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Hartl FU. Molecular chaperones in cellular protein folding. Nature. 381:1996;571-580.
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of special interest. An excellent comprehensive and current review of GroEL-mediated protein folding.
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of special interest Fenton WA, Horwich AL. GroEL-mediated protein folding. Protein Sci. 6:1997;743-760 An excellent comprehensive and current review of GroEL-mediated protein folding.
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Fenton, W.A.1
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Hayes, S.A.1
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The crystal structure of the bacterial chaperonin GroEL at 2.8 Å
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Braig K, Otwinowski Z, Hegde R, Boisvert DC, Joachimiak A, Horwich AL, Sigler PB. The crystal structure of the bacterial chaperonin GroEL at 2.8 Å Nature. 371:1994;578-586.
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Conformational variability in the refined structure of the chaperonin GroEL at 2.8 Å resolution
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Braig K, Adams PD, Brünger AT. Conformational variability in the refined structure of the chaperonin GroEL at 2.8 Å resolution. Nat Struct Biol. 2:1995;1083-1094.
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Roseman AM, Chen S, White H, Braig K, Saibil HR. The chaperonin ATPase cycle: mechanism of allosteric switching and movements of substrate-binding domains in GroEL. Cell. 87:1996;241-251.
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Martin J, Langer T, Boteva R, Schramel A, Horwich AL, Hartl FU. Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate. Nature. 352:1991;36-42.
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Martin, J.1
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Yifrach O, Horovitz A. Allosteric control by ATP of non-folded protein binding to GroEL. J Mol Biol. 255:1996;356-361.
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Gray TE, Fersht AR. Cooperativity in ATP hydrolysis by GroEL is increased by GroES. FEBS Lett. 292:1991;254-258.
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Bochkareva ES, Lissin NM, Flynn GC, Rothman JE, Girshovich AS. Positive cooperativity in the functioning of molecular chaperone GroEL. J Biol Chem. 267:1992;6796-6800.
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Binding and hydrolysis of nucleotides in the chaperonin catalytic cycle: Implications for the mechanism of assisted protein folding
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Jackson GS, Staniforth RA, Halsall DJ, Atkinson T, Holbrook JJ, Clarke AR, Burston SG. Binding and hydrolysis of nucleotides in the chaperonin catalytic cycle: implications for the mechanism of assisted protein folding. Biochemistry. 32:1993;2554-2563.
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Jackson, G.S.1
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0027250447
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Hydrolysis of adenosine 5'-triphosphate by Escherichia coli GroEL: Effects of GroES and potassium ion
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Tood MJ, Viitanen PV, Lorimer GH. Hydrolysis of adenosine 5'-triphosphate by Escherichia coli GroEL: effects of GroES and potassium ion. Biochemistry. 32:1993;8560-8567.
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Tood, M.J.1
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Affinity of chaperonin-60 for a protein substrate and its modulation by nucleotides and chaperonin-10
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Staniforth RA, Burston SG, Atkinson T, Clarke AR. Affinity of chaperonin-60 for a protein substrate and its modulation by nucleotides and chaperonin-10. Biochem J. 300:1994;651-658.
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Staniforth, R.A.1
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18
-
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0030870719
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7 chaperonin complex
-
7 chaperonin complex determined by X-ray crystallography at 3.0 Å resolution. Elevation and twist of the apical domains enable bound GroES to stabilize a folding chamber that is doubled in volume and has a hydrophilic lining. In contrast, the trans ring, which is in an acceptor state for nonfolded proteins, has a hydrophobic lining. An inward tilt of the equatorial domains in the cis ring, causes an outward tilt of the subunits in the trans ring, which explains the observed negative cooperatively between rings in GroEL.
-
7 chaperonin complex determined by X-ray crystallography at 3.0 Å resolution. Elevation and twist of the apical domains enable bound GroES to stabilize a folding chamber that is doubled in volume and has a hydrophilic lining. In contrast, the trans ring, which is in an acceptor state for nonfolded proteins, has a hydrophobic lining. An inward tilt of the equatorial domains in the cis ring, causes an outward tilt of the subunits in the trans ring, which explains the observed negative cooperatively between rings in GroEL.
