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FRISC: The Faculty Research Interests Science Comparator
David T. Chuang, Ph.D.
Associate Professor of Biochemistry
Biological Chemistry
Office: (214) 648-2457
FAX: (214) 648-8856
Email: chuang01@utsw.swmed.edu
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Results - FULL MEDLINE:
Encapsulation of an 86-kDa assembly intermediate inside the cavities of GroEL and its single-ring variant SR1 by GroES.
Jiu-Li Song ... David T Chuang
J Biol Chem 2003 Jan; 278(4)2515-21.
Score: 0.755
Maple syrup urine disease: it has come a long way.
D T Chuang
J Pediatr 1998 Mar; 132(3 Pt 2)S17-23.
Score: 0.736
GroEL/GroES promote dissociation/reassociation cycles of a heterodimeric intermediate during alpha(2)beta(2) protein assembly. Iterative annealing at the quaternary structure level.
R M Wynn ... D T Chuang
J Biol Chem 2000 Jan; 275(4)2786-94.
Score: 0.726
Natural osmolyte trimethylamine N-oxide corrects assembly defects of mutant branched-chain alpha-ketoacid decarboxylase in maple syrup urine disease.
J L Song ... D T Chuang
J Biol Chem 2001 Oct; 276(43)40241-6.
Score: 0.712
Molecular chaperones in cellular protein folding.
F U Hartl ... J Martin
Curr Opin Struct Biol 1995 Feb; 5(1)92-102.
Score: 0.563
Protein folding assisted by the GroEL/GroES chaperonin system.
J Martin
Biochemistry (Mosc) 1998 Apr; 63(4)374-81.
Score: 0.556
Putting a lid on protein folding: structure and function of the co-chaperonin, GroES.
W A Fenton ... A L Horwich
Chem Biol 1996 Mar; 3(3)157-61.
Score: 0.536
Human mutations affecting branched chain alpha-ketoacid dehydrogenase.
D J Danner ... C B Doering
Front Biosci 1998 Jun; 3()d517-24.
Score: 0.526
Role of the chaperonin cofactor Hsp10 in protein folding and sorting in yeast mitochondria.
J Höhfeld ... F U Hartl
J Cell Biol 1994 Jul; 126(2)305-15.
Score: 0.525
Molecular basis of maple syrup urine disease and stable correction by retroviral gene transfer.
D T Chuang ... R P Cox
J Nutr 1995 Jun; 125(6 Suppl)1766S-1772S.
Score: 0.524
Maple syrup urine disease: domain structure, mutations and exon skipping in the dihydrolipoyl transacylase (E2) component of the branched-chain alpha-keto acid dehydrogenase complex.
D T Chuang ... R P Cox
Mol Biol Med 1991 Feb; 8(1)49-63.
Score: 0.513
Interactions of GroEL/GroES with a heterodimeric intermediate during alpha 2beta 2 assembly of mitochondrial branched-chain alpha-ketoacid dehydrogenase. cis capping of the native-like 86-kDa intermediate by GroES.
J L Song ... D T Chuang
J Biol Chem 2000 Jul; 275(29)22305-12.
Score: 0.512
Procollagen folding and assembly: the role of endoplasmic reticulum enzymes and molecular chaperones.
S R Lamandé ... J F Bateman
Semin Cell Dev Biol 1999 Oct; 10(5)455-64.
Score: 0.502
Dual function of protein confinement in chaperonin-assisted protein folding.
A Brinker ... M Hayer-Hartl
Cell 2001 Oct; 107(2)223-33.
Score: 0.500
Molecular roles of chaperones in assisted folding and assembly of proteins.
Mark T Fisher
Genet Eng (N Y) 2006 ; 27()191-229.
Score: 0.498
GroE chaperonin-assisted folding and assembly of dodecameric glutamine synthetase.
M T Fisher
Biochemistry (Mosc) 1998 Apr; 63(4)382-98.
Score: 0.495
Chaperonin assisted polypeptide folding and assembly: implications for the production of functional proteins in bacteria.
A A Gatenby ... G H Lorimer
Trends Biotechnol 1990 Dec; 8(12)354-8.
Score: 0.492
The oligomeric structure of GroEL/GroES is required for biologically significant chaperonin function in protein folding.
F Weber ... F U Hartl
Nat Struct Biol 1998 Nov; 5(11)977-85.
Score: 0.492
Molecular chaperones in cellular protein folding.
F U Hartl
Nature 1996 Jun; 381(6583)571-9.
Score: 0.491
Molecular chaperones in protein folding: the art of avoiding sticky situations.
F U Hartl ... T Langer
Trends Biochem Sci 1994 Jan; 19(1)20-5.
Score: 0.491
The effect of macromolecular crowding on chaperonin-mediated protein folding.
J Martin ... F U Hartl
Proc Natl Acad Sci U S A 1997 Feb; 94(4)1107-12.
Score: 0.490
Roles of active site and novel K+ ion-binding site residues in human mitochondrial branched-chain alpha-ketoacid decarboxylase/dehydrogenase.
R M Wynn ... D T Chuang
J Biol Chem 2001 Feb; 276(6)4168-74.
Score: 0.490
Folding and assembly of the Escherichia coli succinyl-CoA synthetase heterotetramer without participation of molecular chaperones.
G Fong ... W A Bridger
Biochemistry 1992 Jun; 31(24)5661-4.
Score: 0.489
Tetrameric assembly and conservation in the ATP-binding domain of rat branched-chain alpha-ketoacid dehydrogenase kinase.
R M Wynn ... D T Chuang
J Biol Chem 2000 Sep; 275(39)30512-9.
Score: 0.485
Chaperone-assisted protein folding.
J Martin ... F U Hartl
Curr Opin Struct Biol 1997 Feb; 7(1)41-52.
Score: 0.485
Controlled overexpression of BCKD kinase expression: metabolic engineering applied to BCAA metabolism in a mammalian system.
C B Doering ... D J Danner
Metab Eng 2000 Oct; 2(4)349-56.
