-
2
-
-
0037040541
-
Molecular chaperones in the cytosol: from nascent chain to folded protein
-
Hartl F.U., and Hayer-Hartl M. Molecular chaperones in the cytosol: from nascent chain to folded protein. Science 295 (2002) 1852-1858
-
(2002)
Science
, vol.295
, pp. 1852-1858
-
-
Hartl, F.U.1
Hayer-Hartl, M.2
-
4
-
-
0027943510
-
Crystal structure of GroEL at 2.8 Å
-
Braig K., Otwinowski Z., Hegde R., Boisvert D., Joachimiak A., Horwich A.L., and Sigler P.B. Crystal structure of GroEL at 2.8 Å. Nature 371 (1994) 578-586
-
(1994)
Nature
, vol.371
, pp. 578-586
-
-
Braig, K.1
Otwinowski, Z.2
Hegde, R.3
Boisvert, D.4
Joachimiak, A.5
Horwich, A.L.6
Sigler, P.B.7
-
5
-
-
0028027055
-
Location of a folding protein and shape changes in GroEL-GroES complexes imaged by cryo-electron microscopy
-
Chen S., Roseman A.M., Hunter A.S., Wood S.P., Burston S.G., Ranson N.A., Clarke A.R., and Saibil H.R. Location of a folding protein and shape changes in GroEL-GroES complexes imaged by cryo-electron microscopy. Nature 371 (1994) 261-264
-
(1994)
Nature
, vol.371
, pp. 261-264
-
-
Chen, S.1
Roseman, A.M.2
Hunter, A.S.3
Wood, S.P.4
Burston, S.G.5
Ranson, N.A.6
Clarke, A.R.7
Saibil, H.R.8
-
6
-
-
0028785583
-
Mechanism of GroEL action: productive release of polypeptide from a sequestered position under GroES
-
Weissman J.S., Hohl C.M., Kovalenko O., Chen S., Braig K., Saibil H.R., Fenton W.A., and Horwich A.L. Mechanism of GroEL action: productive release of polypeptide from a sequestered position under GroES. Cell 83 (1995) 577-587
-
(1995)
Cell
, vol.83
, pp. 577-587
-
-
Weissman, J.S.1
Hohl, C.M.2
Kovalenko, O.3
Chen, S.4
Braig, K.5
Saibil, H.R.6
Fenton, W.A.7
Horwich, A.L.8
-
7
-
-
0030067634
-
The crystal structure of the GroES co-chaperonin at 2.8 Å resolution
-
Hunt J.F., Weaver A.J., Landry S.J., Gierasch L., and Deisenhofer J. The crystal structure of the GroES co-chaperonin at 2.8 Å resolution. Nature 379 (1996) 37-45
-
(1996)
Nature
, vol.379
, pp. 37-45
-
-
Hunt, J.F.1
Weaver, A.J.2
Landry, S.J.3
Gierasch, L.4
Deisenhofer, J.5
-
8
-
-
0030056969
-
Characterization of the active intermediate of a GroEL-GroES-mediated folding reaction
-
Weissman J.S., Rye H.S., Fenton W.A., Beechem J.M., and Horwich A.L. Characterization of the active intermediate of a GroEL-GroES-mediated folding reaction. Cell 84 (1996) 481-490
-
(1996)
Cell
, vol.84
, pp. 481-490
-
-
Weissman, J.S.1
Rye, H.S.2
Fenton, W.A.3
Beechem, J.M.4
Horwich, A.L.5
-
9
-
-
0030045870
-
Protein folding in the central cavity of the GroEL-GroES chaperonin complex
-
Mayhew M., da Silva A.C.R., Martin J., Erdjument-Bromage H., Tempst P., and Hartl F.U. Protein folding in the central cavity of the GroEL-GroES chaperonin complex. Nature 379 (1996) 420-426
-
(1996)
Nature
, vol.379
, pp. 420-426
-
-
Mayhew, M.1
da Silva, A.C.R.2
Martin, J.3
Erdjument-Bromage, H.4
Tempst, P.5
Hartl, F.U.6
-
11
-
-
0033617129
-
