Results 11 to 20 of about 225,633 (278)

Cytosolic chaperones influence the fate of a toxin dislocated from the endoplasmic reticulum [PDF]

open access: yes, 2008
The plant cytotoxin ricin enters target mammalian cells by receptor-mediated endocytosis and undergoes retrograde transport to the endoplasmic reticulum (ER).
R. A. Spooner   +32 more
core   +4 more sources

Molecular Chaperone Receptors [PDF]

open access: yes, 2017
Extracellular heat shock proteins (HSP) play important roles in cell signaling and immunity. Many of these effects are mediated by surface receptors expressed on a wide range of cell types. We have investigated the nature of such proteins by cloning candidate receptors into cells (CHO-K1) with the rare property of being null for HSP binding. Using this
Ayesha, Murshid   +3 more
openaire   +2 more sources

BAG5 Promotes Alpha-Synuclein Oligomer Formation and Functionally Interacts With the Autophagy Adaptor Protein p62

open access: yesFrontiers in Cell and Developmental Biology, 2020
Molecular chaperones are critical to maintaining intracellular proteostasis and have been shown to have a protective role against alpha-synuclein-mediated toxicity.
Erik L. Friesen   +21 more
doaj   +1 more source

Small heat-shock proteins: important players in regulating cellular proteostasis [PDF]

open access: yes, 2015
Small heat-shock proteins (sHsps) are a diverse family of intra-cellular molecular chaperone proteins that play a critical role in mitigating and preventing protein aggregation under stress conditions such as elevated temperature, oxidation and infection.
Carver, John A.   +3 more
core   +1 more source

Role of Subunit Exchange and Electrostatic Interactions on the Chaperone Activity of Mycobacterium leprae HSP18. [PDF]

open access: yesPLoS ONE, 2015
Mycobacterium leprae HSP18, a major immunodominant antigen of M. leprae pathogen, is a small heat shock protein. Previously, we reported that HSP18 is a molecular chaperone that prevents aggregation of different chemically and thermally stressed client ...
Sandip Kumar Nandi   +4 more
doaj   +1 more source

Structural Bioinformatics and Protein Docking Analysis of the Molecular Chaperone-Kinase Interactions: Towards Allosteric Inhibition of Protein Kinases by Targeting the Hsp90-Cdc37 Chaperone Machinery

open access: yesPharmaceuticals, 2013
A fundamental role of the Hsp90-Cdc37 chaperone system in mediating maturation of protein kinase clients and supporting kinase functional activity is essential for the integrity and viability of signaling pathways involved in cell cycle control and ...
Gennady Verkhivker   +3 more
doaj   +1 more source

αA-Crystallin-derived mini-chaperone modulates stability and function of cataract causing αAG98R-crystallin. [PDF]

open access: yesPLoS ONE, 2012
A substitution mutation in human αA-crystallin (αAG98R) is associated with autosomal dominant cataract. The recombinant mutant αAG98R protein exhibits altered structure, substrate-dependent chaperone activity, impaired oligomer stability and aggregation ...
Murugesan Raju   +2 more
doaj   +1 more source

Unraveling the molecular basis of subunit specificity in P pilus assembly by mass spectrometry [PDF]

open access: yes, 2008
P pili are multisubunit fibers essential for the attachment of uropathogenic Escherichia coli to the kidney. These fibers are formed by the noncovalent assembly of six different homologous subunit types in an array that is strictly defined in terms of ...
A. E. Ashcroft   +28 more
core   +2 more sources

Functions and Therapeutic Potential of Extracellular Hsp60, Hsp70, and Hsp90 in Neuroinflammatory Disorders

open access: yesApplied Sciences, 2021
Neuroinflammation is implicated in central nervous system (CNS) diseases, but the molecular mechanisms involved are poorly understood. Progress may be accelerated by developing a comprehensive view of the pathogenesis of CNS disorders, including the ...
Giusi Alberti   +7 more
doaj   +1 more source

Hsp70 in mitochondrial biogenesis [PDF]

open access: yes, 1994
The family of hsp70 (70 kilodalton heat shock protein) molecular chaperones plays an essential and diverse role in cellular physiology, Hsp70 proteins appear to elicit their effects by interacting with polypeptides that present domains which exhibit non ...
A. Tzagoloff   +53 more
core   +1 more source

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