Score: 0.484
The molecular chaperone concept.
R J Ellis
Semin Cell Biol 1990 Feb; 1(1)1-9.
Score: 0.482
On the role of groES in the chaperonin-assisted folding reaction. Three case studies.
M Schmidt ... P V Viitanen
J Biol Chem 1994 Apr; 269(14)10304-11.
Score: 0.482
The function of chaperones during intracellular protein sorting, folding and assembly.
J Ostermann
Biotechnol Genet Eng Rev 1990 ; 8()219-49.
Score: 0.481
Chaperones in bacteriophage T4 assembly.
E I Marusich ... V V Mesyanzhinov
Biochemistry (Mosc) 1998 Apr; 63(4)399-406.
Score: 0.480
Protein folding. Chaperonin duet.
R J Ellis
Nature 1993 Nov; 366(6452)213-4.
Score: 0.479
Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones.
J Frydman ... F U Hartl
Nature 1994 Jul; 370(6485)111-7.
Score: 0.478
Substrate mutations that bypass a specific Cpn10 chaperonin requirement for protein folding.
J D Andreadis ... L W Black
J Biol Chem 1998 Dec; 273(51)34075-86.
Score: 0.471
The plastid chaperonin.
S M Hemmingsen
Semin Cell Biol 1990 Feb; 1(1)47-54.
Score: 0.470
Insulin increases branched-chain alpha-ketoacid dehydrogenase kinase expression in Clone 9 rat cells.
Mary M Nellis ... Dean J Danner
Am J Physiol Endocrinol Metab 2002 Oct; 283(4)E853-60.
Score: 0.466
Biochemical basis of type IB (E1beta ) mutations in maple syrup urine disease. A prevalent allele in patients from the Druze kindred in Israel.
R M Wynn ... D T Chuang
J Biol Chem 2001 Sep; 276(39)36550-6.
Score: 0.464
Chemical synthesis of 10 kDa chaperonin. Biological activity suggests chaperonins do not require other molecular chaperones.
P Mascagni ... A Coates
FEBS Lett 1991 Jul; 286(1-2)201-3.
Score: 0.456
A single ring is sufficient for productive chaperonin-mediated folding in vivo.
K L Nielsen ... N J Cowan
Mol Cell 1998 Jul; 2(1)93-9.
Score: 0.456
Characterization of the active intermediate of a GroEL-GroES-mediated protein folding reaction.
J S Weissman ... A L Horwich
Cell 1996 Feb; 84(3)481-90.
Score: 0.455
The chaperonin containing t-complex polypeptide 1 (TCP-1). Multisubunit machinery assisting in protein folding and assembly in the eukaryotic cytosol.
H Kubota ... K Willison
Eur J Biochem 1995 May; 230(1)3-16.
Score: 0.455
Proteome-wide analysis of chaperonin-dependent protein folding in Escherichia coli.
Michael J Kerner ... F Ulrich Hartl
Cell 2005 Jul; 122(2)209-20.
Score: 0.451
Contribution of molecular chaperones to protein folding in the cytoplasm of prokaryotic and eukaryotic cells.
D J Naylor ... F U Hartl
Biochem Soc Symp 2001 ; (68)45-68.
Score: 0.450
The general concept of molecular chaperones.
R J Ellis
Philos Trans R Soc Lond B Biol Sci 1993 Mar; 339(1289)257-61.
Score: 0.449
Principles of chaperone-mediated protein folding.
F U Hartl
Philos Trans R Soc Lond B Biol Sci 1995 Apr; 348(1323)107-12.
Score: 0.448
Reversible oligomerization and denaturation of the chaperonin GroES.
J W Seale ... P M Horowitz
Biochemistry 1996 Apr; 35(13)4079-83.
Score: 0.447
Protein folding: how the mechanism of GroEL action is defined by kinetics.
C Frieden ... A C Clark
Proc Natl Acad Sci U S A 1997 May; 94(11)5535-8.
Score: 0.447
Lessons from genetic disorders of branched-chain amino acid metabolism.
David T Chuang ... R Max Wynn
J Nutr 2006 Jan; 136(1 Suppl)243S-9S.
Score: 0.446
Impaired assembly of E1 decarboxylase of the branched-chain alpha-ketoacid dehydrogenase complex in type IA maple syrup urine disease.
R M Wynn ... D T Chuang
J Biol Chem 1998 May; 273(21)13110-8.
Score: 0.445
On the role of symmetrical and asymmetrical chaperonin complexes in assisted protein folding.
M K Hayer-Hartl ... F U Hartl
Biol Chem 1999 May; 380(5)531-40.
Score: 0.445
Hsp60-independent protein folding in the matrix of yeast mitochondria.
S Rospert ... G Schatz
EMBO J 1996 Feb; 15(4)764-74.
Score: 0.444
Mechanisms of protein folding.
V Grantcharova ... A L Horwich
Curr Opin Struct Biol 2001 Feb; 11(1)70-82.
Score: 0.443
Structural and biochemical basis for novel mutations in homozygous Israeli maple syrup urine disease patients: a proposed mechanism for the thiamin-responsive phenotype.
Jacinta L Chuang ... David T Chuang
J Biol Chem 2004 Apr; 279(17)17792-800.
Score: 0.442
Protein folding in the cytosol: chaperonin-dependent and -independent mechanisms.
W J Netzer ... F U Hartl
Trends Biochem Sci 1998 Feb; 23(2)68-73.
Score: 0.442
The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding.
J Martin ... F U Hartl
Nature 1993 Nov; 366(6452)228-33.
Score: 0.441
Chaperonins groEL and groES promote assembly of heterotetramers (alpha 2 beta 2) of mammalian mitochondrial branched-chain alpha-keto acid decarboxylase in Escherichia coli.
R M Wynn ... D T Chuang
J Biol Chem 1992 Jun; 267(18)12400-3.
Score: 0.441
Molecular chaperones and mitochondrial protein folding.