GroEL-GroES cycling: ATP and non-native polypeptide direct alternation of folding-active rings
-
Rye H.S., Roseman A.M., Furtak K., Fenton W.A., Saibil H.R., and Horwich A.L. GroEL-GroES cycling: ATP and non-native polypeptide direct alternation of folding-active rings. Cell 97 (1999) 325-338
-
(1999)
Cell
, vol.97
, pp. 325-338
-
-
Rye, H.S.1
Roseman, A.M.2
Furtak, K.3
Fenton, W.A.4
Saibil, H.R.5
Horwich, A.L.6
-
12
-
-
0030804446
-
Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL
-
Rye H.S., Burston S.G., Fenton W.A., Beechem J.M., Xu Z., Sigler P.B., and Horwich A.L. Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL. Nature 388 (1997) 792-798
-
(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
-
13
-
-
6344277911
-
Substrate polypeptide presents a load on the apical domains of the chaperonin GroEL
-
Motojima F., Chaudhry C., Fenton W.A., Farr G.W., and Horwich A.L. Substrate polypeptide presents a load on the apical domains of the chaperonin GroEL. Proc. Natl. Acad. Sci. USA 101 (2004) 15005-15012
-
(2004)
Proc. Natl. Acad. Sci. USA
, vol.101
, pp. 15005-15012
-
-
Motojima, F.1
Chaudhry, C.2
Fenton, W.A.3
Farr, G.W.4
Horwich, A.L.5
-
14
-
-
41149089882
-
Monitoring protein conformation along the pathway of chaperonin-assisted folding
-
Sharma S., Chakraborty K., Müller B.K., Astola N., Tang Y.C., Lamb D.C., Hayer-Hartl M., and Hartl F.U. Monitoring protein conformation along the pathway of chaperonin-assisted folding. Cell 133 (2008) 142-153
-
(2008)
Cell
, vol.133
, pp. 142-153
-
-
Sharma, S.1
Chakraborty, K.2
Müller, B.K.3
Astola, N.4
Tang, Y.C.5
Lamb, D.C.6
Hayer-Hartl, M.7
Hartl, F.U.8
-
15
-
-
13244295644
-
ATP induces large quaternary rearrangements in a cage-like chaperonin structure
-
Saibil H.R., Zheng D., Roseman A.M., Hunter A.S., Watson G.M., Chen S., Auf Der Mauer A., O'Hara B.P., Wood S.P., Mann N.H., Barnett L.K., and Ellis R.J. ATP induces large quaternary rearrangements in a cage-like chaperonin structure. Curr. Biol. 3 (1993) 265-273
-
(1993)
Curr. Biol.
, vol.3
, pp. 265-273
-
-
Saibil, H.R.1
Zheng, D.2
Roseman, A.M.3
Hunter, A.S.4
Watson, G.M.5
Chen, S.6
Auf Der Mauer, A.7
O'Hara, B.P.8
Wood, S.P.9
Mann, N.H.10
Barnett, L.K.11
Ellis, R.J.12
-
16
-
-
0024820705
-
Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and MgATP
-
Goloubinoff P., Christeller J.T., Gatenby A.A., and Lorimer G.H. Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and MgATP. Nature 342 (1989) 884-889
-
(1989)
Nature
, vol.342
, pp. 884-889
-
-
Goloubinoff, P.1
Christeller, J.T.2
Gatenby, A.A.3
Lorimer, G.H.4
-
17
-
-
0141754010
-
Role of the γ-phosphate of ATP in triggering protein folding by GroEL-GroES: Function, structure, and energetics
-
Chaudhry C., Farr G.W., Todd M.J., Rye H.S., Brunger A.T., Adams P.D., Horwich A.L., and Sigler P.B. Role of the γ-phosphate of ATP in triggering protein folding by GroEL-GroES: Function, structure, and energetics. EMBO J. 22 (2003) 4877-4887
-
(2003)
EMBO J.
