-
1
-
-
0032104477
-
How far divergent evolution goes in proteins
-
Murzin A.G. How far divergent evolution goes in proteins. Curr Opin Struct Biol 8 (1998) 380-387
-
(1998)
Curr Opin Struct Biol
, vol.8
, pp. 380-387
-
-
Murzin, A.G.1
-
2
-
-
0035783063
-
Fold change in evolution of protein structures
-
Grishin N.V. Fold change in evolution of protein structures. J Struct Biol 134 (2001) 167-185
-
(2001)
J Struct Biol
, vol.134
, pp. 167-185
-
-
Grishin, N.V.1
-
3
-
-
0038148710
-
Conformational diversity and protein evolution - a 60-year-old hypothesis revisited
-
James L.C., and Tawfik D.S. Conformational diversity and protein evolution - a 60-year-old hypothesis revisited. Trends Biochem Sci 28 (2003) 361-368
-
(2003)
Trends Biochem Sci
, vol.28
, pp. 361-368
-
-
James, L.C.1
Tawfik, D.S.2
-
4
-
-
23444459516
-
Connecting the protein structure universe by using sparse recurring fragments
-
Friedberg I., and Godzik A. Connecting the protein structure universe by using sparse recurring fragments. Structure 13 (2005) 1213-1224
-
(2005)
Structure
, vol.13
, pp. 1213-1224
-
-
Friedberg, I.1
Godzik, A.2
-
5
-
-
31144467558
-
The impact of structural genomics: expectations and outcomes
-
An insider review of the completion of phase one of the Protein Structure Initiative.
-
Chandonia J.M., and Brenner S.E. The impact of structural genomics: expectations and outcomes. Science 311 (2006) 347-351. An insider review of the completion of phase one of the Protein Structure Initiative.
-
(2006)
Science
, vol.311
, pp. 347-351
-
-
Chandonia, J.M.1
Brenner, S.E.2
-
6
-
-
26944452855
-
Giving credit where credit is due
-
•], we wish to express our support for the proposal to assign a document object identifier (DOI) to each PDB entry, so that structures deposited in the PDB can be referenced and accessed in the same manner as other electronic publications. Meanwhile, we list here the PDB identifiers of all currently unpublished structures discussed in this review: 1txn, 1p8c, 1vke, 1tjn.
-
•], we wish to express our support for the proposal to assign a document object identifier (DOI) to each PDB entry, so that structures deposited in the PDB can be referenced and accessed in the same manner as other electronic publications. Meanwhile, we list here the PDB identifiers of all currently unpublished structures discussed in this review: 1txn, 1p8c, 1vke, 1tjn.
-
(2005)
Nat Struct Mol Biol
, vol.12
, pp. 634
-
-
Wlodawer, A.1
-
8
-
-
0029865623
-
Context-dependent secondary structure formation of a designed protein sequence
-
Minor Jr. D.L., and Kim P.S. Context-dependent secondary structure formation of a designed protein sequence. Nature 380 (1996) 730-734
-
(1996)
Nature
, vol.380
, pp. 730-734
-
-
Minor Jr., D.L.1
Kim, P.S.2
-
9
-
-
4444340508
-
The solution structure of a chimeric LEKTI domain reveals a chameleon sequence
-
Tidow H., Lauber T., Vitzithum K., Sommerhoff C.P., Rosch P., and Marx U.C. The solution structure of a chimeric LEKTI domain reveals a chameleon sequence. Biochemistry 43 (2004) 11238-11247
-
(2004)
Biochemistry
, vol.43
, pp. 11238-11247
-
-
Tidow, H.1
Lauber, T.2
Vitzithum, K.3
Sommerhoff, C.P.4
Rosch, P.5
Marx, U.C.6
-
10
-
-
0036161468
-
The Mad2 spindle checkpoint protein undergoes similar major conformational changes upon binding to either Mad1 or Cdc20
-
Luo X., Tang Z., Rizo J., and Yu H. The Mad2 spindle checkpoint protein undergoes similar major conformational changes upon binding to either Mad1 or Cdc20. Mol Cell 9 (2002) 59-71
-
(2002)
Mol Cell
, vol.9
, pp. 59-71
-
-
Luo, X.1
Tang, Z.2
Rizo, J.3
Yu, H.4
-
11
-
-
1842420626
-
The Mad2 spindle checkpoint protein has two distinct natively folded states
-
Mad2 is a relatively small, single-domain protein that shows some prion-like properties. A transiently formed heterodimer of the N1-Mad2 and N2-Mad2 conformers is converted into the wild-type N2-Mad2 homodimer. The N2-Mad2 solution structure has been determined using a monomeric mutant.
