-
1
-
-
84986522918
-
ICM - A new method for protein modelling and design: Applications to docking and structure prediction from the distorted native conformation
-
Abagyan RA, Totrov MM, Kuznetsov DN. 1994. ICM - A new method for protein modelling and design: Applications to docking and structure prediction from the distorted native conformation. J Comput Chem 75:488-506.
-
(1994)
J Comput Chem
, vol.75
, pp. 488-506
-
-
Abagyan, R.A.1
Totrov, M.M.2
Kuznetsov, D.N.3
-
2
-
-
0025743628
-
Computer simulation and analysis of the reaction pathway of triosephosphate isomerase
-
Bash PA, Field MJ, Davenport RC, Petsko GA, Ringe D, Karplus M. 1991. Computer simulation and analysis of the reaction pathway of triosephosphate isomerase. Biochemistry 30:5826-5832.
-
(1991)
Biochemistry
, vol.30
, pp. 5826-5832
-
-
Bash, P.A.1
Field, M.J.2
Davenport, R.C.3
Petsko, G.A.4
Ringe, D.5
Karplus, M.6
-
3
-
-
0025231512
-
How can a catalytic lesion be offset? The energetics of two pseudorevertant triosephosphate isomerases
-
Blacklow SC, Knowles JR. 1990. How can a catalytic lesion be offset? The energetics of two pseudorevertant triosephosphate isomerases. Biochemistry 25:4099-4108
-
(1990)
Biochemistry
, vol.25
, pp. 4099-4108
-
-
Blacklow, S.C.1
Knowles, J.R.2
-
4
-
-
0028049318
-
Design, creation, and characterization of a stable, monomeric triosephosphate isomerase
-
Borchert TV, Abagyan R, Jaenicke R, Wierenga RK. 1994. Design, creation, and characterization of a stable, monomeric triosephosphate isomerase. Proc Natl Acad Sci USA 97:1515-1518.
-
(1994)
Proc Natl Acad Sci USA
, vol.97
, pp. 1515-1518
-
-
Borchert, T.V.1
Abagyan, R.2
Jaenicke, R.3
Wierenga, R.K.4
-
5
-
-
0027146064
-
The crystal structure of an engineered monomeric triosephosphate isomerase, mono TIM: The correct modelling of an eight-residue loop
-
Borchert TV, Abagyan R, Radha Kishan KV, Zeelen JP, Wierenga RK. 1993a. The crystal structure of an engineered monomeric triosephosphate isomerase, mono TIM: The correct modelling of an eight-residue loop. Structure 1:205-213.
-
(1993)
Structure
, vol.1
, pp. 205-213
-
-
Borchert, T.V.1
Abagyan, R.2
Radha Kishan, K.V.3
Zeelen, J.P.4
Wierenga, R.K.5
-
6
-
-
0029645123
-
Three new structures of point mutation variants of monoTIM: Conformational flexibility of loop 1, loop 4 and loop S
-
Borchert TV, Kishan KR, Zeelen JP, Schliebs W, Thanki N, Abagyan R, Jaenicke R, Wierenga RK. 1995. Three new structures of point mutation variants of monoTIM: Conformational flexibility of loop 1, loop 4 and loop S. Structure 3:669-619.
-
(1995)
Structure
, vol.3
, pp. 669-1619
-
-
Borchert, T.V.1
Kishan, K.R.2
Zeelen, J.P.3
Schliebs, W.4
Thanki, N.5
Abagyan, R.6
Jaenicke, R.7
Wierenga, R.K.8
-
7
-
-
0027401730
-
Over-expression of trypanosomal triosephosphate isomerase in Escherichta coli and characterisation of a dimer-interface mutant
-
Borchert TV, Pratt K, Zeelen JP, Callens M, Noble MEM, Opperdoes FR, Michels PAM, Wierenga RK. 1993b. Over-expression of trypanosomal triosephosphate isomerase in Escherichta coli and characterisation of a dimer-interface mutant. Eur J Biochem 211:703-710.
-
(1993)
Eur J Biochem
, vol.211
, pp. 703-710
-
-
Borchert, T.V.1
Pratt, K.2
Zeelen, J.P.3
Callens, M.4
Noble, M.E.M.5
Opperdoes, F.R.6
Michels, P.A.M.7
Wierenga, R.K.8
-
8
-
-
0000182975
-
XL1-blue: A high efficiency plasmid transforming recA Escherichia coli strain with B-galactosidase selection
-
Bullock WO, Fernandez JM, Short JM. 1987. XL1-blue: A high efficiency plasmid transforming recA Escherichia coli strain with B-galactosidase selection. BioTechniques 5:376-378.