, vol.22
, pp. 4877-4887
-
-
Chaudhry, C.1
Farr, G.W.2
Todd, M.J.3
Rye, H.S.4
Brunger, A.T.5
Adams, P.D.6
Horwich, A.L.7
Sigler, P.B.8
-
18
-
-
0031557387
-
Binding, encapsulation and ejection: substrate dynamics during a chaperonin-assisted folding reaction
-
Ranson N.A., Burston S.G., and Clarke A.R. Binding, encapsulation and ejection: substrate dynamics during a chaperonin-assisted folding reaction. J. Mol. Biol. 266 (1997) 656-664
-
(1997)
J. Mol. Biol.
, vol.266
, pp. 656-664
-
-
Ranson, N.A.1
Burston, S.G.2
Clarke, A.R.3
-
19
-
-
0027933369
-
GroEL-mediated protein folding proceeds by multiple rounds of release and rebinding of non-native forms
-
Weissman J.S., Kashi Y., Fenton W.A., and Horwich A.L. GroEL-mediated protein folding proceeds by multiple rounds of release and rebinding of non-native forms. Cell 78 (1994) 693-702
-
(1994)
Cell
, vol.78
, pp. 693-702
-
-
Weissman, J.S.1
Kashi, Y.2
Fenton, W.A.3
Horwich, A.L.4
-
20
-
-
33847777828
-
Disulfide bond formation as probe of topology during folding in the GroEL-GroES chamber: Correct formation of long-range bonds and editing of incorrect short-range ones
-
Park E.S., Fenton W.A., and Horwich A.L. Disulfide bond formation as probe of topology during folding in the GroEL-GroES chamber: Correct formation of long-range bonds and editing of incorrect short-range ones. Proc. Natl. Acad. Sci. USA 104 (2007) 2145-2150
-
(2007)
Proc. Natl. Acad. Sci. USA
, vol.104
, pp. 2145-2150
-
-
Park, E.S.1
Fenton, W.A.2
Horwich, A.L.3
-
21
-
-
0035913902
-
Dual function of protein confinement in chaperonin-assisted protein folding
-
Brinker A., Pfeifer G., Kerner M.J., Naylor D.J., Hartl F.U., and Hayer-Hartl M. Dual function of protein confinement in chaperonin-assisted protein folding. Cell 107 (2001) 223-233
-
(2001)
Cell
, vol.107
, pp. 223-233
-
-
Brinker, A.1
Pfeifer, G.2
Kerner, M.J.3
Naylor, D.J.4
Hartl, F.U.5
Hayer-Hartl, M.6
-
22
-
-
34248349952
-
Perturbed ATPase activity and not "close confinement" of substrate in the cis cavity affects rates of folding by tail-multiplied GroEL
-
Farr G.W., Fenton W.A., and Horwich A.L. Perturbed ATPase activity and not "close confinement" of substrate in the cis cavity affects rates of folding by tail-multiplied GroEL. Proc. Natl. Acad. Sci. USA 104 (2007) 5342-5347
-
(2007)
Proc. Natl. Acad. Sci. USA
, vol.104
, pp. 5342-5347
-
-
Farr, G.W.1
Fenton, W.A.2
Horwich, A.L.3
-
23
-
-
44349090822
-
Essential role of the chaperonin folding compartment in vivo
-
Tang Y.-C., Chang H.-C., Chakraborty K., Hartl F.U., and Hayer-Hartl M. Essential role of the chaperonin folding compartment in vivo. EMBO J. 27 (2008) 1458-1468
-
(2008)
EMBO J.
, vol.27
, pp. 1458-1468
-
-
Tang, Y.-C.1
Chang, H.-C.2
Chakraborty, K.3
Hartl, F.U.4
Hayer-Hartl, M.5
-
24
-
-
33646897305
-
Structural features of the GroEL-GroES nano-cage required for rapid folding of encapsulated protein
-
Tang Y.-C., Chang H.-C., Roeben A., Wischnewski D., Wischnewski N., Kerner M.J., Hartl F.U., and Hayer-Hartl M. Structural features of the GroEL-GroES nano-cage required for rapid folding of encapsulated protein. Cell 125 (2006) 903-914
-
(2006)
Cell
, vol.125
, pp. 903-914
-
-
Tang, Y.-C.1
Chang, H.-C.2
Roeben, A.3
Wischnewski, D.4
Wischnewski, N.5
Kerner, M.J.6
Hartl, F.U.7
Hayer-Hartl, M.8
-
25
-
-
33744463129
-
Glu257 in GroEL is a sensor involved in coupling polypeptide substrate binding to stimulation of ATP hydrolysis
-
Danziger O., Shimon L., and Horovitz A. Glu257 in GroEL is a sensor involved in coupling polypeptide substrate binding to stimulation of ATP hydrolysis. Protein Sci. 15 (2006) 1270-1276
-
(2006)
Protein Sci.