-
Luo X., Tang Z., Xia G., Wassmann K., Matsumoto T., Rizo J., and Yu H. The Mad2 spindle checkpoint protein has two distinct natively folded states. Nat Struct Mol Biol 11 (2004) 338-345. Mad2 is a relatively small, single-domain protein that shows some prion-like properties. A transiently formed heterodimer of the N1-Mad2 and N2-Mad2 conformers is converted into the wild-type N2-Mad2 homodimer. The N2-Mad2 solution structure has been determined using a monomeric mutant.
-
(2004)
Nat Struct Mol Biol
, vol.11
, pp. 338-345
-
-
Luo, X.1
Tang, Z.2
Xia, G.3
Wassmann, K.4
Matsumoto, T.5
Rizo, J.6
Yu, H.7
-
12
-
-
0037093326
-
Crystal structure of the tetrameric Mad1-Mad2 core complex: implications of a 'safety belt' binding mechanism for the spindle checkpoint
-
Sironi L., Mapelli M., Knapp S., De Antoni A., Jeang K.T., and Musacchio A. Crystal structure of the tetrameric Mad1-Mad2 core complex: implications of a 'safety belt' binding mechanism for the spindle checkpoint. EMBO J 21 (2002) 2496-2506
-
(2002)
EMBO J
, vol.21
, pp. 2496-2506
-
-
Sironi, L.1
Mapelli, M.2
Knapp, S.3
De Antoni, A.4
Jeang, K.T.5
Musacchio, A.6
-
14
-
-
18944394158
-
The AXH domain adopts alternative folds: the solution structure of HBP1 AXH
-
•]. The discovery of unexpected structural diversity of this domain is a bonus.
-
•]. The discovery of unexpected structural diversity of this domain is a bonus.
-
(2005)
Structure
, vol.13
, pp. 743-753
-
-
de Chiara, C.1
Menon, R.P.2
Adinolfi, S.3
de Boer, J.4
Ktistaki, E.5
Kelly, G.6
Calder, L.7
Kioussis, D.8
Pastore, A.9
-
15
-
-
4143121188
-
Structure of the N-terminal domain of the circadian clock-associated histidine kinase SasA
-
Vakonakis I., Klewer D.A., Williams S.B., Golden S.S., and LiWang A.C. Structure of the N-terminal domain of the circadian clock-associated histidine kinase SasA. J Mol Biol 342 (2004) 9-17
-
(2004)
J Mol Biol
, vol.342
, pp. 9-17
-
-
Vakonakis, I.1
Klewer, D.A.2
Williams, S.B.3
Golden, S.S.4
LiWang, A.C.5
-
16
-
-
2442569769
-
Anabaena circadian clock proteins KaiA and KaiB reveal a potential common binding site to their partner KaiC
-
Garces R.G., Wu N., Gillon W., and Pai E.F. Anabaena circadian clock proteins KaiA and KaiB reveal a potential common binding site to their partner KaiC. EMBO J 23 (2004) 1688-1698
-
(2004)
EMBO J
, vol.23
, pp. 1688-1698
-
-
Garces, R.G.1
Wu, N.2
Gillon, W.3
Pai, E.F.4
-
17
-
-
21444458211
-
Tetrameric architecture of the circadian clock protein KaiB. A novel interface for intermolecular interactions and its impact on the circadian rhythm
-
Hitomi K., Oyama T., Han S., Arvai A.S., and Getzoff E.D. Tetrameric architecture of the circadian clock protein KaiB. A novel interface for intermolecular interactions and its impact on the circadian rhythm. J Biol Chem 280 (2005) 19127-19135
-
(2005)
J Biol Chem
, vol.280
, pp. 19127-19135
-
-
Hitomi, K.1
Oyama, T.2