J Martin
J Bioenerg Biomembr 1997 Feb; 29(1)35-43.
Score: 0.441
Folding and assembly of oligomeric proteins in Escherichia coli.
C M Teschke ... J King
Curr Opin Biotechnol 1992 Oct; 3(5)468-73.
Score: 0.440
Molecular chaperones: containers and surfaces for folding, stabilising or unfolding proteins.
H Saibil
Curr Opin Struct Biol 2000 Apr; 10(2)251-8.
Score: 0.439
ENU mutagenesis identifies mice with mitochondrial branched-chain aminotransferase deficiency resembling human maple syrup urine disease.
Jer-Yuarn Wu ... Yuan-Tsong Chen
J Clin Invest 2004 Feb; 113(3)434-40.
Score: 0.438
GroEL accelerates the refolding of hen lysozyme without changing its folding mechanism.
J E Coyle ... S E Radford
Nat Struct Biol 1999 Jul; 6(7)683-90.
Score: 0.438
E2 transacylase-deficient (type II) maple syrup urine disease. Aberrant splicing of E2 mRNA caused by internal intronic deletions and association with thiamine-responsive phenotype.
J L Chuang ... D T Chuang
J Clin Invest 1997 Aug; 100(3)736-44.
Score: 0.437
The role of heat-shock proteins as molecular chaperones.
W J Welch
Curr Opin Cell Biol 1991 Dec; 3(6)1033-8.
Score: 0.437
Catalysis of protein folding by symmetric chaperone complexes.
H Sparrer ... J Buchner
Proc Natl Acad Sci U S A 1997 Feb; 94(4)1096-100.
Score: 0.436
Confirmation of the hierarchical folding of RNase H: a protein engineering study.
T M Raschke ... S Marqusee
Nat Struct Biol 1999 Sep; 6(9)825-31.
Score: 0.436
The role of molecular chaperones in protein folding.
J P Hendrick ... F U Hartl
FASEB J 1995 Dec; 9(15)1559-69.
Score: 0.435
Protein folding in the cell: molecular chaperones pave the way.
J Martin ... F U Hartl
Structure 1993 Nov; 1(3)161-4.
Score: 0.434
Degradation of mutant proteins, underlying "loss of function" phenotypes, plays a major role in genetic disease.
P J Waters
Curr Issues Mol Biol 2001 Jul; 3(3)57-65.
Score: 0.434
Chaperonin GroEL meets the substrate protein as a "load" of the rings.
Hideki Taguchi
J Biochem (Tokyo) 2005 May; 137(5)543-9.
Score: 0.433
Minimal and optimal mechanisms for GroE-mediated protein folding.
A P Ben-Zvi ... P Goloubinoff
Proc Natl Acad Sci U S A 1998 Dec; 95(26)15275-80.
Score: 0.433
Chaperone-mediated protein folding.
A L Fink
Physiol Rev 1999 Apr; 79(2)425-49.
Score: 0.431
The chaperonin cycle and protein folding.
P Lund
Bioessays 1994 Apr; 16(4)229-31.
Score: 0.430
"Half of the sites" binding of D-glyceraldehyde-3-phosphate dehydrogenase folding intermediate with GroEL.
J Li ... C C Wang
J Biol Chem 1999 Apr; 274(16)10790-4.
Score: 0.429
Involvement of two novel chaperones in the assembly of mitochondrial NADH:Ubiquinone oxidoreductase (complex I).
R Küffner ... U Schulte
J Mol Biol 1998 Oct; 283(2)409-17.
Score: 0.428
Scaffolding proteins and their role in viral assembly.
T Dokland
Cell Mol Life Sci 1999 Nov; 56(7-8)580-603.
Score: 0.428
Mechanism of chaperonin action: GroES binding and release can drive GroEL-mediated protein folding in the absence of ATP hydrolysis.
M K Hayer-Hartl ... F U Hartl
EMBO J 1996 Nov; 15(22)6111-21.
Score: 0.427
Stress proteins and glycoproteins (Review).
K J Henle ... W A Nagle
Int J Mol Med 1998 Jan; 1(1)25-32.
Score: 0.427
Enzyme assembly after de novo synthesis in rabbit reticulocyte lysate involves molecular chaperones and immunophilins.
M Kruse ... R Zimmermann
J Biol Chem 1995 Feb; 270(6)2588-94.
Score: 0.427
Co-translational involvement of the chaperonin GroEL in the folding of newly translated polypeptides.
Bei-Wen Ying ... Takuya Ueda
J Biol Chem 2005 Mar; 280(12)12035-40.
Score: 0.426
A mitochondrial chaperonin: genetic, biochemical, and molecular characteristics.
R L Hallberg
Semin Cell Biol 1990 Feb; 1(1)37-45.
Score: 0.424
Molecular chaperones: proteins essential for the biogenesis of some macromolecular structures.
R J Ellis ... S M Hemmingsen
Trends Biochem Sci 1989 Aug; 14(8)339-42.
Score: 0.424
The effect of molecular chaperones on in vivo and in vitro folding processes.
E Schwarz ... R Rudolph
Biol Chem 1996 Jul-Aug; 377(7-8)411-6.
Score: 0.423
[Heat shock proteins as molecular chaperones]
André-Patrick Arrigo
Med Sci (Paris) 2005 Jun-Jul; 21(6-7)619-25.
Score: 0.423
Structure and function in GroEL-mediated protein folding.
P B Sigler ... A L Horwich
Annu Rev Biochem 1998 ; 67()581-608.
Score: 0.422
Changing the nature of the initial chaperonin capture complex influences the substrate folding efficiency.
P A Voziyan ... M T Fisher
J Biol Chem 1998 Sep; 273(39)25073-8.
Score: 0.422
[Gene analysis of maple syrup urine disease (MSUD)]
H Mitsubuchi ... I Matsuda
Rinsho Byori 1993 May; 41(5)484-91.
Score: 0.422
Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis.