, vol.15
, pp. 1270-1276
-
-
Danziger, O.1
Shimon, L.2
Horovitz, A.3
-
26
-
-
0037184939
-
Directed evolution of substrate-optimized GroEL/S chaperonins
-
Wang J.D., Herman C., Tipton K.A., Gross C.A., and Weissman J.S. Directed evolution of substrate-optimized GroEL/S chaperonins. Cell 111 (2002) 1027-1039
-
(2002)
Cell
, vol.111
, pp. 1027-1039
-
-
Wang, J.D.1
Herman, C.2
Tipton, K.A.3
Gross, C.A.4
Weissman, J.S.5
-
27
-
-
0028609655
-
Residue Lysine-34 in GroES modulates allosteric transitions in GroEL
-
Kovalenko O., Yifrach O., and Horovitz A. Residue Lysine-34 in GroES modulates allosteric transitions in GroEL. Biochemistry 33 (1994) 14974-14978
-
(1994)
Biochemistry
, vol.33
, pp. 14974-14978
-
-
Kovalenko, O.1
Yifrach, O.2
Horovitz, A.3
-
28
-
-
0028113299
-
Residues in chaperonin GroEL required for polypeptide binding and release
-
Fenton W.A., Kashi Y., Furtak K., and Horwich A.L. Residues in chaperonin GroEL required for polypeptide binding and release. Nature 371 (1994) 614-619
-
(1994)
Nature
, vol.371
, pp. 614-619
-
-
Fenton, W.A.1
Kashi, Y.2
Furtak, K.3
Horwich, A.L.4
-
30
-
-
0026416043
-
Chaperonin-mediated protein folding occurs at the surface of GroEL via a molten globule-like intermediate
-
Martin J., Langer T., Boteva R., Schramel A., Horwich A.L., and Hartl F.U. Chaperonin-mediated protein folding occurs at the surface of GroEL via a molten globule-like intermediate. Nature 352 (1991) 36-42
-
(1991)
Nature
, vol.352
, pp. 36-42
-
-
Martin, J.1
Langer, T.2
Boteva, R.3
Schramel, A.4
Horwich, A.L.5
Hartl, F.U.6
-
31
-
-
56249135270
-
Chaperonin chamber accelerates protein folding through passive action of preventing aggregation
-
Apetri A.C., and Horwich A.L. Chaperonin chamber accelerates protein folding through passive action of preventing aggregation. Proc. Natl. Acad. Sci. USA 105 (2008) 17351-17355
-
(2008)
Proc. Natl. Acad. Sci. USA
, vol.105
, pp. 17351-17355
-
-
Apetri, A.C.1
Horwich, A.L.2
-
32
-
-
0027487182
-
Folding of maltose-binding protein. Evidence for the identity of the rate-determining step in vivo and in vitro
-
Chun S.Y., Strobel S., Bassford P., and Randall L.L. Folding of maltose-binding protein. Evidence for the identity of the rate-determining step in vivo and in vitro. J. Biol. Chem. 268 (1993) 20855-20862
-
(1993)
