-
1
-
-
0023644310
-
Structure of holo-glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus at 1.8 Å resolution
-
Skarzynski T., Moody P.C., Wonacott A.J. Structure of holo-glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus at 1.8 Å resolution. J. Mol. Biol. 193:1987;171-187.
-
(1987)
J. Mol. Biol.
, vol.193
, pp. 171-187
-
-
Skarzynski, T.1
Moody, P.C.2
Wonacott, A.J.3
-
2
-
-
0023717499
-
Coenzyme-induced conformational changes in glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus
-
Skarzynski T., Wonacott A.J. Coenzyme-induced conformational changes in glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus. J. Mol. Biol. 203:1988;1097-1118.
-
(1988)
J. Mol. Biol.
, vol.203
, pp. 1097-1118
-
-
Skarzynski, T.1
Wonacott, A.J.2
-
3
-
-
0033534147
-
Dimers generated from tetrameric phosphorylating glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus are inactive but exhibit cooperativity in NAD binding
-
Roitel O., Sergienko E., Branlant G. Dimers generated from tetrameric phosphorylating glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus are inactive but exhibit cooperativity in NAD binding. Biochemistry. 38:1999;16084-16091.
-
(1999)
Biochemistry
, vol.38
, pp. 16084-16091
-
-
Roitel, O.1
Sergienko, E.2
Branlant, G.3
-
4
-
-
0037129983
-
Thermal unfolding used as a probe to characterize the intra- and intersubunit stabilizing interactions in phosphorylating D-glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus
-
Roitel O., Ivinova O., Muronetz V., Nagradova N., Branlant G. Thermal unfolding used as a probe to characterize the intra- and intersubunit stabilizing interactions in phosphorylating D-glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus. Biochemistry. 41:2002;7556-7564.
-
(2002)
Biochemistry
, vol.41
, pp. 7556-7564
-
-
Roitel, O.1
Ivinova, O.2
Muronetz, V.3
Nagradova, N.4
Branlant, G.5
-
5
-
-
0038058016
-
Comparison of the structures of wild-type and a N313T mutant of Escherichia coli glyceraldehyde 3-phosphate dehydrogenases: Implication for NAD binding and cooperativity
-
Duee E., Olivier-Deyris L., Fanchon E., Corbier C., Branlant G., Dideberg O. Comparison of the structures of wild-type and a N313T mutant of Escherichia coli glyceraldehyde 3-phosphate dehydrogenases: implication for NAD binding and cooperativity. J. Mol. Biol. 257:1996;814-838.
-
(1996)
J. Mol. Biol.
, vol.257
, pp. 814-838
-
-
Duee, E.1
Olivier-Deyris, L.2
Fanchon, E.3
Corbier, C.4
Branlant, G.5
Dideberg, O.6
-
6
-
-
84944815124
-
Small-angle-scattering-data treatment by the regularization method
-
Svergun D., Semenyuk, Feigin L.A. Small-angle-scattering-data treatment by the regularization method. Acta Crystallog. sect., A. 44:1988;244-250.
-
(1988)
Acta Crystallog. sect., A
, vol.44
, pp. 244-250
-
-
Svergun, D.1
Semenyuk2
Feigin, L.A.3
-
7
-
-
0020407335
-
Affinity labeling of glyceraldehyde-3-phosphate dehydrogenase from sturgeon and Bacillus stearothermophilus by 3-chloroacetylpyridine-adenine dinucleotide. Kinetic Studies
-
Branlant G., Eiler B., Wallen L., Biellmann J.F. Affinity labeling of glyceraldehyde-3-phosphate dehydrogenase from sturgeon and Bacillus stearothermophilus by 3-chloroacetylpyridine-adenine dinucleotide. Kinetic Studies. Eur. J. Biochem. 127:1982;519-524.
-
(1982)
Eur. J. Biochem.
, vol.127
, pp. 519-524
-
-
Branlant, G.1
Eiler, B.2
Wallen, L.3
Biellmann, J.F.4
-
8
-
-
0032521628
-
Comparative study of the catalytic domain of phosphorylating glyceraldehyde-3-phosphate dehydrogenases from bacteria and archaea via essential cysteine probes and site-directed mutagenesis
-
Talfournier F., Colloc'h N., Mornon J.P., Branlant G. Comparative study of the catalytic domain of phosphorylating glyceraldehyde-3-phosphate dehydrogenases from bacteria and archaea via essential cysteine probes and site-directed mutagenesis. Eur. J. Biochem. 252:1998;447-457.
-
(1998)
Eur. J. Biochem.
, vol.252
, pp. 447-457
-
-
Talfournier, F.1
Colloc'h, N.2
Mornon, J.P.3
Branlant, G.4
-
9
-
-
0024555940
-
Role of the histidine 176 residue in glyceraldehyde-3-phosphate dehydrogenase as probed by site-directed mutagenesis
-
Soukri A., Mougin A., Corbier C., Wonacott A., Branlant C., Branlant G. Role of the histidine 176 residue in glyceraldehyde-3-phosphate dehydrogenase as probed by site-directed mutagenesis. Biochemistry. 28:1989;2586-2592.
