HSPA8/HSC70 chaperone protein: structure, function, and chemical targeting
F Stricher, C Macri, M Ruff, S Muller - Autophagy, 2013 - Taylor & Francis
HSPA8/HSC70 protein is a fascinating chaperone protein. It represents a constitutively
expressed, cognate protein of the HSP70 family, which is central in many cellular processes …
expressed, cognate protein of the HSP70 family, which is central in many cellular processes …
Nucleocytoplasmic transport: the soluble phase
IW Mattaj, L Englmeier - Annual review of biochemistry, 1998 - annualreviews.org
Active transport between the nucleus and cytoplasm involves primarily three classes of
macromolecules: substrates, adaptors, and receptors. Some transport substrates bind …
macromolecules: substrates, adaptors, and receptors. Some transport substrates bind …
Heat‐shock proteins as molecular chaperones
J Becker, EA Craig - European Journal of Biochemistry, 1994 - Wiley Online Library
Functional proteins within cells are normally present in their native, completely folded form.
However, vital processes of protein biogenesis such as protein synthesis and translocation …
However, vital processes of protein biogenesis such as protein synthesis and translocation …
Comprehensive review on the HSC70 functions, interactions with related molecules and involvement in clinical diseases and therapeutic potential
T Liu, CK Daniels, S Cao - Pharmacology & therapeutics, 2012 - Elsevier
Heat shock cognate protein 70 (HSC70) is a constitutively expressed molecular chaperone
which belongs to the heat shock protein 70 (HSP70) family. HSC70 shares some of the …
which belongs to the heat shock protein 70 (HSP70) family. HSC70 shares some of the …
The GTP-binding protein Ran/TC4 is required for protein import into the nucleus
MS Moore, G Blobel - Nature, 1993 - nature.com
TWO cytosolic fractions (A and B) from Xenopus oocytes are sufficient to support protein
import into the nuclei of digitonin-permeabilized cells1. Fraction A recognizes the nuclear …
import into the nuclei of digitonin-permeabilized cells1. Fraction A recognizes the nuclear …
Inhibition of nuclear protein import by nonhydrolyzable analogues of GTP and identification of the small GTPase Ran/TC4 as an essential transport factor.
We have investigated a possible involvement of GTPases in nuclear protein import using an
in vitro transport system involving digitonin-permeabilized cells supplemented with …
in vitro transport system involving digitonin-permeabilized cells supplemented with …
Role of hsp90 and the hsp90-binding immunophilins in signalling protein movement
The ubiquitous protein chaperone hsp90 has been shown to regulate more than 100
proteins involved in cellular signalling. These proteins are called 'client proteins' for hsp90 …
proteins involved in cellular signalling. These proteins are called 'client proteins' for hsp90 …
Essential role of voltage-dependent anion channel in various forms of apoptosis in mammalian cells
S Shimizu, Y Matsuoka, Y Shinohara… - The Journal of cell …, 2001 - rupress.org
Through direct interaction with the voltage-dependent anion channel (VDAC), proapoptotic
members of the Bcl-2 family such as Bax and Bak induce apoptogenic cytochrome c release …
members of the Bcl-2 family such as Bax and Bak induce apoptogenic cytochrome c release …
Regulation of protein transport to the nucleus: central role of phosphorylation
DA Jans, S Hubner - Physiological reviews, 1996 - journals.physiology.org
Nuclear protein transport is integral to eukaryotic cell processes such as differentiation,
transformation, and the control of gene expression. Although the targeting role of nuclear …
transformation, and the control of gene expression. Although the targeting role of nuclear …
Chaperones in cell cycle regulation and mitogenic signal transduction: a review
K Helmbrecht, E Zeise, L Rensing - Cell proliferation, 2000 - Wiley Online Library
Chaperones/heat shock proteins (HSPs) of the HSP90 and HSP70 families show elevated
levels in proliferating mammalian cells and a cell cycle‐dependent expression. They …
levels in proliferating mammalian cells and a cell cycle‐dependent expression. They …