J. Biol. Chem.
, vol.268
, pp. 20855-20862
-
-
Chun, S.Y.1
Strobel, S.2
Bassford, P.3
Randall, L.L.4
-
33
-
-
38049125649
-
Folding trajectories of human dihydrofolate reductase inside the GroEL-GroES chaperonin cavity and free in solution
-
Horst R., Fenton W.A., Englander S.W., Wüthrich K., and Horwich A.L. Folding trajectories of human dihydrofolate reductase inside the GroEL-GroES chaperonin cavity and free in solution. Proc. Natl. Acad. Sci. USA 104 (2007) 20788-20792
-
(2007)
Proc. Natl. Acad. Sci. USA
, vol.104
, pp. 20788-20792
-
-
Horst, R.1
Fenton, W.A.2
Englander, S.W.3
Wüthrich, K.4
Horwich, A.L.5
-
34
-
-
0028989966
-
Specificity in chaperonin-mediated protein folding
-
Tian G., Vainberg I.E., Tap W.D., Lewis S.A., and Cowan N.J. Specificity in chaperonin-mediated protein folding. Nature 375 (1995) 250-253
-
(1995)
Nature
, vol.375
, pp. 250-253
-
-
Tian, G.1
Vainberg, I.E.2
Tap, W.D.3
Lewis, S.A.4
Cowan, N.J.5
-
35
-
-
0026776331
-
A cytoplasmic chaperonin that catalyzes beta-actin folding
-
Gao Y., Thomas J.O., Chow R.L., Lee G.H., and Cowan N.J. A cytoplasmic chaperonin that catalyzes beta-actin folding. Cell 69 (1992) 1043-1050
-
(1992)
Cell
, vol.69
, pp. 1043-1050
-
-
Gao, Y.1
Thomas, J.O.2
Chow, R.L.3
Lee, G.H.4
Cowan, N.J.5
-
36
-
-
0026650749
-
TCP1 complex is a molecular chaperone in tubulin biogenesis
-
Yaffe M.B., Farr G.W., Miklos D., Horwich A.L., Sternlicht M.L., and Sternlicht H. TCP1 complex is a molecular chaperone in tubulin biogenesis. Nature 358 (1992) 245-248
-
(1992)
Nature
, vol.358
, pp. 245-248
-
-
Yaffe, M.B.1
Farr, G.W.2
Miklos, D.3
Horwich, A.L.4
Sternlicht, M.L.5
Sternlicht, H.6
-
37
-
-
17844378217
-
Sequential ATP-induced allosteric transitions of the cytoplasmic chaperonin containing TCP-1 revealed by EM analysis
-
Rivenzon-Segal D., Wolf S.G., Shimon L., Willison K.R., and Horovitz A. Sequential ATP-induced allosteric transitions of the cytoplasmic chaperonin containing TCP-1 revealed by EM analysis. Nat. Struct. Mol. Biol. 12 (2005) 233-237
-
(2005)
Nat. Struct. Mol. Biol.
, vol.12
, pp. 233-237
-
-
Rivenzon-Segal, D.1
Wolf, S.G.2
Shimon, L.3
Willison, K.R.4
Horovitz, A.5
-
38
-
-
0015504949
-
Role of the host cell in bacteriophage morphogenesis: effects of a bacterial mutation on T4 head assembly
-
Georgopoulos C.P., Hendrix R.W., Kaiser A.D., and Wood W.B. Role of the host cell in bacteriophage morphogenesis: effects of a bacterial mutation on T4 head assembly. Nat. New Biol. 239 (1972) 38-41
-
(1972)
Nat. New Biol.
, vol.239
, pp. 38-41
-
-
Georgopoulos, C.P.1
Hendrix, R.W.2
Kaiser, A.D.3
Wood, W.B.4
-
39
-
-
0028240858
-
Bacteriophage T4 encodes a co-chaperonin that can substitute for Escherichia coli GroES in protein folding
-
Van der Vies S.M., Gatenby A.A., and Georgopoulos C. Bacteriophage T4 encodes a co-chaperonin that can substitute for Escherichia coli GroES in protein folding. Nature 368 (1994) 654-656
-
(1994)
Nature
, vol.368
, pp. 654-656
-
-
Van der Vies, S.M.1
Gatenby, A.A.2
Georgopoulos, C.3
-
40
-
-
0030792944
-
Structural adaptations in the specialized bacteriophage T4 co-chaperonin Gp31 expand the size of the Anfinsen cage
-
Hunt J.F., van der Vies S.M., Henry L., and Deisenhofer J. Structural adaptations in the specialized bacteriophage T4 co-chaperonin Gp31 expand the size of the Anfinsen cage. Cell 90 (1997) 361-371
-
(1997)
Cell
, vol.90
, pp. 361-371
-
-
Hunt, J.F.1