J Ostermann ... F U Hartl
Nature 1989 Sep; 341(6238)125-30.
Score: 0.421
Nuclear chaperones.
A Philpott ... R A Laskey
Semin Cell Dev Biol 2000 Feb; 11(1)7-14.
Score: 0.421
Molecular chaperones in cellular protein folding.
J Martin ... F U Hartl
Bioessays 1994 Sep; 16(9)689-92.
Score: 0.420
Total branched-chain amino acids requirement in patients with maple syrup urine disease by use of indicator amino acid oxidation with L-[1-13C]phenylalanine.
Roya Riazi ... Paul B Pencharz
Am J Physiol Endocrinol Metab 2004 Jul; 287(1)E142-9.
Score: 0.419
From the cradle to the grave: molecular chaperones that may choose between folding and degradation.
J Höhfeld ... C Patterson
EMBO Rep 2001 Oct; 2(10)885-90.
Score: 0.418
Accelerated folding in the weak hydrophobic environment of a chaperonin cavity: creation of an alternate fast folding pathway.
A I Jewett ... J-E Shea
Proc Natl Acad Sci U S A 2004 Sep; 101(36)13192-7.
Score: 0.417
Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding.
P S Kim ... R L Baldwin
Annu Rev Biochem 1982 ; 51()459-89.
Score: 0.417
Protein folding and assembly in the endoplasmic reticulum.
J Wei ... L M Hendershot
EXS 1996 ; 77()41-55.
Score: 0.417
Specificity in chaperonin-mediated protein folding.
G Tian ... N J Cowan
Nature 1995 May; 375(6528)250-3.
Score: 0.416
Truncated GroEL monomer has the ability to promote folding of rhodanese without GroES and ATP.
Y Makino ... M Yoshida
FEBS Lett 1993 Dec; 336(2)363-7.
Score: 0.416
Chaperone-assisted protein folding in the cell cytoplasm.
W A Houry
Curr Protein Pept Sci 2001 Sep; 2(3)227-44.
Score: 0.415
Protein quality control: chaperones culling corrupt conformations.
Amie J McClellan ... Judith Frydman
Nat Cell Biol 2005 Aug; 7(8)736-41.
Score: 0.415
Mimicking the action of GroEL in molecular dynamics simulations: application to the refinement of protein structures.
Hao Fan ... Alan E Mark
Protein Sci 2006 Mar; 15(3)441-8.
Score: 0.415
Protein folding: versatility of the cytosolic chaperonin TRiC/CCT.
M R Leroux ... F U Hartl
Curr Biol 2000 Apr; 10(7)R260-4.
Score: 0.413
Crystal structure of the 65-kilodalton heat shock protein, chaperonin 60.2, of Mycobacterium tuberculosis.
Rohini Qamra ... Shekhar C Mande
J Bacteriol 2004 Dec; 186(23)8105-13.
Score: 0.413
Impaired folding and subunit assembly as disease mechanism: the example of medium-chain acyl-CoA dehydrogenase deficiency.
P Bross ... N Gregersen
Prog Nucleic Acid Res Mol Biol 1998 ; 58()301-37.
Score: 0.413
Prions and molecular chaperones.
J P Liautard
Arch Virol Suppl 1993 ; 7()227-43.
Score: 0.413
Involvement of molecular chaperones in intracellular protein breakdown.
M Y Sherman ... A L Goldberg
EXS 1996 ; 77()57-78.
Score: 0.413
A simple model of chaperonin-mediated protein folding.
H S Chan ... K A Dill
Proteins 1996 Mar; 24(3)345-51.
Score: 0.412
In vivo observation of polypeptide flux through the bacterial chaperonin system.
K L Ewalt ... F U Hartl
Cell 1997 Aug; 90(3)491-500.
Score: 0.411
Regulation of the branched-chain alpha-ketoacid dehydrogenase and elucidation of a molecular basis for maple syrup urine disease.
R A Harris ... D W Crabb
Adv Enzyme Regul 1990 ; 30()245-63.
Score: 0.411
Protein folding and diseases.
Cheolju Lee ... Myeong-Hee Yu
J Biochem Mol Biol 2005 May; 38(3)275-80.
Score: 0.411
Toward a mechanism for GroEL.GroES chaperone activity: an ATPase-gated and -pulsed folding and annealing cage.
F J Corrales ... A R Fersht
Proc Natl Acad Sci U S A 1996 Apr; 93(9)4509-12.
Score: 0.410
Mechanism of the eukaryotic chaperonin: protein folding in the chamber of secrets.
Christoph Spiess ... Judith Frydman
Trends Cell Biol 2004 Nov; 14(11)598-604.
Score: 0.409
Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate.
J Martin ... F U Hartl
Nature 1991 Jul; 352(6330)36-42.
Score: 0.409
Principles of chaperone-assisted protein folding: differences between in vitro and in vivo mechanisms.
J Frydman ... F U Hartl
Science 1996 Jun; 272(5267)1497-502.
Score: 0.408
Individual subunits of bacterial luciferase are molten globules and interact with molecular chaperones.
G C Flynn ... F W Dahlquist
Proc Natl Acad Sci U S A 1993 Nov; 90(22)10826-30.
Score: 0.408
Protein folding and chaperonins.
A A Gatenby
Plant Mol Biol 1992 Jul; 19(4)677-87.
Score: 0.408
Characterization of a quaternary-structured folding intermediate of an antibody Fab-fragment.
H Lilie ... J Buchner
Protein Sci 1995 May; 4(5)917-24.
Score: 0.408
Protein folding in the cell: on the mechanisms of its acceleration.
N K Nagradova
Biochemistry (Mosc) 2004 Aug; 69(8)830-43.
Score: 0.407
Im7 folding mechanism: misfolding on a path to the native state.
Andrew P Capaldi ... Sheena E Radford
Nat Struct Biol 2002 Mar; 9(3)209-16.
Score: 0.407
Revisiting the Anfinsen cage.
R J Ellis
Fold Des 1996 ; 1(1)R9-15.