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(1997)
Nature
, vol.388
, pp. 741-750
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Xu, Z.1
Horwich, A.L.2
Sigler, P.B.3
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19
-
-
0031228499
-
Structural basis of allosteric changes in the GroEL mutant Arg197→Ala
-
of outstanding interest. The 3D structures of the Arg197Ala GroEL mutant [37] in the absence and presence of different concentrations of ATP were determined at 30 Å resolution by electron cryo-microscopy and single particle reconstruction. The differences between the structures of the three allosteric states are clearly visualized. The structure of the TR state, which is strongly asymmetric, shows ring opening and anticlockwise rotation of the apical domains in the ATP-bound (R) ring and ring closing and clockwise rotation of the apical domains in the T ring. In the RR state, both rings open and only anticlockwise rotation is observed. Also seen is the elongation of the structure during this transitions TT→TR→RR. A fit of the atomic coordinates of the apical domain [35] to the EM density maps shows that the lining of the cavity in the TT state is continuous and hydrophobic, thus forming a binding site for nonfolded proteins, whereas in the rings in the R state
-
of outstanding interest White HE, Chen S, Roseman AM, Yifrach O, Horovitz A, Saibil HR. Structural basis of allosteric changes in the GroEL mutant Arg197→Ala. Nat Struct Biol. 4:1997;690-694 The 3D structures of the Arg197Ala GroEL mutant [37] in the absence and presence of different concentrations of ATP were determined at 30 Å resolution by electron cryo-microscopy and single particle reconstruction. The differences between the structures of the three allosteric states are clearly visualized. The structure of the TR state, which is strongly asymmetric, shows ring opening and anticlockwise rotation of the apical domains in the ATP-bound (R) ring and ring closing and clockwise rotation of the apical domains in the T ring. In the RR state, both rings open and only anticlockwise rotation is observed. Also seen is the elongation of the structure during this transitions TT→TR→RR. A fit of the atomic coordinates of the apical domain [35] to the EM density maps shows that the lining of the cavity in the TT state is continuous and hydrophobic, thus forming a binding site for nonfolded proteins, whereas in the rings in the R state it is disrupted. The fit also shows that up to 42 intersubunit electrostatic interactions in the T ring may break during the TR→RR transition.
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(1997)
Nat Struct Biol
, vol.4
, pp. 690-694
-
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White, H.E.1
Chen, S.2
Roseman, A.M.3
Yifrach, O.4
Horovitz, A.5
Saibil, H.R.6
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20
-
-
0030966765
-
A structural model for GroEL - Polypeptide recognition
-
of outstanding interest. This paper describes the 1.7 Å resolution structure of the apical domain of GroEL with a 17-residue N-terminal tag. The N-terminal tag of one molecule is bound to a neighbouring molecule in the crystal at a site that corresponds to a region previously identified by site-directed mutagenesis [21] to be involved in polypeptide binding. This appears to mimic the binding of a peptide substrate to GroEL, thereby providing the first high-resolution information on GroEL - polypeptide interactions. The conformation of the tag is extended and the binding involves both hydrophobic interactions and hydrogen bonds between sidechains of GroEL and the mainchain of the substrate.
-
of outstanding interest Buckle AM, Zahn R, Fersht AR. A structural model for GroEL - polypeptide recognition. Proc Natl Acad Sci USA. 94:1997;3571-3575 This paper describes the 1.7 Å resolution structure of the apical domain of GroEL with a 17-residue N-terminal tag. The N-terminal tag of one molecule is bound to a neighbouring molecule in the crystal at a site that corresponds to a region previously identified by site-directed mutagenesis [21] to be involved in polypeptide binding. This appears to mimic the binding of a peptide substrate to GroEL, thereby providing the first high-resolution information on GroEL - polypeptide interactions. The conformation of the tag is extended and the binding involves both hydrophobic interactions and hydrogen bonds between sidechains of GroEL and the mainchain of the substrate.
-
(1997)
Proc Natl Acad Sci USA
, vol.94
, pp. 3571-3575
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Buckle, A.M.1
Zahn, R.2
Fersht, A.R.3
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21
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0028113299
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Residues in chaperonin GroEL required for polypeptide binding and release
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Fenton WA, Kashi Y, Furtak K, Horwich AL. Residues in chaperonin GroEL required for polypeptide binding and release. Nature. 371:1994;614-619.
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(1994)
Nature
, vol.371
, pp. 614-619
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Fenton, W.A.1
Kashi, Y.2
Furtak, K.3
Horwich, A.L.4
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22
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0028792612
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Nature and consequences of GroEL - Protein interactions
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Itzhaki LS, Otzen DE, Fersht AR. Nature and consequences of GroEL - protein interactions. Biochemistry. 34:1995;14581-14587.
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(1995)
Biochemistry
, vol.34
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Itzhaki, L.S.1
Otzen, D.E.2
Fersht, A.R.3
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23
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0000047619
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Electrostatic as well as hydrophobic interactions are important for the association of Cpn60 (groEL) with peptides
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Hutchinson JP, Oldham TC, El-Thaher TSH, Miller AD. Electrostatic as well as hydrophobic interactions are important for the association of Cpn60 (groEL) with peptides. J Chem Soc Perkin Trans. 2:1997;279-288.