Han, S.3
Arvai, A.S.4
Getzoff, E.D.5
-
18
-
-
30044441280
-
Functionally important substructures of circadian clock protein KaiB in a unique tetramer complex
-
Iwase R., Imada K., Hayashi F., Uzumaki T., Morishita M., Onai K., Furukawa Y., Namba K., and Ishiura M. Functionally important substructures of circadian clock protein KaiB in a unique tetramer complex. J Biol Chem 280 (2005) 43141-43149
-
(2005)
J Biol Chem
, vol.280
, pp. 43141-43149
-
-
Iwase, R.1
Imada, K.2
Hayashi, F.3
Uzumaki, T.4
Morishita, M.5
Onai, K.6
Furukawa, Y.7
Namba, K.8
Ishiura, M.9
-
19
-
-
4644367297
-
Crystal structure of the oxygen-dependant coproporphyrinogen oxidase (Hem13p) of Saccharomyces cerevisiae
-
Phillips J.D., Whitby F.G., Warby C.A., Labbe P., Yang C., Pflugrath J.W., Ferrara J.D., Robinson H., Kushner J.P., and Hill C.P. Crystal structure of the oxygen-dependant coproporphyrinogen oxidase (Hem13p) of Saccharomyces cerevisiae. J Biol Chem 279 (2004) 38960-38968
-
(2004)
J Biol Chem
, vol.279
, pp. 38960-38968
-
-
Phillips, J.D.1
Whitby, F.G.2
Warby, C.A.3
Labbe, P.4
Yang, C.5
Pflugrath, J.W.6
Ferrara, J.D.7
Robinson, H.8
Kushner, J.P.9
Hill, C.P.10
-
20
-
-
26444584539
-
Structural basis of hereditary coproporphyria
-
Lee D.S., Flachsova E., Bodnarova M., Demeler B., Martasek P., and Raman C.S. Structural basis of hereditary coproporphyria. Proc Natl Acad Sci USA 102 (2005) 14232-14237
-
(2005)
Proc Natl Acad Sci USA
, vol.102
, pp. 14232-14237
-
-
Lee, D.S.1
Flachsova, E.2
Bodnarova, M.3
Demeler, B.4
Martasek, P.5
Raman, C.S.6
-
21
-
-
13444291040
-
A segment of cold shock protein directs the folding of a combinatorial protein
-
This paper reports the first structure of an artificial protein from the set of novel folded domains generated by random shuffling of non-homologous polypeptide segments and discusses its evolutionary implications.
-
de Bono S., Riechmann L., Girard E., Williams R.L., and Winter G. A segment of cold shock protein directs the folding of a combinatorial protein. Proc Natl Acad Sci USA 102 (2005) 1396-1401. This paper reports the first structure of an artificial protein from the set of novel folded domains generated by random shuffling of non-homologous polypeptide segments and discusses its evolutionary implications.
-
(2005)
Proc Natl Acad Sci USA
, vol.102
, pp. 1396-1401
-
-
de Bono, S.1
Riechmann, L.2
Girard, E.3
Williams, R.L.4
Winter, G.5
-
22
-
-
18044393058
-
Folding and stability of a primitive protein
-
••]. They confirm that segment swapping and associated oligomerisation are both powerful ways of stabilising proteins, supporting the view that this may have been a feature of early protein evolution.
-
••]. They confirm that segment swapping and associated oligomerisation are both powerful ways of stabilising proteins, supporting the view that this may have been a feature of early protein evolution.