-
(1987)
BioTechniques
, vol.5
, pp. 376-378
-
-
Bullock, W.O.1
Fernandez, J.M.2
Short, J.M.3
-
9
-
-
0015951899
-
An activated intermediate analogue. The use of phosphoglycolohydroxamate as a stable analogue of a transiently occurring dihydroxyacetone phosphate-derived enolate in enzymatic catalysis
-
Collins KD. 1974. An activated intermediate analogue. The use of phosphoglycolohydroxamate as a stable analogue of a transiently occurring dihydroxyacetone phosphate-derived enolate in enzymatic catalysis. J Biol Chem 249:136-142.
-
(1974)
J Biol Chem
, vol.249
, pp. 136-142
-
-
Collins, K.D.1
-
10
-
-
0025882959
-
Structure of the triosephosphate isomerase-phosphoglycolohydroxamate complex: An analogue of the intermediate on the reaction pathway
-
Davenport RC, Bash PA, Seaton BA, Karplus M, Petsko GA, Ringe D. 1991. Structure of the triosephosphate isomerase-phosphoglycolohydroxamate complex: An analogue of the intermediate on the reaction pathway. Biochemisiry 30:5821-5826.
-
(1991)
Biochemisiry
, vol.30
, pp. 5821-5826
-
-
Davenport, R.C.1
Bash, P.A.2
Seaton, B.A.3
Karplus, M.4
Petsko, G.A.5
Ringe, D.6
-
11
-
-
0008890550
-
Methylglyoxal
-
Bergmeyer HU, ed. Weinheim, Germany: Verlag Chemie GmbH
-
Gawehn K, Bergmeyer HU. 1974. Methylglyoxal. In: Bergmeyer HU, ed. Methoden der enzymatischen Analyse. Weinheim, Germany: Verlag Chemie GmbH, pp 1542-1544.
-
(1974)
Methoden der Enzymatischen Analyse
, pp. 1542-1544
-
-
Gawehn, K.1
Bergmeyer, H.U.2
-
12
-
-
0001823786
-
Recombinant PCR
-
Innis MA, Gelford DH, Sninsky JJ, White TJ, eds. San Diego, California: Academic Press
-
Higuchi R. 1990. Recombinant PCR. In: Innis MA, Gelford DH, Sninsky JJ, White TJ, eds. PCR protocols: A guide to methods and applications. San Diego, California: Academic Press, pp 177-183.
-
(1990)
PCR Protocols: A Guide to Methods and Applications
, pp. 177-183
-
-
Higuchi, R.1
-
13
-
-
84889120137
-
Improved methods for building protein models in electron density maps and the location of errors in these models
-
Jones TA, Zou JY, Cowan SW, Kjeldgaard M. 1991. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr A 47:110-119.
-
(1991)
Acta Crystallogr A
, vol.47
, pp. 110-119
-
-
Jones, T.A.1
Zou, J.Y.2
Cowan, S.W.3
Kjeldgaard, M.4
-
14
-
-
0025015392
-
Anatomy of a conformational change: Hinged "lid" motion of the triosephosphate isomerase loop
-
Joseph D, Petsko GA, Karplus M. 1990. Anatomy of a conformational change: Hinged "lid" motion of the triosephosphate isomerase loop. Science 249:1425-1428.
-
(1990)
Science
, vol.249
, pp. 1425-1428
-
-
Joseph, D.1
Petsko, G.A.2
Karplus, M.3
-
15
-
-
0028210137
-
Crystal structure of the K12M/G15A triosephosphate isomerase double mutant and electrostatic analysis of the active site
-
Joseph-McCarthy D, Lolis E, Komives EA, Petsko GA. 1994. Crystal structure of the K12M/G15A triosephosphate isomerase double mutant and electrostatic analysis of the active site. Biochemistry 35:2815-2823.
-
(1994)
Biochemistry
, vol.35
, pp. 2815-2823
-
-
Joseph-McCarthy, D.1
Lolis, E.2
Komives, E.A.3
Petsko, G.A.4
-
16
-
-
0025763437
-
Enzyme catalysis: Not different, just better
-
Knowles JR. 1991. Enzyme catalysis: Not different, just better. Nature 350:121-124.