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(1997)
J Chem Soc Perkin Trans
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, pp. 279-288
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Hutchinson, J.P.1
Oldham, T.C.2
El-Thaher, T.S.H.3
Miller, A.D.4
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24
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0028838951
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The hydrophobic nature of GroEL - Substrate binding
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Lin Z, Schwarz FP, Eisenstein E. The hydrophobic nature of GroEL - substrate binding. J Biol Chem. 270:1995;1011-1014.
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(1995)
J Biol Chem
, vol.270
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Lin, Z.1
Schwarz, F.P.2
Eisenstein, E.3
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25
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0030582682
-
Dominant forces in the recognition of a transient folding intermediate of α-lactalbumin by GroEL
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Katsumata K, Okazaki A, Tsurupa GP, Kuwajima K. Dominant forces in the recognition of a transient folding intermediate of α-lactalbumin by GroEL. J Mol Biol. 264:1996;643-649.
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(1996)
J Mol Biol
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Katsumata, K.1
Okazaki, A.2
Tsurupa, G.P.3
Kuwajima, K.4
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26
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0031588017
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Importance of electrostatic interactions in the rapid binding of polypeptides to GroEL
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Perrett S, Zahn R, Stenberg G, Fersht AR. Importance of electrostatic interactions in the rapid binding of polypeptides to GroEL. J Mol Biol. 269:1997;892-901.
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J Mol Biol
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Perrett, S.1
Zahn, R.2
Stenberg, G.3
Fersht, A.R.4
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27
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0031554905
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Multiple cycles of global unfolding of GroEL-bound cyclophilin A evidenced by NMR
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Nieba-Axmann SE, Ottiger M, Wüthrich K, Plückthun A. Multiple cycles of global unfolding of GroEL-bound cyclophilin A evidenced by NMR. J Mol Biol. 271:1997;803-818.
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J Mol Biol
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Nieba-Axmann, S.E.1
Ottiger, M.2
Wüthrich, K.3
Plückthun, A.4
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28
-
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0030061845
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Catalysis of amide proton exchange by the molecular chaperones GroEL and SecB
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Zahn R, Perrett S, Stenberg G, Fersht AR. Catalysis of amide proton exchange by the molecular chaperones GroEL and SecB. Science. 271:1996;642-645.
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(1996)
Science
, vol.271
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Zahn, R.1
Perrett, S.2
Stenberg, G.3
Fersht, A.R.4
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29
-
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0030576536
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Conformational states bound by the molecular chaperones GroEL and SecB: A hidden unfolding (annealing) activity
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Zahn R, Perrett S, Fersht AR. Conformational states bound by the molecular chaperones GroEL and SecB: a hidden unfolding (annealing) activity. J Mol Biol. 261:1996;43-61.
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(1996)
J Mol Biol
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Zahn, R.1
Perrett, S.2
Fersht, A.R.3
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30
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0030451744
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Significant hydrogen exchange protection in GroEL-bound DHFR is maintained during iterative rounds of substrate cycling
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Groß M, Robinson CV, Mayhew M, Hartl FU, Radford SE. Significant hydrogen exchange protection in GroEL-bound DHFR is maintained during iterative rounds of substrate cycling. Protein Sci. 5:1996;2506-2513.
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Protein Sci
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, pp. 2506-2513
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Groß, M.1
Robinson, C.V.2
Mayhew, M.3
Hartl, F.U.4
Radford, S.E.5
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31
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0031030036
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Native-like structure of a protein-folding intermediate bound to the chaperonin GroEL
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Goldberg MS, Zhang J, Sondek S, Matthews CR, Fox RO, Horwich AL. Native-like structure of a protein-folding intermediate bound to the chaperonin GroEL. Proc Natl Acad Sci USA. 94:1997;1080-1085.
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Proc Natl Acad Sci USA
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Goldberg, M.S.1
Zhang, J.2
Sondek, S.3
Matthews, C.R.4
Fox, R.O.5
Horwich, A.L.6
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32
-
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0029861712
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β-lactamase binds to GroEL in a conformation highly protected against hydrogen/deuterium exchange
-
Gervasoni P, Staudenmann W, James P, Gehrig P, Plückthun A. β-lactamase binds to GroEL in a conformation highly protected against hydrogen/deuterium exchange. Proc Natl Acad Sci USA. 93:1996;12189-12194.
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(1996)
Proc Natl Acad Sci USA
, vol.93
, pp. 12189-12194
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Gervasoni, P.1
Staudenmann, W.2
James, P.3
Gehrig, P.4
Plückthun, A.5
-
33
-
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0029837424
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A thermodynamic coupling mechanisms for GroEL-mediated unfolding
-
of special interest. This study shows that GroEL induces the unfolding of a variant of RNase T1 by shifting the equilibrium toward the unfolded state and not by catalysing unfolding.