-
(2005)
J Mol Biol
, vol.348
, pp. 1261-1272
-
-
Riechmann, L.1
Lavenir, I.2
de Bono, S.3
Winter, G.4
-
23
-
-
0032874536
-
The evolutionary transition from monomeric to oligomeric proteins: tools, the environment, hypotheses
-
D'Alessio G. The evolutionary transition from monomeric to oligomeric proteins: tools, the environment, hypotheses. Prog Biophys Mol Biol 72 (1999) 271-298
-
(1999)
Prog Biophys Mol Biol
, vol.72
, pp. 271-298
-
-
D'Alessio, G.1
-
24
-
-
26844537302
-
Revised structure of the AbrB N-terminal domain unifies a diverse superfamily of putative DNA-binding proteins
-
Bobay B.G., Andreeva A., Mueller G.A., Cavanagh J., and Murzin A.G. Revised structure of the AbrB N-terminal domain unifies a diverse superfamily of putative DNA-binding proteins. FEBS Lett 579 (2005) 5669-5674
-
(2005)
FEBS Lett
, vol.579
, pp. 5669-5674
-
-
Bobay, B.G.1
Andreeva, A.2
Mueller, G.A.3
Cavanagh, J.4
Murzin, A.G.5
-
25
-
-
20444422946
-
AbrB-like transcription factors assume a swapped hairpin fold that is evolutionarily related to double-psi β-barrels
-
Coles M., Djuranovic S., Söding J., Frickey T., Koretke K., Truffault V., Martin J., and Lupas A.N. AbrB-like transcription factors assume a swapped hairpin fold that is evolutionarily related to double-psi β-barrels. Structure 13 (2005) 919-928
-
(2005)
Structure
, vol.13
, pp. 919-928
-
-
Coles, M.1
Djuranovic, S.2
Söding, J.3
Frickey, T.4
Koretke, K.5
Truffault, V.6
Martin, J.7
Lupas, A.N.8
-
26
-
-
0142103146
-
Functional analysis of substrate and cofactor complex structures of a thymidylate synthase-complementing protein
-
Mathews I.I., Deacon A.M., Canaves J.M., McMullan D., Lesley S.A., Agarwalla S., and Kuhn P. Functional analysis of substrate and cofactor complex structures of a thymidylate synthase-complementing protein. Structure 11 (2003) 677-690
-
(2003)
Structure
, vol.11
, pp. 677-690
-
-
Mathews, I.I.1
Deacon, A.M.2
Canaves, J.M.3
McMullan, D.4
Lesley, S.A.5
Agarwalla, S.6
Kuhn, P.7
-
27
-
-
2442601478
-
Functional evidence for active site location of tetrameric thymidylate synthase X at the interphase of three monomers
-
Homo-oligomeric enzymes with active sites formed at the interface of three or more monomers are rare. In this case, each monomer is shown to contribute a catalytically essential residue, suggesting that the ThyX tetramer may have evolved by oligomerisation of 'inactive' monomers.
-
Leduc D., Graziani S., Lipowski G., Marchand C., Le Marechal P., Liebl U., and Myllykallio H. Functional evidence for active site location of tetrameric thymidylate synthase X at the interphase of three monomers. Proc Natl Acad Sci USA 101 (2004) 7252-7257. Homo-oligomeric enzymes with active sites formed at the interface of three or more monomers are rare. In this case, each monomer is shown to contribute a catalytically essential residue, suggesting that the ThyX tetramer may have evolved by oligomerisation of 'inactive' monomers.
-
(2004)
Proc Natl Acad Sci USA
, vol.101
, pp. 7252-7257
-
-
Leduc, D.1
Graziani, S.2
Lipowski, G.3
Marchand, C.4
Le Marechal, P.5
Liebl, U.6
Myllykallio, H.7
-
28
-
-
0037039818
-
Metabolic enzymes of mycobacteria linked to antioxidant defense by a thioredoxin-like protein
-
Bryk R., Lima C.D., Erdjument-Bromage H., Tempst P., and Nathan C. Metabolic enzymes of mycobacteria linked to antioxidant defense by a thioredoxin-like protein. Science 295 (2002) 1073-1077
-
(2002)
Science
, vol.295
, pp. 1073-1077
-
-
Bryk, R.1
Lima, C.D.2
Erdjument-Bromage, H.3
Tempst, P.4
Nathan, C.5
-
29
-
-
0037205463
-
Ortiz de Montellano PR. The crystal structure of Mycobacterium tuberculosis alkylhydroperoxidase AhpD, a potential target for antitubercular drug design
-
Nunn C.M., Djordjevic S., Hillas P.J., and Nishida C.R. Ortiz de Montellano PR. The crystal structure of Mycobacterium tuberculosis alkylhydroperoxidase AhpD, a potential target for antitubercular drug design. J Biol Chem 277 (2002) 20033-20040
-
(2002)
J Biol Chem
, vol.277
, pp. 20033-20040
-
-
Nunn, C.M.1
Djordjevic, S.2
Hillas, P.J.3
Nishida, C.R.4
-
30
-
-
33646147373
-
-
Ito K, Arai R, Fusatomi E, Kamo-Uchikubo T, Kawaguchi S-I, Akasaka R, Terada T, Kuramitsu S, Shirouzu M, Yokoyama S: Crystal structure of the conserved protein TTHA0727 from Thermus thermophilus HB8 at 1.9 Å resolution: a CMD family member distinct from carboxymuconolactone decarboxylase (CMD) and AhpD. Protein Sci 2006; doi:10.1110/ps.062148506.