Score: 0.407
Molecular chaperones, folding catalysts, and the recovery of active recombinant proteins from E. coli. To fold or to refold.
J G Thomas ... F Baneyx
Appl Biochem Biotechnol 1997 Jun; 66(3)197-238.
Score: 0.406
Chaperonins.
N A Ranson ... H R Saibil
Biochem J 1998 Jul; 333 ( Pt 2)()233-42.
Score: 0.406
Quasi-native chaperonin-bound intermediates in facilitated protein folding.
G Tian ... N J Cowan
J Biol Chem 1995 Oct; 270(41)23910-3.
Score: 0.405
GroEL-mediated protein folding.
W A Fenton ... A L Horwich
Protein Sci 1997 Apr; 6(4)743-60.
Score: 0.404
Protein folding in the central cavity of the GroEL-GroES chaperonin complex.
M Mayhew ... F U Hartl
Nature 1996 Feb; 379(6564)420-6.
Score: 0.404
Refolding and reassembly of active chaperonin GroEL after denaturation.
J Ybarra ... P M Horowitz
J Biol Chem 1995 Sep; 270(38)22113-5.
Score: 0.404
[Molecular chaperones: new proteins--new functions]
V A Ivaniushina ... O I Kiselev
Mol Biol (Mosk) 1991 Jul-Aug; 25(4)869-82.
Score: 0.404
Molecular and biochemical basis of intermediate maple syrup urine disease. Occurrence of homozygous G245R and F364C mutations at the E1 alpha locus of Hispanic-Mexican patients.
J L Chuang ... D T Chuang
J Clin Invest 1995 Mar; 95(3)954-63.
Score: 0.403
PapD-like chaperones provide the missing information for folding of pilin proteins.
M M Barnhart ... S J Hultgren
Proc Natl Acad Sci U S A 2000 Jul; 97(14)7709-14.
Score: 0.403
Functional TIM10 chaperone assembly is redox-regulated in vivo.
Hui Lu ... Kostas Tokatlidis
J Biol Chem 2004 Apr; 279(18)18952-8.
Score: 0.402
Interaction of GroEL with a highly structured folding intermediate: iterative binding cycles do not involve unfolding.
H Lilie ... J Buchner
Proc Natl Acad Sci U S A 1995 Aug; 92(18)8100-4.
Score: 0.402
Requirement for GroEL/GroES-dependent protein folding under nonpermissive conditions of macromolecular crowding.
Jörg Martin
Biochemistry 2002 Apr; 41(15)5050-5.
Score: 0.402
The mitochondrial chaperonin hsp60 is required for its own assembly.
M Y Cheng ... A L Horwich
Nature 1990 Nov; 348(6300)455-8.
Score: 0.401
GroEL-GroES-mediated protein folding requires an intact central cavity.
J D Wang ... J S Weissman
Proc Natl Acad Sci U S A 1998 Oct; 95(21)12163-8.
Score: 0.400
Molecular chaperones in protein quality control.
Sukyeong Lee ... Francis T F Tsai
J Biochem Mol Biol 2005 May; 38(3)259-65.
Score: 0.400
GroEL under heat-shock. Switching from a folding to a storing function.
O Llorca ... J M Valpuesta
J Biol Chem 1998 Dec; 273(49)32587-94.
Score: 0.400
A peptide model of a protein folding intermediate.
T G Oas ... P S Kim
Nature 1988 Nov; 336(6194)42-8.
Score: 0.399
The Escherichia coli heat shock proteins GroEL and GroES modulate the folding of the beta-lactamase precursor.
A A Laminet ... A Plückthun
EMBO J 1990 Jul; 9(7)2315-9.
Score: 0.399
Intermediates in protein folding reactions and the mechanism of protein folding.
R L Baldwin
Annu Rev Biochem 1975 ; 44()453-75.
Score: 0.399
Influence of subunit transcript and protein levels on formation of a mitochondrial multienzyme complex.
B B McConnell ... D J Danner
J Cell Biochem 1996 Apr; 61(1)118-26.
Score: 0.399
Purified chaperonin 60 (groEL) interacts with the nonnative states of a multitude of Escherichia coli proteins.
P V Viitanen ... G H Lorimer
Protein Sci 1992 Mar; 1(3)363-9.
Score: 0.398
Molecular chaperones. Unfolding protein folding.
T E Creighton
Nature 1991 Jul; 352(6330)17-8.
Score: 0.398
Protein folding and molecular chaperones in archaea.
M R Leroux
Adv Appl Microbiol 2001 ; 50()219-77.
Score: 0.398
What does protein refolding in vitro tell us about protein folding in the cell?
R Jaenicke
Philos Trans R Soc Lond B Biol Sci 1993 Mar; 339(1289)287-94; discussion 294-5.
Score: 0.398
Asymmetrical interaction of GroEL and GroES in the ATPase cycle of assisted protein folding.
M K Hayer-Hartl ... F U Hartl
Science 1995 Aug; 269(5225)836-41.
Score: 0.398
How chaperones fold proteins.
M Beissinger ... J Buchner
Biol Chem 1998 Mar; 379(3)245-59.
Score: 0.397
Binding, encapsulation and ejection: substrate dynamics during a chaperonin-assisted folding reaction.
N A Ranson ... A R Clarke
J Mol Biol 1997 Mar; 266(4)656-64.
Score: 0.397
Facilitated folding of actins and tubulins occurs via a nucleotide-dependent interaction between cytoplasmic chaperonin and distinctive folding intermediates.
R Melki ... N J Cowan
Mol Cell Biol 1994 May; 14(5)2895-904.
Score: 0.397
Catalysis, commitment and encapsulation during GroE-mediated folding.
M Beissinger ... J Buchner
J Mol Biol 1999 Jun; 289(4)1075-92.
Score: 0.396
Limits of protein folding inside GroE complexes.
H Grallert ... J Buchner
J Biol Chem 2000 Jul; 275(27)20424-30.