-
of special interest Walter S, Lorimer GH, Schmid FX. A thermodynamic coupling mechanisms for GroEL-mediated unfolding. Proc Natl Acad Sci USA. 93:1996;9425-9430 This study shows that GroEL induces the unfolding of a variant of RNase T1 by shifting the equilibrium toward the unfolded state and not by catalysing unfolding.
-
(1996)
Proc Natl Acad Sci USA
, vol.93
, pp. 9425-9430
-
-
Walter, S.1
Lorimer, G.H.2
Schmid, F.X.3
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34
-
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0030992101
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Hydrogen-exchange kinetics of reduced α-lactalbumin bound to the chaperonin GroEL
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Okazaki A, Katsumata K, Kuwajima K. Hydrogen-exchange kinetics of reduced α-lactalbumin bound to the chaperonin GroEL. J Biochem. 121:1997;534-541.
-
(1997)
J Biochem
, vol.121
, pp. 534-541
-
-
Okazaki, A.1
Katsumata, K.2
Kuwajima, K.3
-
35
-
-
0030461621
-
Chaperone activity and structure of monomeric polypeptide binding domains of GroEL
-
Zahn R, Buckle AM, Perrett S, Johnson CM, Corrales FJ, Golbik R, Fersht AR. Chaperone activity and structure of monomeric polypeptide binding domains of GroEL. Proc Natl Acad Sci USA. 93:1996;15024-15029.
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(1996)
Proc Natl Acad Sci USA
, vol.93
, pp. 15024-15029
-
-
Zahn, R.1
Buckle, A.M.2
Perrett, S.3
Johnson, C.M.4
Corrales, F.J.5
Golbik, R.6
Fersht, A.R.7
-
36
-
-
0030890701
-
Refolding chromatography with immobilized mini-chaperones
-
of special interest. This paper describes a new method of refolding apparently irreversibly denatured proteins using the apical domain of GroEL immobilized to agarose either in column chromatography or batchwise.
-
of special interest Altamirano MM, Golbik R, Zahn R, Buckle AM, Fersht AR. Refolding chromatography with immobilized mini-chaperones. Proc Natl Acad Sci USA. 94:1997;3576-3578 This paper describes a new method of refolding apparently irreversibly denatured proteins using the apical domain of GroEL immobilized to agarose either in column chromatography or batchwise.
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(1997)
Proc Natl Acad Sci USA
, vol.94
, pp. 3576-3578
-
-
Altamirano, M.M.1
Golbik, R.2
Zahn, R.3
Buckle, A.M.4
Fersht, A.R.5
-
37
-
-
0028135063
-
Two lines of allosteric communication in the oligomeric chaperonin GroEL are revealed by the single mutation Arg196→Ala
-
Yifrach O, Horovitz A. Two lines of allosteric communication in the oligomeric chaperonin GroEL are revealed by the single mutation Arg196→Ala. J Mol Biol. 243:1994;397-401.
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(1994)
J Mol Biol
, vol.243
, pp. 397-401
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Yifrach, O.1
Horovitz, A.2
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38
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0029004759
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Nested cooperativity in the ATPase activity of the oligomeric chaperonin GroEL
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Yifrach O, Horovitz A. Nested cooperativity in the ATPase activity of the oligomeric chaperonin GroEL. Biochemistry. 34:1995;5303-5308.
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(1995)
Biochemistry
, vol.34
, pp. 5303-5308
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Yifrach, O.1
Horovitz, A.2
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39
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0030892675
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Is substrate inhibition a consequence of allostery in aspartate transcarbamylase?
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LiCata VJ, Allewell NM. Is substrate inhibition a consequence of allostery in aspartate transcarbamylase? Biophys Chem. 64:1997;225-234.
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(1997)
Biophys Chem
, vol.64
, pp. 225-234
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Licata, V.J.1
Allewell, N.M.2
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40
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0030726403
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Conformational changes in the GroEL oligomer during the functional cycle
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Llorca O, Marco S, Carrascosa JL, Valpuesta JM. Conformational changes in the GroEL oligomer during the functional cycle. J Struct Biol. 118:1997;31-42.
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(1997)
J Struct Biol
, vol.118
, pp. 31-42
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Llorca, O.1
Marco, S.2
Carrascosa, J.L.3
Valpuesta, J.M.4
-
41
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0031058827
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Detection of changes in pairwise interactions during allosteric transitions: Coupling between local and global conformational changes in GroEL
-
Aharoni A, Horovitz A. Detection of changes in pairwise interactions during allosteric transitions: coupling between local and global conformational changes in GroEL. Proc Natl Acad Sci USA. 94:1997;1698-1702.