-
(1989)
Biochemistry
, vol.28
, pp. 2586-2592
-
-
Soukri, A.1
Mougin, A.2
Corbier, C.3
Wonacott, A.4
Branlant, C.5
Branlant, G.6
-
10
-
-
0025197777
-
The nicotinamide subsite of glyceraldehyde-3-phosphate dehydrogenase studied by site-directed mutagenesis
-
Corbier C., Mougin A., Mely Y., Adolph H.W., Zeppezauer M., Gerard D., et al. The nicotinamide subsite of glyceraldehyde-3-phosphate dehydrogenase studied by site-directed mutagenesis. Biochimie. 72:1990;545-554.
-
(1990)
Biochimie
, vol.72
, pp. 545-554
-
-
Corbier, C.1
Mougin, A.2
Mely, Y.3
Adolph, H.W.4
Zeppezauer, M.5
Gerard, D.6
-
11
-
-
0027383390
-
Determinants of coenzyme specificity in glyceraldehyde-3-phosphate dehydrogenase: Role of the acidic residue in the fingerprint region of the nucleotide binding fold
-
Clermont S., Corbier C., Mely Y., Gerard D., Wonacott A., Branlant G. Determinants of coenzyme specificity in glyceraldehyde-3-phosphate dehydrogenase: role of the acidic residue in the fingerprint region of the nucleotide binding fold. Biochemistry. 32:1993;10178-10184.
-
(1993)
Biochemistry
, vol.32
, pp. 10178-10184
-
-
Clermont, S.1
Corbier, C.2
Mely, Y.3
Gerard, D.4
Wonacott, A.5
Branlant, G.6
-
12
-
-
0013863816
-
Comparison of experimental binding data and theoretical models in proteins containing subunits
-
Koshland D.E. Jr, Nemethy G., Filmer D. Comparison of experimental binding data and theoretical models in proteins containing subunits. Biochemistry. 5:1966;365-385.
-
(1966)
Biochemistry
, vol.5
, pp. 365-385
-
-
Koshland D.E., Jr.1
Nemethy, G.2
Filmer, D.3
-
13
-
-
0001195192
-
The binding of nicotinamide-adenine dinucleotide to D-glyceraldehyde-3-phosphate dehydrogenase: Temperature jump relaxation studies on the mechanism of an allosteric enzyme
-
Kirschner K., Eigen M., Bittman R., Voigt B. The binding of nicotinamide-adenine dinucleotide to D-glyceraldehyde-3-phosphate dehydrogenase: temperature jump relaxation studies on the mechanism of an allosteric enzyme. Proc. Natl. Acad. Sci. USA. 56:1966;1661-1667.
-
(1966)
Proc. Natl. Acad. Sci. USA
, vol.56
, pp. 1661-1667
-
-
Kirschner, K.1
Eigen, M.2
Bittman, R.3
Voigt, B.4
-
14
-
-
0014954234
-
Positive and negative cooperativity in yeast glyceraldehyde 3-phosphate dehydrogenase
-
Cook R.A., Koshland D.E. Jr. Positive and negative cooperativity in yeast glyceraldehyde 3-phosphate dehydrogenase. Biochemistry. 9:1970;3337-3342.
-
(1970)
Biochemistry
, vol.9
, pp. 3337-3342
-
-
Cook, R.A.1
Koshland D.E., Jr.2
-
15
-
-
0015243230
-
Co-operative binding of nicotinamide-adenine dinucleotide to yeast glyceraldehyde-3-phosphate dehydrogenase. II. Stopped-flow studies at pH 8-5 and 40 degrees C
-
Kirschner K. Co-operative binding of nicotinamide-adenine dinucleotide to yeast glyceraldehyde-3-phosphate dehydrogenase. II. Stopped-flow studies at pH 8-5 and 40 degrees C. J. Mol. Biol. 58:1971;51-68.
-
(1971)
J. Mol. Biol.
, vol.58
, pp. 51-68
-
-
Kirschner, K.1
-
16
-
-
0016776237
-
The binding of nicotinamide-adenine dimucleotide to glyceraldehyde 3-phosphate dehydrogenase from Bacillus stearothermophilus
-
Allen G., Harris J.I. The binding of nicotinamide-adenine dimucleotide to glyceraldehyde 3-phosphate dehydrogenase from Bacillus stearothermophilus. Biochem. J. 151:1975;747-749.
-
(1975)
Biochem. J.
, vol.151
, pp. 747-749
-
-
Allen, G.1
Harris, J.I.2
-
17
-
-
0017132753
-
Negative homotropic cooperativity and affinity heterogeneity: Preparation of yeast glyceraldehyde-3-phosphate dehydrogenase with maximal affinity homogeneity
-
Gennis L.S. Negative homotropic cooperativity and affinity heterogeneity: preparation of yeast glyceraldehyde-3-phosphate dehydrogenase with maximal affinity homogeneity. Proc. Natl Acad. Sci. USA. 73:1976;3928-3932.