-
-
-
-
31
-
-
32044441001
-
Structural basis for sulfur relay to RNA mediated by heterohexameric TusBCD complex
-
Recent genetic studies reveal that the products of five novel genes, tusABCDE, function in 2-thiouridine modification of tRNA wobble positions. The TusBCD complex is a dimer of heterotrimers of homologous subunits, related to hypothetical protein YchN [32], of which only TusD retains the catalytic cysteine residue.
-
Numata T., Fukai S., Ikeuchi Y., Suzuki T., and Nureki O. Structural basis for sulfur relay to RNA mediated by heterohexameric TusBCD complex. Structure 14 (2006) 357-366. Recent genetic studies reveal that the products of five novel genes, tusABCDE, function in 2-thiouridine modification of tRNA wobble positions. The TusBCD complex is a dimer of heterotrimers of homologous subunits, related to hypothetical protein YchN [32], of which only TusD retains the catalytic cysteine residue.
-
(2006)
Structure
, vol.14
, pp. 357-366
-
-
Numata, T.1
Fukai, S.2
Ikeuchi, Y.3
Suzuki, T.4
Nureki, O.5
-
32
-
-
0036292374
-
Crystal structure of a conserved hypothetical protein from Escherichia coli
-
Shin D.H., Yokota H., Kim R., and Kim S.H. Crystal structure of a conserved hypothetical protein from Escherichia coli. J Struct Funct Genomics 2 (2002) 53-66
-
(2002)
J Struct Funct Genomics
, vol.2
, pp. 53-66
-
-
Shin, D.H.1
Yokota, H.2
Kim, R.3
Kim, S.H.4
-
33
-
-
33645047892
-
1.6 Å crystal structure of the secreted chorismate mutase from Mycobacterium tuberculosis: novel fold topology revealed
-
α subclass by gene duplication and fusion events to generate different fold variants.
-
α subclass by gene duplication and fusion events to generate different fold variants.
-
(2006)
J Mol Biol
, vol.357
, pp. 1483-1499
-
-
Ökvist, M.1
Dey, R.2
Sasso, S.3
Grahn, E.4
Kast, P.5
Krengel, U.6
-
34
-
-
24344438922
-
The monomeric dUTPase from Epstein-Barr virus mimics trimeric dUTPases
-
The monomeric and trimeric dUTPases both contain the same five characteristic sequence motifs, but in a different order. This example of evolution from the trimeric to the monomeric enzyme is contrary to the commonly observed trend for efficient genome usage in viruses, as the monomeric dUTPase needs more coding sequence than a trimeric one.
-
Tarbouriech N., Buisson M., Seigneurin J.-M., Cusack S., and Burmeister W.P. The monomeric dUTPase from Epstein-Barr virus mimics trimeric dUTPases. Structure 13 (2005) 1299-1310. The monomeric and trimeric dUTPases both contain the same five characteristic sequence motifs, but in a different order. This example of evolution from the trimeric to the monomeric enzyme is contrary to the commonly observed trend for efficient genome usage in viruses, as the monomeric dUTPase needs more coding sequence than a trimeric one.