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(1997)
Proc Natl Acad Sci USA
, vol.94
, pp. 1698-1702
-
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Aharoni, A.1
Horovitz, A.2
-
42
-
-
0029903725
-
GroEL locked in a closed conformation by an interdomain cross-link can bind ATP and polypeptide but cannot process further reaction steps
-
of special interest. Cross-linking of the apical domains to the equatorial domains by formation of a disulphide bridge between residues at position 83 in the equatorial domain and position 327 in the apical domain blocks the hinge motion and inhibits ATP hydrolysis, GroES binding and substrate release, thereby indicating that the hinge movements in GroEL are critical for its function.
-
of special interest Murai N, Makino Y, Yoshida M. GroEL locked in a closed conformation by an interdomain cross-link can bind ATP and polypeptide but cannot process further reaction steps. J Biol Chem. 271:1996;28229-28234 Cross-linking of the apical domains to the equatorial domains by formation of a disulphide bridge between residues at position 83 in the equatorial domain and position 327 in the apical domain blocks the hinge motion and inhibits ATP hydrolysis, GroES binding and substrate release, thereby indicating that the hinge movements in GroEL are critical for its function.
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(1996)
J Biol Chem
, vol.271
, pp. 28229-28234
-
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Murai, N.1
Makino, Y.2
Yoshida, M.3
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43
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0029664944
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The 2.4 Å crystal structure of the bacterial chaperonin GroEL complexed with ATPγS
-
Boisvert DC, Wang J, Otwinowski Z, Horwich AL, Sigler PB. The 2.4 Å crystal structure of the bacterial chaperonin GroEL complexed with ATPγS. Nat Struct Biol. 3:1996;170-177.
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(1996)
Nat Struct Biol
, vol.3
, pp. 170-177
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Boisvert, D.C.1
Wang, J.2
Otwinowski, Z.3
Horwich, A.L.4
Sigler, P.B.5
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44
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0029877893
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Inter-ring communication is disrupted in the GroEL mutant Arg13→Gly; Ala126→Val with known crystal structure
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Aharoni A, Horovitz A. Inter-ring communication is disrupted in the GroEL mutant Arg13→Gly; Ala126→Val with known crystal structure. J Mol Biol. 258:1996;732-735.
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(1996)
J Mol Biol
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Aharoni, A.1
Horovitz, A.2
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45
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0030067634
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The crystal structure of the GroES co-chaperonin at 2.8 Å resolution
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Hunt JF, Weaver AJ, Landry SJ, Gierasch L, Deisenhofer J. The crystal structure of the GroES co-chaperonin at 2.8 Å resolution. Nature. 379:1996;37-45.
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46
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Structure of the heat shock protein chaperonin-10 of Mycobacterium leprae
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Mande SC, Mehra V, Bloom BR, Hol WGJ. Structure of the heat shock protein chaperonin-10 of Mycobacterium leprae. Science. 271:1996;203-207.
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Science
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Mande, S.C.1
Mehra, V.2
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Hol, W.G.J.4
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48
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0030995661
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Nucleotide-dependent complex formation between the Escherichia coli chaperonins GroEL and GroES studied under equilibrium conditions
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Behlke J, Ristau O, Schönfeld HJ. Nucleotide-dependent complex formation between the Escherichia coli chaperonins GroEL and GroES studied under equilibrium conditions. Biochemistry. 36:1997;5149-5156.
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Biochemistry
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Behlke, J.1
Ristau, O.2
Schönfeld, H.J.3
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49
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0028785583
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Mechanism of GroEL action: Productive release of polypeptide from a sequestered position under GroES
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Weissman JS, Hohl CM, Kovalenko O, Kashi Y, Chen S, Braig K, Saibil HR, Fenton WA, Horwich AL. Mechanism of GroEL action: productive release of polypeptide from a sequestered position under GroES. Cell. 83:1995;577-587.
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Weissman, J.S.1
Hohl, C.M.2
Kovalenko, O.3
Kashi, Y.4
Chen, S.5
Braig, K.6
Saibil, H.R.7
Fenton, W.A.8
Horwich, A.L.9
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50
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0030045870
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Protein folding in the central cavity of the GroEL - GroES chaperonin complex
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Mayhew M, Da Silva ACR, Martin J, Erdjument-Bromage H, Tempst P, Hartl FU. Protein folding in the central cavity of the GroEL - GroES chaperonin complex. Nature. 379:1996;420-426.
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Nature
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Mayhew, M.1
Da Silva, A.C.R.2
Martin, J.3
Erdjument-Bromage, H.4
Tempst, P.5
Hartl, F.U.6
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51
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Binding, encapsulation and ejection: Substrate dynamics during a chaperonin-assisted folding reaction
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Ranson NA, Burston SG, Clarke AR. Binding, encapsulation and ejection: substrate dynamics during a chaperonin-assisted folding reaction. J Mol Biol. 266:1997;656-664.