Score: 0.396
Function of the maize mitochondrial chaperonin hsp60: specific association between hsp60 and newly synthesized F1-ATPase alpha subunits.
T K Prasad ... R L Hallberg
Mol Cell Biol 1990 Aug; 10(8)3979-86.
Score: 0.395
Branched-chain ketoacid dehydrogenase activity and growth of normal and mutant human fibroblasts: the effect of branched-chain amino acid concentration in culture medium.
D J Danner ... J H Priest
Biochem Genet 1983 Oct; 21(9-10)895-905.
Score: 0.395
Coupling between protein folding and allostery in the GroE chaperonin system.
O Yifrach ... A Horovitz
Proc Natl Acad Sci U S A 2000 Feb; 97(4)1521-4.
Score: 0.395
TRiC/CCT cooperates with different upstream chaperones in the folding of distinct protein classes.
Katja Siegers ... F Ulrich Hartl
EMBO J 2003 Oct; 22(19)5230-40.
Score: 0.395
The N terminus of the molecular chaperonin GroEL is a crucial structural element for its assembly.
A Horovitz ... A S Girshovich
J Biol Chem 1993 May; 268(14)9957-9.
Score: 0.394
Reversal by GroES of the GroEL preference from hydrophobic amino acids toward hydrophilic amino acids.
A de Crouy-Chanel ... G Richarme
J Biol Chem 1995 May; 270(18)10571-5.
Score: 0.394
Mechanism of capsid maturation in a double-stranded DNA virus.
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Proc Natl Acad Sci U S A 1998 Aug; 95(17)9885-90.
Score: 0.393
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Masataka Mori
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Score: 0.393
Review: cellular substrates of the eukaryotic chaperonin TRiC/CCT.
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J Struct Biol 2001 Aug; 135(2)176-84.
Score: 0.393
Analysis of GroE-assisted folding under nonpermissive conditions.
H Grallert ... J Buchner
J Biol Chem 1999 Jul; 274(29)20171-7.
Score: 0.393
Native-like structure of a protein-folding intermediate bound to the chaperonin GroEL.
M S Goldberg ... A L Horwich
Proc Natl Acad Sci U S A 1997 Feb; 94(4)1080-5.
Score: 0.393
Cyclophilin 20 is involved in mitochondrial protein folding in cooperation with molecular chaperones Hsp70 and Hsp60.
J Rassow ... M Tropschug
Mol Cell Biol 1995 May; 15(5)2654-62.
Score: 0.392
A comparison of the GroE chaperonin requirements for sequentially and structurally homologous malate dehydrogenases: the importance of folding kinetics and solution environment.
B C Tieman ... M T Fisher
J Biol Chem 2001 Nov; 276(48)44541-50.
Score: 0.392
Two new mutations in the human E1 beta subunit of branched chain alpha-ketoacid dehydrogenase associated with maple syrup urine disease.
B B McConnell ... D J Danner
Biochim Biophys Acta 1997 Oct; 1361(3)263-71.
Score: 0.392
Bacteriophage T4 encodes a co-chaperonin that can substitute for Escherichia coli GroES in protein folding.
S M van der Vies ... C Georgopoulos
Nature 1994 Apr; 368(6472)654-6.
Score: 0.392
Identification of in vivo substrates of the yeast mitochondrial chaperonins reveals overlapping but non-identical requirement for hsp60 and hsp10.
Y Dubaquié ... S Rospert
EMBO J 1998 Oct; 17(20)5868-76.
Score: 0.392
Protein folding in the cell.
M J Gething ... J Sambrook
Nature 1992 Jan; 355(6355)33-45.
Score: 0.391
Folding and assembly of viral membrane proteins.
R W Doms ... A Helenius
Virology 1993 Apr; 193(2)545-62.
Score: 0.391
GroEL-mediated folding of structurally homologous dihydrofolate reductases.
A C Clark ... C Frieden
J Mol Biol 1997 May; 268(2)512-25.
Score: 0.391
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Douglas E Feldman ... Judith Frydman
Mol Cell 2003 Nov; 12(5)1213-24.
Score: 0.390
In vivo newly translated polypeptides are sequestered in a protected folding environment.
V Thulasiraman ... J Frydman
EMBO J 1999 Jan; 18(1)85-95.
Score: 0.390
Human microRNA (miR29b) expression controls the amount of branched chain alpha-ketoacid dehydrogenase complex in a cell.
Benjamin D Mersey ... Dean J Danner
Hum Mol Genet 2005 Nov; 14(22)3371-7.
Score: 0.390
Polypeptide interactions with molecular chaperones and their relationship to in vivo protein folding.
S J Landry ... L M Gierasch
Annu Rev Biophys Biomol Struct 1994 ; 23()645-69.
Score: 0.389
Generation of a stable folding intermediate which can be rescued by the chaperonins GroEL and GroES.
D Peralta ... P B Høj
FEBS Lett 1994 Feb; 339(1-2)45-9.
Score: 0.389
Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria.
M Y Cheng ... A L Horwich
Nature 1989 Feb; 337(6208)620-5.
Score: 0.389
Folding of newly translated proteins in vivo: the role of molecular chaperones.
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Score: 0.389
Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL.
H S Rye ... A L Horwich
Nature 1997 Aug; 388(6644)792-8.
Score: 0.388
Posttranslational quality control: folding, refolding, and degrading proteins.
S Wickner ... S Gottesman
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Score: 0.388
Intermediate filaments: structure, assembly and molecular interactions.
M Stewart
Curr Opin Cell Biol 1990 Feb; 2(1)91-100.
Score: 0.388
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J F Hunt ... J Deisenhofer
Cell 1997 Jul; 90(2)361-71.
Score: 0.388
GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms.
J S Weissman ... A L Horwich
Cell 1994 Aug; 78(4)693-702.
Score: 0.388
A quantitative assessment of the role of the chaperonin proteins in protein folding in vivo.
G H Lorimer
FASEB J 1996 Jan; 10(1)5-9.