-
(1991)
Nature
, vol.350
, pp. 121-124
-
-
Knowles, J.R.1
-
17
-
-
0000283648
-
Perfection in enzyme catalysis: The energetics of triosephosphate isomerase
-
Knowles JR, Albery WJ. 1977. Perfection in enzyme catalysis: The energetics of triosephosphate isomerase. Ace Chem Res 10:105-111.
-
(1977)
Ace Chem Res
, vol.10
, pp. 105-111
-
-
Knowles, J.R.1
Albery, W.J.2
-
18
-
-
0023428359
-
Kinetic properties of triosephosphate isomerase from Trypanosoma brucei brucei. A comparison with the rabbit muscle and yeast enzymes
-
Lambeir AM, Opperdoes FR, Wierenga RK. 1987. Kinetic properties of triosephosphate isomerase from Trypanosoma brucei brucei. A comparison with the rabbit muscle and yeast enzymes. Eur J Biochem 168:69-74.
-
(1987)
Eur J Biochem
, vol.168
, pp. 69-74
-
-
Lambeir, A.M.1
Opperdoes, F.R.2
Wierenga, R.K.3
-
19
-
-
0004166184
-
-
Staines, UK: Erithacus Software Ltd
-
Leatherbarrow RJ. 1992. GraFit. Staines, UK: Erithacus Software Ltd.
-
(1992)
GraFit
-
-
Leatherbarrow, R.J.1
-
20
-
-
0017665725
-
Inhibition of fructose-1,6-biphosphate aldolase from rabbit muscle and Bacillus stearothermophilius
-
Lewis DJ, Lowe G 1977. Inhibition of fructose-1,6-biphosphate aldolase from rabbit muscle and Bacillus stearothermophilius. Eur J Biochem 80:119-133.
-
(1977)
Eur J Biochem
, vol.80
, pp. 119-133
-
-
Lewis, D.J.1
Lowe, G.2
-
21
-
-
0028296717
-
Triosephosphate isomerase requires a positively charged active site: The role of lysine-12
-
Lodi PJ, Chang LC, Knowles JR, Knowles EA. 1994. Triosephosphate isomerase requires a positively charged active site: The role of lysine-12. Biochemiitry 33:2809-2914.
-
(1994)
Biochemiitry
, vol.33
, pp. 2809-2914
-
-
Lodi, P.J.1
Chang, L.C.2
Knowles, J.R.3
Knowles, E.A.4
-
22
-
-
0025871717
-
Neutral imidazole is the electrophile in the reaction catalyzed by triosephosphate isomerase: Structural origins and catalytic implications
-
Lodi PJ, Knowles JR. 1991. Neutral imidazole is the electrophile in the reaction catalyzed by triosephosphate isomerase: Structural origins and catalytic implications. Biochemistry 30:6948-6956.
-
(1991)
Biochemistry
, vol.30
, pp. 6948-6956
-
-
Lodi, P.J.1
Knowles, J.R.2
-
23
-
-
0025331920
-
Crystallographic analysis of the complex between triosephosphate isomerase and 2-phosphoglycolate at 2.5-A resolution: Implications for catalysis
-
Lolis E, Petsko GA. 1990. Crystallographic analysis of the complex between triosephosphate isomerase and 2-phosphoglycolate at 2.5-A resolution: Implications for catalysis. Biochemistry 29:6619-6625.
-
(1990)
Biochemistry
, vol.29
, pp. 6619-6625
-
-
Lolis, E.1
Petsko, G.A.2
-
24
-
-
0024282745
-
Triosephosphate isomerase: Removal of a putatively electrophilic histidine residue results in a subtle change in catalytic mechanism
-
Nickbarg EB, Davenport RC, Petsko GA, Knowles JR. 1988. Triosephosphate isomerase: Removal of a putatively electrophilic histidine residue results in a subtle change in catalytic mechanism. Biochemistry 27:5948-5960.
-
(1988)
Biochemistry
, vol.27
, pp. 5948-5960
-
-
Nickbarg, E.B.1
Davenport, R.C.2
Petsko, G.A.3
Knowles, J.R.4
-
25
-
-
0027242141
-
Structures of the "open" and "closed" state of trypanosomal triosephosphate isomerase, as observed in a new crystal form: Implications for the reaction mechanism
-
Noble MEM, Zeelen JP, Wierenga RK. 1993. Structures of the "open" and "closed" state of trypanosomal triosephosphate isomerase, as observed in a new crystal form: Implications for the reaction mechanism. Proteins Struct Funct Genet 16:311-326.
