PMID- 10542082
OWN - NLM
STAT- MEDLINE
DCOM- 20020618
LR  - 20081121
IS  - 1072-8368 (Print)
IS  - 1072-8368 (Linking)
VI  - 6
IP  - 11
DP  - 1999 Nov
TI  - A chaperone with a hydrophilic surface.
PG  - 990-1
AB  - The folding of native tubulin involves at least seven different chaperone
      proteins: prefoldin, the cytosolic chaperonin CCT and five tubulin-specific
      chaperone proteins named cofactors A-E. The structure of the yeast homolog of
      cofactor A, Rbl2p, shows it to be a dimer with largely hydrophilic surfaces,
      reflecting the fact that it interacts with quasi-native, not unfolded,
      beta-tubulin.
FAU - Cowan, N J
AU  - Cowan NJ
AD  - Department of Biochemistry, New York University Medical Center, 550 First Avenue,
      New York, New York 10016, USA. cowann01@mcrcr.med.nyu.edu
FAU - Lewis, S A
AU  - Lewis SA
LA  - eng
PT  - Comment
PT  - News
PL  - United States
TA  - Nat Struct Biol
JT  - Nature structural biology
JID - 9421566
RN  - 0 (Microtubule-Associated Proteins)
RN  - 0 (Molecular Chaperones)
RN  - 0 (RBL2 protein, S cerevisiae)
RN  - 0 (Saccharomyces cerevisiae Proteins)
RN  - 0 (Tubulin)
SB  - IM
CON - Nat Struct Biol. 1999 Nov;6(11):1029-32. PMID: 10542094
MH  - Animals
MH  - Microtubule-Associated Proteins/*chemistry/*metabolism
MH  - Models, Biological
MH  - Molecular Chaperones/*chemistry/*metabolism
MH  - Protein Binding
MH  - *Protein Folding
MH  - Protein Structure, Quaternary
MH  - Saccharomyces cerevisiae Proteins/*chemistry/*metabolism
MH  - Static Electricity
MH  - Tubulin/*chemistry/*metabolism
EDAT- 1999/12/14 09:00
MHDA- 2002/06/19 10:01
CRDT- 1999/12/14 09:00
PHST- 1999/12/14 09:00 [pubmed]
PHST- 2002/06/19 10:01 [medline]
PHST- 1999/12/14 09:00 [entrez]
AID - 10.1038/14870 [doi]
PST - ppublish
SO  - Nat Struct Biol. 1999 Nov;6(11):990-1. doi: 10.1038/14870.