Chemistry Reference
In-Depth Information
Alberti S, Esser C, H￶hfeld J (2003) BAG-1- a nucleotide exchange factor of Hsc70 with multiple
cellular functions. Cell Stress Chaperones 8:225-231
Alberti S, Bohse K, Arndt V, Schmitz A, H￶hfeld J (2004) The co-chaperone HspBP1 inhibits
the CHIP ubiquitin ligase and stimulates the maturation of the cystic fibrosis transmembrane
conductance regulator. Mol Biol Cell 15:4003-4010
Andreasson C, Fiaux J, Rampelt H, Mayer MP, Bukau B (2008) Hsp110 is a nucleotide-activated
exchange factor for Hsp70. J Biol Chem 283:8877-8884
Andreasson C, Rampelt H, Fiaux J, Druffel-Augustin S, Bukau B (2010) The endoplasmic reticu-
lum Grp170 acts as a nucleotide exchange factor of Hsp70 via a mechanism similar to that of
the cytosolic Hsp110. J Biol Chem 285:12445-12453
Ang D, Georgopoulos C (1989) The heat-shock-regulated grpE gene of Escherichia coli is required
for bacterial growth at all temperatures but is dispensable in certain mutant backgrounds. J
Bacteriol 171:2748-2755
Antoku K, Maser RS, Scully WJ Jr, Delach SM, Johnson DE (2001) Isolation of Bcl-2 binding
proteins that exhibit homology with BAG-1 and suppressor of death domains protein. Biochem
Biophys Res Commun 286:1003-1010
Anttonen AK, Mahjneh I, Hamalainen RH, Lagier-Tourenne C, Kopra O, Waris L, Anttonen M,
Joensuu T, Kalimo H, Paetau A, Tranebjaerg L, Chaigne D, Koenig M, Eeg-Olofsson O, Udd
B, Somer M, Somer H, Lehesjoki AE (2005) The gene disrupted in Marinesco-Sjogren syn-
drome encodes SIL1, an HSPA5 cochaperone. Nat Genet 37:1309-1311
Arakawa A, Handa N, Ohsawa N, Shida M, Kigawa T, Hayashi F, Shirouzu M, Yokoyama S
(2010) The C-terminal BAG domain of BAG5 induces conformational changes of the Hsp70
nucleotide-binding domain for ADP-ATP exchange. Structure 18:309-319
Arakawa A, Handa N, Shirouzu M, Yokoyama S (2011) Biochemical and structural studies on the
high affinity of Hsp70 for ADP. Protein Sci 20:1367-1379
Arndt V, Daniel C, Nastainczyk W, Alberti S, H￶hfeld J (2005) BAG-2 acts as an inhibitor of the
chaperone-associated ubiquitin ligase CHIP. Mol Biol Cell 16:5891-5900
Arndt V, Dick N, Tawo R, Dreiseidler M, Wenzel D, Hesse M, Frst DO, Saftig P, Saint R, Fleis-
chmann BK, Hoch M, H￶hfeld J (2010) Chaperone-assisted selective autophagy is essential for
muscle maintenance. Curr Biol 20:143-148
Balch WE, Morimoto RI, Dillin A, Kelly JW (2008) Adapting proteostasis for disease interven-
tion. Science 319:916-919
Bertelsen EB, Chang L, Gestwicki JE, Zuiderweg ER (2009) Solution conformation of wild-type
E. coli Hsp70 (DnaK) chaperone complexed with ADP and substrate. Proc Natl Acad Sci U S
A 106:8471-8476
Bimston D, Song J, Winchester D, Takayama S, Reed JC, Morimoto RI (1998) BAG-1, a negative
regulator of Hsp70 chaperone activity, uncouples nucleotide hydrolysis from substrate release.
EMBO J 17:6871-6878
Binici J, Koch J (2013) BAG-6, a jack of all trades in health and disease. Cell Mol Life Sci.
doi:10.1007/s00018-013-1522-y
Brehmer D, Rdiger S, G¦ssler CS, Klostermeier D, Packschies L, Reinstein J, Mayer MP, Bukau
B (2001) Tuning of chaperone activity of Hsp70 proteins by modulation of nucleotide ex-
change. Nat Struct Biol 8:427-432
Briknarova K, Takayama S, Brive L, Havert ML, Knee DA, Velasco J, Homma S, Cabezas E,
Stuart J, Hoyt DW, Satterthwait AC, Llinas M, Reed JC, Ely KR (2001) Structural analysis
of BAG1 cochaperone and its interactions with Hsc70 heat shock protein. Nat Struct Biol
8:349-352
Briknarova K, Takayama S, Homma S, Baker K, Cabezas E, Hoyt DW, Li Z, Satterthwait AC, Ely
KR (2002) BAG4/SODD protein contains a short BAG domain. J Biol Chem 277:31172-31178
Brockmann C, Leitner D, Labudde D, Diehl A, Sievert V, Bssow K, Khne R, Oschkinat H
(2004) The solution structure of the SODD BAG domain reveals additional electrostatic inter-
actions in the HSP70 complexes of SODD subfamily BAG domains. FEBS Lett 558:101-106
Brodsky JL, Bracher A (2007) Nucleotide Exchange Factors for Hsp70 Molecular Chaperones. In:
Balch GL (ed) Networking of chaperones by co-chaperones. Molecular Biology Intelligence
Unit. Landes Biosciences, Austin, pp 1-12
Search WWH ::




Custom Search