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 …

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 …

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 …

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 …

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 …

Inhibition of nuclear protein import by nonhydrolyzable analogues of GTP and identification of the small GTPase Ran/TC4 as an essential transport factor.

F Melchior, B Paschal, J Evans, L Gerace - The Journal of cell biology, 1993 - rupress.org
We have investigated a possible involvement of GTPases in nuclear protein import using an
in vitro transport system involving digitonin-permeabilized cells supplemented with …

Role of hsp90 and the hsp90-binding immunophilins in signalling protein movement

WB Pratt, MD Galigniana, JM Harrell, DB DeFranco - Cellular signalling, 2004 - Elsevier
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 …

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 …

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 …

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 …