Results 31 to 40 of about 94,343 (283)
The discovery of SycO reveals a new function for type three secretion effector chaperones [PDF]
, 2006 The Type Three Secretion (T3S) system is a device used by many Gram-negative pathogens that allows bacteria to deliver effector proteins straight into the eukaryotic cell cytosol.
Letzelter, Michel
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Molecular chaperone genes in the sugarcane expressed sequence database (SUCEST)
Genetics and Molecular Biology, 2001 Some newly synthesized proteins require the assistance of molecular chaperones for their correct folding. Chaperones are also involved in the dissolution of protein aggregates making their study significant for both biotechnology and medicine and the ...
Júlio C. Borges +2 more
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Molecular chaperones and photoreceptor function [PDF]
, 2008 Molecular chaperones facilitate and regulate protein conformational change within cells. This encompasses many fundamental cellular processes: including the correct folding of nascent chains; protein transport and translocation; signal transduction and ...
Cheetham, Michael E. +7 more
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F1000Research, 2015 Proteins must adopt a defined three-dimensional structure in order to gain functional activity, or must they? An ever-increasing number of intrinsically disordered proteins and amyloid-forming polypeptides challenge this dogma. While molecular chaperones
Wilson Jeng +4 more
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Life, 2020 The property of molecular chaperones to dissolve protein aggregates of Parkinson-related α-synuclein has been known for some time. Recent findings point to an even more active role of molecular chaperones preventing the transformation of α-synuclein into
Emelie E. Aspholm +2 more
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Malaria Journal, 2010 Background Molecular chaperones have been shown to be important in the growth of the malaria parasite Plasmodium falciparum and inhibition of chaperone function by pharmacological agents has been shown to abrogate parasite growth.
Pallavi Rani +4 more
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Molecular chaperones and their denaturing effect on client proteins [PDF]
, 2021 Advanced NMR methods combined with biophysical techniques have recently provided unprecedented insight into structure and dynamics of molecular chaperones and their interaction with client proteins.
Hiller, Sebastian
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Emerging roles of J proteins in neurodegenerative disorders
Neurobiology of Disease, 2008 Several families of proteins called molecular chaperones comprise the cellular machinery that has evolved to maintain protein structure and eliminate misfolded proteins in the cell. In experimental animal models, chaperones have been shown to be powerful
Sarah J. Gibbs, Janice E.A. Braun
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RNA can function as molecular chaperone for RNA folding
Giant, 2020 RNAs can mimic the information storage, replication and catalysis functions of DNAs and proteins, providing physical evidence for the widely accepted RNA world hypothesis that RNA alone constitutes earlier life forms.
Zhi-Chao Lei +8 more
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Molecular Chaperones and Neurodegeneration [PDF]
, 2017 Molecular chaperones or heat-shock proteins (HSPs) play essential roles in safeguarding structural stability and preventing misfolding and aggregation of proteins, and maintaining the proteome functionality in the cell.
Cintia Roodveldt +2 more
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