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Ranson, N.A.1
Burston, S.G.2
Clarke, A.R.3
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52
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0029823985
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Release of both native and non-native proteins from a cis-only GroEL ternary complex
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of special interest. This paper shows that mixed-ring complexes provide an extremely powerful tool for analysing the role of the double-ring structure in GroEL's function. By preparing a mixed-ring GroEL complex in which only one ring is able to bind polypeptide and GroES it was shown that both native and non-native forms are released from cis ternary complexes.
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of special interest Burston SG, Weissman JS, Farr GW, Fenton WA, Horwich AL. Release of both native and non-native proteins from a cis-only GroEL ternary complex. Nature. 383:1996;96-99 This paper shows that mixed-ring complexes provide an extremely powerful tool for analysing the role of the double-ring structure in GroEL's function. By preparing a mixed-ring GroEL complex in which only one ring is able to bind polypeptide and GroES it was shown that both native and non-native forms are released from cis ternary complexes.
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(1996)
Nature
, vol.383
, pp. 96-99
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Burston, S.G.1
Weissman, J.S.2
Farr, G.W.3
Fenton, W.A.4
Horwich, A.L.5
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54
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0030334841
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2 complexes in molecular chaperone activity
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2 complexes in molecular chaperone activity. Folding Des. 1:1996;265-273.
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(1996)
Folding des
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Corrales, F.J.1
Fersht, A.R.2
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55
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0031037687
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Catalysis of protein folding by symmetric chaperone complexes
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Sparrer H, Rutkat K, Buchner J. Catalysis of protein folding by symmetric chaperone complexes. Proc Natl Acad Sci USA. 94:1997;1096-1100.
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(1997)
Proc Natl Acad Sci USA
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, pp. 1096-1100
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Sparrer, H.1
Rutkat, K.2
Buchner, J.3
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56
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0027933369
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GroEL-mediated protein folding proceeds by multiple rounds of binding and release of non-native forms
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Weissman JS, Kashi Y, Fenton WA, Horwich AL. GroEL-mediated protein folding proceeds by multiple rounds of binding and release of non-native forms. Cell. 78:1994;693-702.
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(1994)
Cell
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Weissman, J.S.1
Kashi, Y.2
Fenton, W.A.3
Horwich, A.L.4
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57
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0027179284
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Refolding of barnase in the presence of GroE
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Gray TE, Fersht AR. Refolding of barnase in the presence of GroE. J Mol Biol. 232:1993;1197-1207.
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(1993)
J Mol Biol
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Gray, T.E.1
Fersht, A.R.2
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58
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0031547963
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GroEL-mediated folding of structurally homologous dihydrofolate reductases
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Clark AC, Frieden C. GroEL-mediated folding of structurally homologous dihydrofolate reductases. J Mol Biol. 268:1997;512-525.
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(1997)
J Mol Biol
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Clark, A.C.1
Frieden, C.2
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59
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0031004530
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Protein folding: How the mechanism of GroEL action is defined by kinetics
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of special interest. An interesting discussion of issues concerning the kinetic mechanism of GroEL action. Based on their work using various DHFRs as substrates, the authors suggest that folding in the cavity occurs by the same mechanism and at the same rate as in solution.
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of special interest Frieden C, Clark AC. Protein folding: how the mechanism of GroEL action is defined by kinetics. Proc Natl Acad Sci USA. 94:1997;5535-5538 An interesting discussion of issues concerning the kinetic mechanism of GroEL action. Based on their work using various DHFRs as substrates, the authors suggest that folding in the cavity occurs by the same mechanism and at the same rate as in solution.
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(1997)
Proc Natl Acad Sci USA
, vol.94
, pp. 5535-5538
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Frieden, C.1
Clark, A.C.2
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60
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0029664316
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Toward a mechanism for GroEL - GroES chaperone activity: An ATPase-gated and -pulsed folding and annealing cage
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Corrales FJ, Fersht AR. Toward a mechanism for GroEL - GroES chaperone activity: an ATPase-gated and -pulsed folding and annealing cage. Proc Natl Acad Sci USA. 93:1996;4509-4512.
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(1996)
Proc Natl Acad Sci USA
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Corrales, F.J.1
Fersht, A.R.2
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61
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0030006212
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Chaperonin-facilitated protein folding: Optimization of rate and yield by an iterative annealing mechanism
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Tood MJ, Lorimer GH, Thirumalai D. Chaperonin-facilitated protein folding: optimization of rate and yield by an iterative annealing mechanism. Proc Natl Acad Sci USA. 93:1996;4030-4035.
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(1996)
Proc Natl Acad Sci USA
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Tood, M.J.1
Lorimer, G.H.2
Thirumalai, D.3
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62
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0029087065
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Chaperonins can catalyse the reversal of early aggregation steps when a protein misfolds
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Ranson RA, Dunster NJ, Burston SG, Clarke AR. Chaperonins can catalyse the reversal of early aggregation steps when a protein misfolds. J Mol Biol. 250:1995;581-586.