-
(1993)
Proteins Struct Funct Genet
, vol.16
, pp. 311-326
-
-
Noble, M.E.M.1
Zeelen, J.P.2
Wierenga, R.K.3
-
26
-
-
0025276041
-
Stabilization of a reaction intermediate as a catalytic device: Definition of the functional role of the flexible loop in triosephosphate isomerase
-
Pompliano DL, Peyman A, Knowles JR. 1990. Stabilization of a reaction intermediate as a catalytic device: Definition of the functional role of the flexible loop in triosephosphate isomerase. Biochemistry 29:3186-3194.
-
(1990)
Biochemistry
, vol.29
, pp. 3186-3194
-
-
Pompliano, D.L.1
Peyman, A.2
Knowles, J.R.3
-
27
-
-
0021471746
-
Acid-base catalysis of the elimination and isomerization reactions of triose phosphates
-
Richard JP. 1984. Acid-base catalysis of the elimination and isomerization reactions of triose phosphates. J Am Chem Soc 106:4926-4936.
-
(1984)
J Am Chem Soc
, vol.106
, pp. 4926-4936
-
-
Richard, J.P.1
-
28
-
-
0023042283
-
Use of the bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes
-
Studier FW, Moffatt BA. 1986. Use of the bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. J Mol Biol 189:113-130.
-
(1986)
J Mol Biol
, vol.189
, pp. 113-130
-
-
Studier, F.W.1
Moffatt, B.A.2
-
29
-
-
0025398721
-
WHAT IF: A molecular modelling and drug design program
-
Vriend G. 1990. WHAT IF: A molecular modelling and drug design program. J Mol Graph 8:52-56.
-
(1990)
J Mol Graph
, vol.8
, pp. 52-56
-
-
Vriend, G.1
-
30
-
-
0015819192
-
Refolding of triose phosphate isomerase
-
Waley SG. 1973. Refolding of triose phosphate isomerase. Biochem J 135: 165-172.
-
(1973)
Biochem J
, vol.135
, pp. 165-172
-
-
Waley, S.G.1
-
31
-
-
0026681342
-
Crystallographic binding studies with triosephosphate isomerases: Conformational changes induced by substrate and substrate-analogues
-
Wierenga RK, Borchert TV, Noble MEM. 1992. Crystallographic binding studies with triosephosphate isomerases: Conformational changes induced by substrate and substrate-analogues. FEBS Lett 307:34-49.
-
(1992)
FEBS Lett
, vol.307
, pp. 34-49
-
-
Wierenga, R.K.1
Borchert, T.V.2
Noble, M.E.M.3
-
32
-
-
0025785056
-
Refined 1.83 a structure of trypanosomal triosephosphate isomerase crystallized in the presence of 2.4 M ammonium sulphate. A comparison with the structure of the trypanosomal triosephosphate isamerase-glycerol-S-phosphate complex
-
Wierenga RK, Noble MEM, Vriend G, Nauche S, Hol WGJ. 1991. Refined 1.83 A structure of trypanosomal triosephosphate isomerase crystallized in the presence of 2.4 M ammonium sulphate. A comparison with the structure of the trypanosomal triosephosphate isamerase-glycerol-S-phosphate complex. J Mol Biol 220:995-1015.
-
(1991)
J Mol Biol
, vol.220
, pp. 995-1015
-
-
Wierenga, R.K.1
Noble, M.E.M.2
Vriend, G.3
Nauche, S.4
Hol, W.G.J.5
-
33
-
-
0029000872
-
Dynamics of the flexible loop of triosephosphate isomerase: The loop motion is not ligand gated
-
Williams JC, McDermott AE, 1995. Dynamics of the flexible loop of triosephosphate isomerase: The loop motion is not ligand gated. Biochemistry 34:8309-8319.
-
(1995)
Biochemistry
, vol.34
, pp. 8309-8319
-
-
Williams, J.C.1
McDermott, A.E.2
-
34
-
-
0014681301
-
Transition state analogues for enzyme catalysis
-
Wolfenden R. 1969. Transition state analogues for enzyme catalysis. Nature 223:104-705.
-
(1969)
Nature
, vol.223
, pp. 104-705
-
-
Wolfenden, R.1
-
35
-
-
0019089331
-
Folding and association of triose phosphate isomerase from rabbit muscle
-
Zabori S, Rudolph R, Jaenicke R. 1980. Folding and association of triose phosphate isomerase from rabbit muscle. Z Naturforsch 35C:999-1004.
-
(1980)
Z Naturforsch
, vol.35 C
, pp. 999-1004
-
-
Zabori, S.1
Rudolph, R.2
Jaenicke, R.3
|