Chemistry Reference
In-Depth Information
Kuo Y, Ren S, Lao U, Edgar BA, Wang T (2013) Suppression of polyglutamine protein toxicity by
co-expression of a heat-shock protein 40 and a heat-shock protein 110. Cell Death Dis 4:e833
Kwon KR, Ahn JY, Kim MS, Jung JY, Lee JH, Oh IH (2010) Disruption of bis leads to the deterio-
ration of the vascular niche for hematopoietic stem cells. Stem Cells 28:268-278
Laloraya S, Gambill BD, Craig EA (1994) A role for a eukaryotic GrpE-related protein, Mge1p, in
protein translocation. Proc Natl Acad Sci U S A 91:6481-6485
Laloraya S, Dekker PJ, Voos W, Craig EA, Pfanner N (1995) Mitochondrial GrpE modulates
the function of matrix Hsp70 in translocation and maturation of preproteins. Mol Cell Biol
15:7098-7105
Lamark T, Johansen T (2012) Aggrephagy: selective disposal of protein aggregates by macroau-
tophagy. Int J Cell Biol. doi:10.1155/2012/736905
Laufen T, Mayer MP, Beisel C, Klostermeier D, Mogk A, Reinstein J, Bukau B (1999) Mecha-
nism of regulation of hsp70 chaperones by DnaJ cochaperones. Proc Natl Acad Sci U S A
96:5452-5457
Li Z, Hartl FU, Bracher A (2013) Structure and function of Hip, an attenuator of the Hsp70 chap-
erone cycle. Nat Struct Mol Biol 20:929-935
Lin J, Hutchinson L, Gaston SM, Raab G, Freeman MR (2001) BAG-1 is a novel cytoplasmic
binding partner of the membrane form of heparin-binding EGF-like growth factor: a unique
role for proHB-EGF in cell survival regulation. J Biol Chem 276:30127-30132
Liu Q, Hendrickson WA (2007) Insights into Hsp70 chaperone activity from a crystal structure of
the yeast Hsp110 Sse1. Cell 131:106-120
Liu XD, Morano KA, Thiele DJ (1999) The yeast Hsp110 family member, Sse1, is an Hsp90 co-
chaperone. J Biol Chem 274:26654-26660
Liu Y, Gierasch LM, Bahar I (2010) Role of Hsp70 ATPase domain intrinsic dynamics and se-
quence evolution in enabling its functional interactions with NEFs. PLoS Comput Biol 6.
doi:10.1371/journal.pcbi.1000931
Makhnevych T, Wong P, Pogoutse O, Vizeacoumar FJ, Greenblatt JF, Emili A, Houry WA (2012)
Hsp110 is required for spindle length control. J Cell Biol 198:623-636
Mandal AK, Gibney PA, Nillegoda NB, Theodoraki MA, Caplan AJ, Morano KA (2010) Hsp110
chaperones control client fate determination in the hsp70-Hsp90 chaperone system. Mol Biol
Cell 21:1439-1448
Marada A, Allu PK, Murari A, PullaReddy B, Tammineni P, Thiriveedi VR, Danduprolu J, Sepuri
NB (2013) Mge1, a nucleotide exchange factor of Hsp70, acts as an oxidative sensor to regu-
late mitochondrial Hsp70 function. Mol Biol Cell 24:692-703
Mariappan M, Li X, Stefanovic S, Sharma A, Mateja A, Keenan RJ, Hegde RS (2010) A ribosome-
associating factor chaperones tail-anchored membrane proteins. Nature 466:1120-1124
Masison DC, Kirkland PA, Sharma D (2009) Influence of Hsp70s and their regulators on yeast
prion propagation. Prion 3:65-73
Mattoo RU, Sharma SK, Priya S, Finka A, Goloubinoff P (2013) Hsp110 is a bona fide chaperone
using ATP to unfold stable misfolded polypeptides and reciprocally collaborate with Hsp70 to
solubilize protein aggregates. J Biol Chem 288:21399-21411
Mayer MP, Bukau B (2005) Hsp70 chaperones: cellular functions and molecular mechanism. Cell
Mol Life Sci 62:670-684
McClellan AJ, Scott MD, Frydman J (2005) Folding and quality control of the VHL tumor sup-
pressor proceed through distinct chaperone pathways. Cell 121:739-748
Meacham GC, Patterson C, Zhang W, Younger JM, Cyr DM (2001) The Hsc70 co-chaperone
CHIP targets immature CFTR for proteasomal degradation. Nat Cell Biol 3:100-105
Miao B, Davis JE, Craig EA (1997) Mge1 functions as a nucleotide release factor for Ssc1, a mi-
tochondrial Hsp70 of Saccharomyces cerevisiae. J Mol Biol 265:541-552
Mohamed BA, Barakat AZ, Held T, Elkenani M, Muhlfeld C, Manner J, Adham IM (2014) Respi-
ratory distress and early neonatal lethality in hspa4 l/hspa4 double-mutant mice. Am J Respir
Cell Mol Biol 50:817-824
Mokranjac D, Bourenkov G, Hell K, Neupert W, Groll M (2006) Structure and function of Tim14
and Tim16, the J and J-like components of the mitochondrial protein import motor. EMBO J
25:4675-4685
Search WWH ::




Custom Search