Score: 0.387
Predicting the protein folding nucleus from sequences [correction of a sequence]
A Poupon ... J P Mornon
FEBS Lett 1999 Jun; 452(3)283-9.
Score: 0.387
A protein folding pathway with multiple folding intermediates at atomic resolution.
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Score: 0.387
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G M Mueller ... H S Paul
Gene Ther 1995 Sep; 2(7)461-8.
Score: 0.386
Luciferase assembly after transport into mammalian microsomes involves molecular chaperones and peptidyl-prolyl cis/trans-isomerases.
M Brunke ... R Zimmermann
J Biol Chem 1996 Sep; 271(38)23487-94.
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Cotranslational folding of proteins.
V A Kolb ... A S Spirin
Biochem Cell Biol 1995 Nov-Dec; 73(11-12)1217-20.
Score: 0.386
Chaperone-percolator model: a possible molecular mechanism of Anfinsen-cage-type chaperones.
P Csermely
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Score: 0.386
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Score: 0.385
A concerted mechanism for the suppression of a folding defect through interactions with chaperones.
Shannon M Doyle ... Carolyn M Teschke
J Biol Chem 2004 Apr; 279(17)17473-82.
Score: 0.384
Unfolding the role of chaperones and chaperonins in human disease.
A M Slavotinek ... L G Biesecker
Trends Genet 2001 Sep; 17(9)528-35.
Score: 0.384
Structure of a folding intermediate reveals the interplay between core and peripheral elements in RNA folding.
Nathan J Baird ... Tobin R Sosnick
J Mol Biol 2005 Sep; 352(3)712-22.
Score: 0.384
Molecular chaperones and the cytoskeleton.
P Liang ... T H MacRae
J Cell Sci 1997 Jul; 110 ( Pt 13)()1431-40.
Score: 0.383
Theory of protein folding.
José Nelson Onuchic ... Peter G Wolynes
Curr Opin Struct Biol 2004 Feb; 14(1)70-5.
Score: 0.383
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Score: 0.383
Folding kinetics of the lipoic acid-bearing domain of human mitochondrial branched chain alpha-ketoacid dehydrogenase complex.
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The molecular chaperone concept.
R J Ellis ... S M Hemmingsen
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Score: 0.383
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Score: 0.383
Watching protein folding unfold.
H Roder
Nat Struct Biol 1995 Oct; 2(10)817-20.
Score: 0.383
The importance of a mobile loop in regulating chaperonin/ co-chaperonin interaction: humans versus Escherichia coli.
A Richardson ... C Georgopoulos
J Biol Chem 2001 Feb; 276(7)4981-7.
Score: 0.382
Chaperonin-facilitated protein folding: optimization of rate and yield by an iterative annealing mechanism.
M J Todd ... D Thirumalai
Proc Natl Acad Sci U S A 1996 Apr; 93(9)4030-5.
Score: 0.382
Branched-chain amino acids: enzyme and substrate regulation.
John T Brosnan ... Margaret E Brosnan
J Nutr 2006 Jan; 136(1 Suppl)207S-11S.
Score: 0.382
Refolding of yeast enolase in the presence of the chaperonin GroE. The nucleotide specificity of GroE and the role of GroES.
T Kubo ... Y Kawata
J Biol Chem 1993 Sep; 268(26)19346-51.
Score: 0.382
Mechanism of substrate recognition by the chaperonin GroEL.
W A Houry
Biochem Cell Biol 2001 ; 79(5)569-77.
Score: 0.382
Roles of molecular chaperones in cytoplasmic protein folding.
V R Agashe ... F U Hartl
Semin Cell Dev Biol 2000 Feb; 11(1)15-25.
Score: 0.381
Intermediates and the folding of proteins L and G.
Scott Brown ... Teresa Head-Gordon
Protein Sci 2004 Apr; 13(4)958-70.
Score: 0.381
The chaperonin GroEL binds a polypeptide in an alpha-helical conformation.
S J Landry ... L M Gierasch
Biochemistry 1991 Jul; 30(30)7359-62.
Score: 0.381
The role of molecular chaperones in mitochondrial protein import and folding.
M T Ryan ... N J Hoogenraad
Int Rev Cytol 1997 ; 174()127-93.
Score: 0.380
Molecular chaperones as essential mediators of mitochondrial biogenesis.
Wolfgang Voos ... Karin Röttgers
Biochim Biophys Acta 2002 Sep; 1592(1)51-62.
Score: 0.380
Differential regulation of branched-chain alpha-ketoacid dehydrogenase kinase expression by glucocorticoids and acidification in LLC-PK1-GR101 cells.
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Am J Physiol Renal Physiol 2004 Mar; 286(3)F504-8.
Score: 0.380
Function in protein folding of TRiC, a cytosolic ring complex containing TCP-1 and structurally related subunits.
J Frydman ... F U Hartl
EMBO J 1992 Dec; 11(13)4767-78.
Score: 0.379
Selective in vivo rescue by GroEL/ES of thermolabile folding intermediates to phage P22 structural proteins.
C L Gordon ... J King
J Biol Chem 1994 Nov; 269(45)27941-51.
Score: 0.379
Periplasmic chaperone recognition motif of subunits mediates quaternary interactions in the pilus.
G E Soto ... S J Hultgren
EMBO J 1998 Nov; 17(21)6155-67.
Score: 0.379
Transient folding intermediates characterized by protein engineering.
A Matouschek ... A R Fersht
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Score: 0.379
Supervising the fold: functional principles of molecular chaperones.
J Buchner
FASEB J 1996 Jan; 10(1)10-9.
Score: 0.379
Kinetic model of BiP- and PDI-mediated protein folding and assembly.
Ramon Gonz lez ... Juan A Asenjo
J Theor Biol 2002 Feb; 214(4)529-37.
Score: 0.379
Protein sorting to mitochondria: evolutionary conservations of folding and assembly.