van der Vies, S.M.2
Henry, L.3
Deisenhofer, J.4
-
41
-
-
20444424595
-
The T4-encoded cochaperonin, gp31, has unique properties that explain its requirement for the folding of the T4 major capsid protein
-
Bakkes P.J., Faber B.W., van Heerikhuizen H., and van der Vies S.M. The T4-encoded cochaperonin, gp31, has unique properties that explain its requirement for the folding of the T4 major capsid protein. Proc. Natl. Acad. Sci. USA 102 (2005) 8144-8149
-
(2005)
Proc. Natl. Acad. Sci. USA
, vol.102
, pp. 8144-8149
-
-
Bakkes, P.J.1
Faber, B.W.2
van Heerikhuizen, H.3
van der Vies, S.M.4
-
42
-
-
58149229533
-
Chaperonin complex with a newly folded protein encapsulated in the folding chamber
-
Clare D.K., Bakkes P.J., van Heerikhuizen H., van der Vies S.M., and Saibil H.R. Chaperonin complex with a newly folded protein encapsulated in the folding chamber. Nature 457 (2009) 107-110
-
(2009)
Nature
, vol.457
, pp. 107-110
-
-
Clare, D.K.1
Bakkes, P.J.2
van Heerikhuizen, H.3
van der Vies, S.M.4
Saibil, H.R.5
-
43
-
-
0036747242
-
Bacteriophage-encoded cochaperonins can substitute for Escherichia coli's essential GroES protein
-
Keppel F., Rychner M., and Georgopoulos C. Bacteriophage-encoded cochaperonins can substitute for Escherichia coli's essential GroES protein. EMBO Rep. 3 (2002) 893-898
-
(2002)
EMBO Rep.
, vol.3
, pp. 893-898
-
-
Keppel, F.1
Rychner, M.2
Georgopoulos, C.3
-
44
-
-
0037120882
-
Solution NMR techniques for very large molecular and supramolecular structures
-
Riek R., Fiaux J., Bertelsen E.B., Horwich A.L., and Wüthrich K. Solution NMR techniques for very large molecular and supramolecular structures. J. Am. Chem. Soc. 124 (2002) 12144-12153
-
(2002)
J. Am. Chem. Soc.
, vol.124
, pp. 12144-12153
-
-
Riek, R.1
Fiaux, J.2
Bertelsen, E.B.3
Horwich, A.L.4
Wüthrich, K.5
-
45
-
-
33847635621
-
Concerted ATP-induced allosteric transitions in GroEL facilitate release of protein substrate domains in an all-or-none manner
-
Kipnis Y., Papo N., Haran G., and Horovitz A. Concerted ATP-induced allosteric transitions in GroEL facilitate release of protein substrate domains in an all-or-none manner. Proc. Natl. Acad. Sci. USA 104 (2007) 3119-3124
-
(2007)
Proc. Natl. Acad. Sci. USA
, vol.104
, pp. 3119-3124
-
-
Kipnis, Y.1
Papo, N.2
Haran, G.3
Horovitz, A.4
-
46
-
-
45649083920
-
Concerted release of substrate domains from GroEL by ATP is demonstrated with FRET
-
Papo N., Kipnis Y., Haran G., and Horovitz A. Concerted release of substrate domains from GroEL by ATP is demonstrated with FRET. J. Mol. Biol. 380 (2008) 717-725
-
(2008)
J. Mol. Biol.
, vol.380
, pp. 717-725
-
-
Papo, N.1
Kipnis, Y.2
Haran, G.3
Horovitz, A.4
-
47
-
-
2442482377
-
GroEL mediates protein holding with a two successive timer mechanism
-
Ueno T., Taguchi H., Yoshida M., and Funatsu T. GroEL mediates protein holding with a two successive timer mechanism. Mol. Cell 14 (2004) 423-434
-
(2004)
Mol. Cell
, vol.14
, pp. 423-434
-
-
Ueno, T.1
Taguchi, H.2
Yoshida, M.3
Funatsu, T.4
-
48
-
-
0035966323
-
ATP-bound states of GroEL captured by cryo-electron microscopy
-
Ranson N.A., Farr G.W., Roseman A.M., Gowen B., Fenton W.A., Horwich A.L., and Saibil H.R. ATP-bound states of GroEL captured by cryo-electron microscopy. Cell 107 (2001) 869-879
-
(2001)
Cell
, vol.107
, pp. 869-879
-
-
Ranson, N.A.1
Farr, G.W.2
Roseman, A.M.3
Gowen, B.4
Fenton, W.A.5
Horwich, A.L.6
Saibil, H.R.7
|