-
(2005)
Structure
, vol.13
, pp. 1299-1310
-
-
Tarbouriech, N.1
Buisson, M.2
Seigneurin, J.-M.3
Cusack, S.4
Burmeister, W.P.5
-
35
-
-
14644444463
-
Dimeric dUTPases, HisE, and MazG belong to a new superfamily of all-α NTP pyrophosphohydrolases with potential 'house-cleaning' functions
-
Moroz O.V., Murzin A.G., Makarova K.S., Koonin E.V., Wilson K.S., and Galperin M.Y. Dimeric dUTPases, HisE, and MazG belong to a new superfamily of all-α NTP pyrophosphohydrolases with potential 'house-cleaning' functions. J Mol Biol 347 (2005) 243-255
-
(2005)
J Mol Biol
, vol.347
, pp. 243-255
-
-
Moroz, O.V.1
Murzin, A.G.2
Makarova, K.S.3
Koonin, E.V.4
Wilson, K.S.5
Galperin, M.Y.6
-
36
-
-
0033578347
-
Common chelatase design in the branched tetrapyrrole pathways of heme and anaerobic cobalamin synthesis
-
Schubert H.L., Raux E., Wilson K.S., and Warren M.J. Common chelatase design in the branched tetrapyrrole pathways of heme and anaerobic cobalamin synthesis. Biochemistry 38 (1999) 10660-10669
-
(1999)
Biochemistry
, vol.38
, pp. 10660-10669
-
-
Schubert, H.L.1
Raux, E.2
Wilson, K.S.3
Warren, M.J.4
-
37
-
-
3943054839
-
The Sir2 family of protein deacetylases
-
Blander G., and Guarente L. The Sir2 family of protein deacetylases. Annu Rev Biochem 73 (2004) 417-435
-
(2004)
Annu Rev Biochem
, vol.73
, pp. 417-435
-
-
Blander, G.1
Guarente, L.2
-
38
-
-
0030906745
-
Molybdenum-cofactor-containing enzymes: structure and mechanism
-
Kisker C., Schindelin H., and Rees D.C. Molybdenum-cofactor-containing enzymes: structure and mechanism. Annu Rev Biochem 66 (1997) 233-267
-
(1997)
Annu Rev Biochem
, vol.66
, pp. 233-267
-
-
Kisker, C.1
Schindelin, H.2
Rees, D.C.3
-
39
-
-
0028773899
-
Crystallographic study of coenzyme, coenzyme analogue and substrate binding in 6-phosphogluconate dehydrogenase: implications for NADP specificity and the enzyme mechanism
-
Adams M.J., Ellis G.H., Gover S., Naylor C.E., and Phillips C. Crystallographic study of coenzyme, coenzyme analogue and substrate binding in 6-phosphogluconate dehydrogenase: implications for NADP specificity and the enzyme mechanism. Structure 2 (1994) 651-668
-
(1994)
Structure
, vol.2
, pp. 651-668
-
-
Adams, M.J.1
Ellis, G.H.2
Gover, S.3
Naylor, C.E.4
Phillips, C.5
-
40
-
-
0030996769
-
The crystal structure of plant acetohydroxy acid isomeroreductase complexed with NADPH, two magnesium ions and a herbicidal transition state analog determined at 1.65 Å resolution
-
Biou V., Dumas R., Cohen-Addad C., Douce R., Job D., and Pebay-Peyroula E. The crystal structure of plant acetohydroxy acid isomeroreductase complexed with NADPH, two magnesium ions and a herbicidal transition state analog determined at 1.65 Å resolution. EMBO J 16 (1997) 3405-3415
-
(1997)
EMBO J
, vol.16
, pp. 3405-3415
-
-
Biou, V.1
Dumas, R.2
Cohen-Addad, C.3
Douce, R.4
Job, D.5
Pebay-Peyroula, E.6
-
41
-
-
0037044776
-
Crystal structure of Pseudomonas fluorescens mannitol 2-dehydrogenase binary and ternary complexes: specificity and catalytic mechanism
-