F U Hartl ... W Neupert
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Score: 0.378
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C B Doering ... D J Danner
Am J Physiol Cell Physiol 2000 Nov; 279(5)C1587-94.
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Significance of chaperonin 10-mediated inhibition of ATP hydrolysis by chaperonin 60.
Y Dubaquié ... S Rospert
Proc Natl Acad Sci U S A 1997 Aug; 94(17)9011-6.
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Myosin II folding is mediated by a molecular chaperonin.
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Intermediates in the folding of the membrane protein bacteriorhodopsin.
P J Booth ... H G Khorana
Nat Struct Biol 1995 Feb; 2(2)139-43.
Score: 0.377
Chaperonin releases the substrate protein in a form with tendency to aggregate and ability to rebind to chaperonin.
H Taguchi ... M Yoshida
FEBS Lett 1995 Feb; 359(2-3)195-8.
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Potential role of leucine metabolism in the leucine-signaling pathway involving mTOR.
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Directionality of polypeptide transfer in the mitochondrial pathway of chaperone-mediated protein folding.
N Heyrovská ... F U Hartl
Biol Chem 1998 Mar; 379(3)301-9.
Score: 0.377
Chaperonins facilitate the in vitro folding of monomeric mitochondrial rhodanese.
J A Mendoza ... P M Horowitz
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Score: 0.377
Translocation boost protein-folding efficiency of double-barreled chaperonins.
Ivan Coluzza ... Daan Frenkel
Biophys J 2006 May; 90(10)3375-81.
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GroEL and GroES control of substrate flux in the in vivo folding pathway of phage P22 coat protein.
W S Nakonechny ... C M Teschke
J Biol Chem 1998 Oct; 273(42)27236-44.
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RNA and protein folding: common themes and variations.
D Thirumalai ... Changbong Hyeon
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Folding and stability of the ligand-binding domain of the glucocorticoid receptor.
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Chaperonin GroESL mediates the protein folding of human liver mitochondrial aldehyde dehydrogenase in Escherichia coli.
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Score: 0.375
Periplasmic chaperones--preservers of subunit folding energy for organelle assembly.
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Cell 2003 May; 113(5)556-7.
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RNA folding in vivo.
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M D Morris ... R Fiser
J Lancet 1966 Mar; 86(3)149-52.
Score: 0.374
The role of chaperone-assisted folding and quality control in inborn errors of metabolism: protein folding disorders.
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Molecular guardians for newborn proteins: ribosome-associated chaperones and their role in protein folding.
R D Wegrzyn ... E Deuerling
Cell Mol Life Sci 2005 Dec; 62(23)2727-38.
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Protein folding and the regulation of signaling pathways.
S L Rutherford ... C S Zuker
Cell 1994 Dec; 79(7)1129-32.
Score: 0.374
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R G WESTALL
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Score: 0.374
Molecular chaperones in protein folding and translocation.
A R Clarke
Curr Opin Struct Biol 1996 Feb; 6(1)43-50.
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M Bixel ... B Hamprecht
J Histochem Cytochem 2001 Mar; 49(3)407-18.
Score: 0.373
Location of a folding protein and shape changes in GroEL-GroES complexes imaged by cryo-electron microscopy.
S Chen ... H R Saibil
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Identification of twelve novel mutations in patients with classic and variant forms of maple syrup urine disease.
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An expanded protein folding cage in the GroEL-gp31 complex.
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Chaperone-assisted folding of newly synthesized proteins in the cytosol.
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Influence of molecular and chemical chaperones on protein folding.
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Role of the GroEL chaperonin intermediate domain in coupling ATP hydrolysis to polypeptide release.
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Design of a molecular chaperone-assisted protein folding bioreactor.
R J Kohler ... A D Miller
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Specific non-native hydrophobic interactions in a hidden folding intermediate: implications for protein folding.
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The ins and outs of GroEL-mediated protein folding.
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Protein self-organization in vitro and in vivo: partitioning between physical biochemistry and cell biology.
R Jaenicke
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A thermodynamic coupling mechanism can explain the GroEL-mediated acceleration of the folding of barstar.
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A polypeptide bound by the chaperonin groEL is localized within a central cavity.
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The Escherichia coli groE chaperonins.
C Georgopoulos ... D Ang
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Folding in vivo of bacterial cytoplasmic proteins: role of GroEL.
A L Horwich ... K Furtak
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Score: 0.370
Refolding of target proteins from a "rigid" mutant chaperonin demonstrates a minimal mechanism of chaperonin binding and release.
T Mizobata ... Y Kawata
J Biol Chem 2000 Aug; 275(33)25600-7.
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Dissecting the assembly pathway of the 20S proteasome.
F Zühl ... W Baumeister
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Stability of the asymmetric Escherichia coli chaperonin complex. Guanidine chloride causes rapid dissociation.
M J Todd ... G H Lorimer
J Biol Chem 1995 Mar; 270(10)5388-94.
Score: 0.370
Binding of a burst-phase intermediate formed in the folding of denatured D-glyceraldehyde-3-phosphate dehydrogenase by chaperonin 60 and 8-anilino-1-naphthalenesulphonic acid.
X L Li ... C L Tsou
Biochem J 1998 Apr; 331 ( Pt 2)()505-11.
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Chaperonin function--effects of crowding and confinement.
Jörg Martin
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GroEL, GroES, and ATP-dependent folding and spontaneous assembly of ornithine transcarbamylase.
X Zheng ... W A Fenton
J Biol Chem 1993 Apr; 268(10)7489-93.
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Chaperone protein GrpE and the GroEL/GroES complex promote the correct folding of tobacco mosaic virus coat protein for ribonucleocapsid assembly in vivo.
D J Hwang ... T M Wilson
Arch Virol 1998 ; 143(11)2203-14.
Score: 0.369
Pharmacological chaperones: a new twist on receptor folding.
J P Morello ... M Bouvier
Trends Pharmacol Sci 2000 Dec; 21(12)466-9.
Score: 0.368
Conformational states bound by the
