Na 99mTcO…”
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Activities of DL-α-Difluoromethylarginine and Polyamine Analogues against Cryptosporidium parvum Infection in a T-Cell Receptor Alpha-Deficient Mouse Model
Published in Antimicrobial Agents and Chemotherapy (01-04-2007)“…The in vivo effectiveness of a series of conformationally restricted polyamine analogues alone and selected members in combination with…”
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Cellular strategies of protein quality control
Published in Cold Spring Harbor perspectives in biology (01-08-2011)“…Eukaryotic cells must contend with a continuous stream of misfolded proteins that compromise the cellular protein homeostasis balance and jeopardize cell…”
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Purification of the cytosolic chaperonin TRiC from bovine testis
Published in Methods in molecular biology (Clifton, N.J.) (2000)Get more information
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AGING-LINKED PROTEOSTASIS DECLINE: IMPLICATIONS FOR NEURODEGENERATIVE DISEASE
Published in Innovation in aging (01-07-2017)“…Chaperones help proteins fold or send them to degradation, but they also regulate conformational protein cycles, protein-protein interactions, transcriptional…”
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Suppression and Regression of Choroidal Neovascularization by Polyamine Analogues
Published in Investigative ophthalmology & visual science (01-09-2005)“…Polyamine analogues inhibit tumor growth in vitro and in vivo, and oligoamines with a chain length of 10, 12, or 14 are particularly potent. This study was…”
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Diverse Cellular Functions of the Hsp90 Molecular Chaperone Uncovered Using Systems Approaches
Published in Cell (05-10-2007)“…A comprehensive understanding of the cellular functions of the Hsp90 molecular chaperone has remained elusive. Although Hsp90 is essential, highly abundant…”
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Systems Analyses Reveal Two Chaperone Networks with Distinct Functions in Eukaryotic Cells
Published in Cell (13-01-2006)“…Molecular chaperones assist the folding of newly translated and stress-denatured proteins. In prokaryotes, overlapping sets of chaperones mediate both…”
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Mechanism of the eukaryotic chaperonin: protein folding in the chamber of secrets
Published in Trends in cell biology (01-11-2004)“…Chaperonins are key components of the cellular chaperone machinery. These large, cylindrical complexes contain a central cavity that binds to unfolded…”
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Protein quality control: chaperones culling corrupt conformations
Published in Nature cell biology (01-08-2005)“…Achieving the correct balance between folding and degradation of misfolded proteins is critical for cell viability. The importance of defining the mechanisms…”
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Folding and Quality Control of the VHL Tumor Suppressor Proceed through Distinct Chaperone Pathways
Published in Cell (03-06-2005)“…The mechanisms by which molecular chaperones assist quality control of cytosolic proteins are poorly understood. Analysis of the chaperone requirements for…”
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Acetylsalicylic acid decreases the labeling of blood constituents with technetium-99M
Published in Acta biologica Hungarica (01-06-2007)“…Acetylsalicylic acid is the most widely used drug as antipyretic, analgesic, anti-inflammatory agent and for secondary prevention of thrombotic phenomena in…”
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An ATP-Stabilized Inhibitor of the Proteasome is a Component of the 1500-kDa Ubiquitin Conjugate-Degrading Complex
Published in Proceedings of the National Academy of Sciences - PNAS (01-06-1992)“…Proteins conjugated to ubiquitin are degraded by a 26S (1500-kDa) proteolytic complex that, in reticulocyte extracts, can be formed by the association of three…”
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The Predicted Structure of the Headpiece of the Huntingtin Protein and Its Implications on Huntingtin Aggregation
Published in Journal of molecular biology (22-05-2009)“…We have performed simulated tempering molecular dynamics simulations to study the thermodynamics of the headpiece of the Huntingtin (Htt) protein (N17 Htt)…”
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