Kavanagh K.L., Klimacek M., Nidetzky B., and Wilson D.K. Crystal structure of Pseudomonas fluorescens mannitol 2-dehydrogenase binary and ternary complexes: specificity and catalytic mechanism. J Biol Chem 277 (2002) 43433-43442
-
(2002)
J Biol Chem
, vol.277
, pp. 43433-43442
-
-
Kavanagh, K.L.1
Klimacek, M.2
Nidetzky, B.3
Wilson, D.K.4
-
42
-
-
0034643813
-
The first structure of UDP-glucose dehydrogenase reveals the catalytic residues necessary for the two-fold oxidation
-
Campbell R.E., Mosimann S.C., van De Rijn I., Tanner M.E., and Strynadka N.C. The first structure of UDP-glucose dehydrogenase reveals the catalytic residues necessary for the two-fold oxidation. Biochemistry 39 (2000) 7012-7023
-
(2000)
Biochemistry
, vol.39
, pp. 7012-7023
-
-
Campbell, R.E.1
Mosimann, S.C.2
van De Rijn, I.3
Tanner, M.E.4
Strynadka, N.C.5
-
43
-
-
0034710671
-
A deeply knotted protein structure and how it might fold
-
Taylor W.R. A deeply knotted protein structure and how it might fold. Nature 406 (2000) 916-919
-
(2000)
Nature
, vol.406
, pp. 916-919
-
-
Taylor, W.R.1
-
44
-
-
0037472127
-
Crystal structure of GDP-mannose dehydrogenase: a key enzyme of alginate biosynthesis in P. aeruginosa
-
Snook C.F., Tipton P.A., and Beamer L.J. Crystal structure of GDP-mannose dehydrogenase: a key enzyme of alginate biosynthesis in P. aeruginosa. Biochemistry 42 (2003) 4658-4668
-
(2003)
Biochemistry
, vol.42
, pp. 4658-4668
-
-
Snook, C.F.1
Tipton, P.A.2
Beamer, L.J.3
-
45
-
-
24644525066
-
Crystal structure of novel NADP-dependent 3-hydroxyisobutyrate dehydrogenase from Thermus thermophilus HB8
-
Lokanath N.K., Ohshima N., Takio K., Shiromizu I., Kuroishi C., Okazaki N., Kuramitsu S., Yokoyama S., Miyano M., and Kunishima N. Crystal structure of novel NADP-dependent 3-hydroxyisobutyrate dehydrogenase from Thermus thermophilus HB8. J Mol Biol 352 (2005) 905-917
-
(2005)
J Mol Biol
, vol.352
, pp. 905-917
-
-
Lokanath, N.K.1
Ohshima, N.2
Takio, K.3
Shiromizu, I.4
Kuroishi, C.5
Okazaki, N.6
Kuramitsu, S.7
Yokoyama, S.8
Miyano, M.9
Kunishima, N.10
-
46
-
-
0037466290
-
Crystal structure of class I acetohydroxy acid isomeroreductase from Pseudomonas aeruginosa
-
Ahn H.J., Eom S.J., Yoon H.J., Lee B.I., Cho H., and Suh S.W. Crystal structure of class I acetohydroxy acid isomeroreductase from Pseudomonas aeruginosa. J Mol Biol 328 (2003) 505-515
-
(2003)
J Mol Biol
, vol.328
, pp. 505-515
-
-
Ahn, H.J.1
Eom, S.J.2
Yoon, H.J.3
Lee, B.I.4
Cho, H.5
Suh, S.W.6
-
47
-
-
0034658406
-
A potential target enzyme for trypanocidal drugs revealed by the crystal structure of NAD-dependent glycerol-3-phosphate dehydrogenase from Leishmania mexicana
-
Suresh S., Turley S., Opperdoes F.R., Michels P.A., and Hol W.G. A potential target enzyme for trypanocidal drugs revealed by the crystal structure of NAD-dependent glycerol-3-phosphate dehydrogenase from Leishmania mexicana. Structure 8 (2000) 541-552
-
(2000)
Structure
, vol.8
, pp. 541-552
-
-
Suresh, S.1
Turley, S.2
Opperdoes, F.R.3
Michels, P.A.4
Hol, W.G.5
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