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(1995)
J Mol Biol
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Ranson, R.A.1
Dunster, N.J.2
Burston, S.G.3
Clarke, A.R.4
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63
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0030835654
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GroEL provides a folding pathway with lower apparent activation energy compared to spontaneous refolding of human carbonic anhydrase II
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Persson M, Carlsson U, Bergenhem N. GroEL provides a folding pathway with lower apparent activation energy compared to spontaneous refolding of human carbonic anhydrase II. FEBS Lett. 411:1997;43-47.
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(1997)
FEBS Lett
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Persson, M.1
Carlsson, U.2
Bergenhem, N.3
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64
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0031574908
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GroE modulates kinetic partitioning of folding intermediates between alternative states to maximize the yield of biologically active protein
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Fedorov AN, Baldwin TO. GroE modulates kinetic partitioning of folding intermediates between alternative states to maximize the yield of biologically active protein. J Mol Biol. 268:1997;712-723.
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(1997)
J Mol Biol
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Fedorov, A.N.1
Baldwin, T.O.2
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65
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0030792944
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Structural adaptations in the specialized bacteriophage T4 co-chaperonin Gp31 expand the size of the Anfinsen cage
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of special interest. This paper describes the 2.3 Å resolution structure of the co-chaperonin Gp31 which is required for the folding/assembly of the T4 major capsid protein and is able to functionally substitute for GroES in GroE-mediated folding. The paper highlights structural differences between GroES and Gp31 that may lead to expansion of the Anfinsen cage when Gp31 is in complex with GroEL.
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of special interest Hunt JF, Van der Vies SM, Henry L, Deisenhofer J. Structural adaptations in the specialized bacteriophage T4 co-chaperonin Gp31 expand the size of the Anfinsen cage. Cell. 90:1997;361-371 This paper describes the 2.3 Å resolution structure of the co-chaperonin Gp31 which is required for the folding/assembly of the T4 major capsid protein and is able to functionally substitute for GroES in GroE-mediated folding. The paper highlights structural differences between GroES and Gp31 that may lead to expansion of the Anfinsen cage when Gp31 is in complex with GroEL.
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(1997)
Cell
, vol.90
, pp. 361-371
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Hunt, J.F.1
Van Der Vies, S.M.2
Henry, L.3
Deisenhofer, J.4
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66
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0030741282
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Significance of chaperonin 10-mediated inhibition of ATP hydrolysis by chaperonin 60
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Dubaquié Y, Looser R, Rospert S. Significance of chaperonin 10-mediated inhibition of ATP hydrolysis by chaperonin 60. Proc Natl Acad Sci USA. 94:1997;9011-9016.
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(1997)
Proc Natl Acad Sci USA
, vol.94
, pp. 9011-9016
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Dubaquié, Y.1
Looser, R.2
Rospert, S.3
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67
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0030827121
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GroES promotes the T to R transition of the GroEL ring distal to GroES in the GroEL - GroES complex
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of special interest. It is shown that GroES can facilitate the release of protein substrates from both trans and cis ternary complexes with GroEL - GroES by promoting the T to R transition of the GroEL ring distal to GroES in the complex.
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of special interest Inbar E, Horovitz A. GroES promotes the T to R transition of the GroEL ring distal to GroES in the GroEL - GroES complex. Biochemistry. 36:1997;12276-12281 It is shown that GroES can facilitate the release of protein substrates from both trans and cis ternary complexes with GroEL - GroES by promoting the T to R transition of the GroEL ring distal to GroES in the complex.
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(1997)
Biochemistry
, vol.36
, pp. 12276-12281
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Inbar, E.1
Horovitz, A.2
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68
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0030936011
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ATP hydrolysis is critical for induction of conformational changes in GroEL that expose hydrophobic surfaces
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Gorovits BM, Ybarra J, Horowitz PM. ATP hydrolysis is critical for induction of conformational changes in GroEL that expose hydrophobic surfaces. J Biol Chem. 272:1997;6842-6845.
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(1997)
J Biol Chem
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Gorovits, B.M.1
Ybarra, J.2
Horowitz, P.M.3
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69
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0028031345
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Dynamics of the chaperonin ATPase cycle: Implications for facilitated protein folding
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Todd MJ, Viitanen PV, Lorimer GH. Dynamics of the chaperonin ATPase cycle: implications for facilitated protein folding. Science. 265:1994;659-666.