-
(1976)
Proc. Natl Acad. Sci. USA
, vol.73
, pp. 3928-3932
-
-
Gennis, L.S.1
-
18
-
-
0020513891
-
Coenzyme binding in crystals of glyceraldehyde-3-phosphate dehydrogenase
-
Leslie A.G., Wonacott A.J. Coenzyme binding in crystals of glyceraldehyde-3-phosphate dehydrogenase. J. Mol. Biol. 165:1983;375-391.
-
(1983)
J. Mol. Biol.
, vol.165
, pp. 375-391
-
-
Leslie, A.G.1
Wonacott, A.J.2
-
19
-
-
0035311517
-
Mass spectrometry as a novel approach to probe cooperativity in multimeric enzymatic systems
-
Rogniaux H., Sanglier S., Strupat K., Azza S., Roitel O., Ball V., et al. Mass spectrometry as a novel approach to probe cooperativity in multimeric enzymatic systems. Anal. Biochem. 291:2001;48-61.
-
(2001)
Anal. Biochem.
, vol.291
, pp. 48-61
-
-
Rogniaux, H.1
Sanglier, S.2
Strupat, K.3
Azza, S.4
Roitel, O.5
Ball, V.6
-
20
-
-
0037174921
-
A key structural role for active site type 3 copper ions in human ceruloplasmin
-
Vachette P., Dainese E., Vasyliev V.B., DiMuro P., Beltramini M., Svergun D.I., et al. A key structural role for active site type 3 copper ions in human ceruloplasmin. J. Biol. Chem. 277:2002;40823-40831.
-
(2002)
J. Biol. Chem.
, vol.277
, pp. 40823-40831
-
-
Vachette, P.1
Dainese, E.2
Vasyliev, V.B.3
DiMuro, P.4
Beltramini, M.5
Svergun, D.I.6
-
21
-
-
0029095399
-
X-ray scattering titration of the quaternary structure transition of aspartate transcarbamylase with a bisubstrate analogue: Influence of nucleotide effectors
-
Fetler L., Tauc P., Herve G., Moody M.F., Vachette P. X-ray scattering titration of the quaternary structure transition of aspartate transcarbamylase with a bisubstrate analogue: influence of nucleotide effectors. J. Mol. Biol. 251:1995;243-255.
-
(1995)
J. Mol. Biol.
, vol.251
, pp. 243-255
-
-
Fetler, L.1
Tauc, P.2
Herve, G.3
Moody, M.F.4
Vachette, P.5
-
22
-
-
0035827220
-
The allosteric activator Mg-ATP modifies the quaternary structure of the R-state of Escherichia coli aspartate transcarbamylase without altering the T↔R equilibrium
-
Fetler L., Vachette P. The allosteric activator Mg-ATP modifies the quaternary structure of the R-state of Escherichia coli aspartate transcarbamylase without altering the T↔R equilibrium. J. Mol. Biol. 309:2001;817-832.
-
(2001)
J. Mol. Biol.
, vol.309
, pp. 817-832
-
-
Fetler, L.1
Vachette, P.2
-
23
-
-
0025328922
-
Probing the coenzyme specificity of glyceraldehyde-3-phosphate dehydrogenases by site-directed mutagenesis
-
Corbier C., Clermont S., Billard P., Skarzynski T., Branlant C., Wonacott A., Branlant G. Probing the coenzyme specificity of glyceraldehyde-3-phosphate dehydrogenases by site-directed mutagenesis. Biochemistry. 29:1990;7101-7106.
-
(1990)
Biochemistry
, vol.29
, pp. 7101-7106
-
-
Corbier, C.1
Clermont, S.2
Billard, P.3
Skarzynski, T.4
Branlant, C.5
Wonacott, A.6
Branlant, G.7
-
24
-
-
0022787110
-
Data appraisal, evaluation and display for synchrotron radiation experiments: Hardware and software
-
Boulin C., Kempf R., Koch M.H.J., McLaughlin S.M. Data appraisal, evaluation and display for synchrotron radiation experiments: hardware and software. Nucl. Instrum. Meth. A249:1986;399-407.
-
(1986)
Nucl. Instrum. Meth.
, vol.A249
, pp. 399-407
-
-
Boulin, C.1
Kempf, R.2
Koch, M.H.J.3
McLaughlin, S.M.4
-
25
-
-
0342511969
-
Improved signal-to-background ratio in small-angle X-ray scattering experiments with synchrotron radiation using an evacuated cell for solutions
-
Dubuisson J.M., Decamps T., Vachette P. Improved signal-to-background ratio in small-angle X-ray scattering experiments with synchrotron radiation using an evacuated cell for solutions. J. Appl. Crystallog. 30:1997;49-54.
-
(1997)
J. Appl. Crystallog.
, vol.30
, pp. 49-54
-
-
Dubuisson, J.M.1
Decamps, T.2
Vachette, P.3
-
27
-
-
0029185933
-
CRYSOL - A program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates
-
Svergun D.I., Barberato C., Koch M.H.J. CRYSOL - a program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates. J. Appl. Crystallog. 28:1995;768-773.
-
(1995)
J. Appl. Crystallog.
, vol.28
, pp. 768-773
-
-
Svergun, D.I.1
Barberato, C.2
Koch, M.H.J.3
|