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(1994)
Science
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Todd, M.J.1
Viitanen, P.V.2
Lorimer, G.H.3
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70
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0030804446
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Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL
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2+ ion associated with ATP [18]. The mutation Asp398Ala inhibits ATP hydrolysis but does not affect ATP binding. By analysing the functional properties of wild type and Asp398Ala mutant single and double rings, and also mixed double rings, it is shown that ATP hydrolysin in the cis ring, and ATP binding (but not hydrolysis) in the trans ring, are necessary for the ejections of GroES from the cis side, thus allowing proteins in the cavity to be released.
-
2+ ion associated with ATP [18]. The mutation Asp398Ala inhibits ATP hydrolysis but does not affect ATP binding. By analysing the functional properties of wild type and Asp398Ala mutant single and double rings, and also mixed double rings, it is shown that ATP hydrolysin in the cis ring, and ATP binding (but not hydrolysis) in the trans ring, are necessary for the ejections of GroES from the cis side, thus allowing proteins in the cavity to be released.
-
(1997)
Nature
, vol.388
, pp. 792-798
-
-
Rye, H.S.1
Burston, S.G.2
Fenton, W.A.3
Beechem, J.M.4
Xu, Z.5
Sigler, P.B.6
Horwich, A.L.7
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71
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0029858706
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Mechanism of chaperonin action: GroES binding and release can drive GroEL-mediated protein folding in the absence of ATP hydrolysis
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Hayer-Hartl MK, Weber F, Hartl FU. Mechanism of chaperonin action: GroES binding and release can drive GroEL-mediated protein folding in the absence of ATP hydrolysis. EMBO J. 15:1996;6111-6121.
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(1996)
EMBO J
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Hayer-Hartl, M.K.1
Weber, F.2
Hartl, F.U.3
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72
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0030050614
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A quantitative assessment of the role of chaperonin proteins in protein folding in vivo
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of special interest. A theoretical analysis is presented indicating that the amount of GroEL and GroES is sufficient to facilitate the folding of no more than 5% of all the proteins in an E. coli cell.
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of special interest Lorimer GH. A quantitative assessment of the role of chaperonin proteins in protein folding in vivo. FASEB J. 10:1996;5-9 A theoretical analysis is presented indicating that the amount of GroEL and GroES is sufficient to facilitate the folding of no more than 5% of all the proteins in an E. coli cell.
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(1996)
FASEB J
, vol.10
, pp. 5-9
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Lorimer, G.H.1
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73
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0030750584
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In vivo observation of polypeptide flux through the bacterial chaperonin system
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of special interest. The contribution of the GroE system to folding in E. coli and in a cell-free translation system is analysed. It is estimated that only 10-15% of all cytoplasmic E. coli proteins interact with GroEL under normal growth conditions, whereas during heat shock a larger fraction of proteins (about 30%) interacts with GroEL.
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of special interest Ewalt KL, Hendrick JP, Houry WA, Hartl FU. In vivo observation of polypeptide flux through the bacterial chaperonin system. Cell. 90:1997;491-500 The contribution of the GroE system to folding in E. coli and in a cell-free translation system is analysed. It is estimated that only 10-15% of all cytoplasmic E. coli proteins interact with GroEL under normal growth conditions, whereas during heat shock a larger fraction of proteins (about 30%) interacts with GroEL.
-
(1997)
Cell
, vol.90
, pp. 491-500
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-
Ewalt, K.L.1
Hendrick, J.P.2
Houry, W.A.3
Hartl, F.U.4
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74
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0030844281
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Recombination of protein domains facilitated by co-translational folding in eukaryotes
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Netzer WJ, Hartl FU. Recombination of protein domains facilitated by co-translational folding in eukaryotes. Nature. 388:1997;343-349.
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(1997)
Nature
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, pp. 343-349
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Netzer, W.J.1
Hartl, F.U.2
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75
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0031030690
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The effect of macromolecular crowding on chaperonin-mediated protein folding
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Martin J, Hartl FU. The effect of macromolecular crowding on chaperonin-mediated protein folding. Proc Natl Acad Sci USA. 94:1997;1107-1112.
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(1997)
Proc Natl Acad Sci USA
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Martin, J.1
Hartl, F.U.2
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76
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0030903748
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Evidence for a lipochaperonin: Association of active protein-folding GroESL oligomers with lipids can stabilize membranes under heat shock conditions
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Török Z, Horváth I, Goloubinoff P, Kovács E, Glatz A, Balogh G, Vigh L. Evidence for a lipochaperonin: association of active protein-folding GroESL oligomers with lipids can stabilize membranes under heat shock conditions. Proc Natl Acad Sci USA. 94:1997;2192-2197.
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(1997)
Proc Natl Acad Sci USA
, vol.94
, pp. 2192-2197
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Török, Z.1
Horváth, I.2
Goloubinoff, P.3
Kovács, E.4
Glatz, A.5
Balogh, G.6
Vigh, L.7
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