-
1
-
-
0034666290
-
1-Cys peroxiredoxin, a bifunctional enzyme with glutathione peroxidase and phospholipase A2 activities
-
Chen, J. W., Dodia, C., Feinstein, S. I., Jain, M. K., and Fisher, A. B. (2000) 1-Cys peroxiredoxin, a bifunctional enzyme with glutathione peroxidase and phospholipase A2 activities J. Biol. Chem. 275, 28421-28427
-
(2000)
J. Biol. Chem.
, vol.275
, pp. 28421-28427
-
-
Chen, J.W.1
Dodia, C.2
Feinstein, S.I.3
Jain, M.K.4
Fisher, A.B.5
-
2
-
-
18844400905
-
Peroxiredoxin 6, a 1-Cys peroxiredoxin, functions in antioxidant defense and lung phospholipid metabolism
-
DOI 10.1016/j.freeradbiomed.2005.02.011, PII S0891584905000821
-
Manevich, Y. and Fisher, A. B. (2005) Peroxiredoxin 6, a 1-Cys peroxiredoxin, functions in antioxidant defense and lung phospholipid metabolism Free Radical Biol. Med. 38, 1422-1432 (Pubitemid 40693827)
-
(2005)
Free Radical Biology and Medicine
, vol.38
, Issue.11
, pp. 1422-1432
-
-
Manevich, Y.1
Fisher, A.B.2
-
3
-
-
79953249112
-
Peroxiredoxin 6: A bifunctional enzyme with glutathione peroxidase and phospholipase A2 activities
-
Fisher, A. B. (2011) Peroxiredoxin 6: A bifunctional enzyme with glutathione peroxidase and phospholipase A2 activities Antioxid. Redox Signaling 15, 831-844
-
(2011)
Antioxid. Redox Signaling
, vol.15
, pp. 831-844
-
-
Fisher, A.B.1
-
4
-
-
0031838091
-
2 of bovine lung
-
DOI 10.1016/S0305-0491(98)10046-9, PII S0305049198100469
-
2+-independent phospholipase A2 of bovine lung Comp. Biochem. Physiol., Part B: Biochem. Mol. Biol. 120, 393-404 (Pubitemid 28386793)
-
(1998)
Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology
, vol.120
, Issue.2
, pp. 393-404
-
-
Akiba, S.1
Dodia, C.2
Chen, X.3
Fisher, A.B.4
-
5
-
-
0029658967
-
2 enzymes in degradation of dipalmitoylphosphatidylcholine by granular pneumocytes
-
Fisher, A. B. and Dodia, C. (1996) Role of phospholipase A2 enzymes in degradation of dipalmitoylphosphatidylcholine by granular pneumocytes J. Lipid Res. 37, 1057-1064 (Pubitemid 26182338)
-
(1996)
Journal of Lipid Research
, vol.37
, Issue.5
, pp. 1057-1064
-
-
Fisher, A.B.1
Dodia, C.2
-
6
-
-
34948878714
-
Structure and phospholipase function of peroxiredoxin 6: Identification of the catalytic triad and its role in phospholipid substrate binding
-
DOI 10.1194/jlr.M700299-JLR200
-
Manevich, Y., Reddy, K. S., Shuvaeva, T., Feinstein, S. I., and Fisher, A. B. (2007) Structure and phospholipase function of peroxiredoxin 6: Identification of the catalytic triad and its role in phospholipid substrate binding J. Lipid Res. 48, 2306-2318 (Pubitemid 47529572)
-
(2007)
Journal of Lipid Research
, vol.48
, Issue.10
, pp. 2306-2318
-
-
Manevich, Y.1
Reddy, K.S.2
Shuvaeva, T.3
Feinstein, S.I.4
Fisher, A.B.5
-
8
-
-
64849097627
-
Mitogen activated protein kinase-mediated phosphorylation of peroxiredoxin 6 regulates its phospholipid A2 activity
-
Wu, Y., Feinstein, S. I., Manevich, Y., Chowdhury, I., Pak, J. H., Kazi, A., Dodia, C., Speicher, D. W., and Fisher, A. B. (2009) Mitogen activated protein kinase-mediated phosphorylation of peroxiredoxin 6 regulates its phospholipid A2 activity Biochem. J. 419, 669-679
-
(2009)
Biochem. J.
, vol.419
, pp. 669-679
-
-
Wu, Y.1
Feinstein, S.I.2
Manevich, Y.3
Chowdhury, I.4
Pak, J.H.5
Kazi, A.6
Dodia, C.7
Speicher, D.W.8
Fisher, A.B.9
-
9
-
-
67349275032
-
Binding of peroxiredoxin 6 to substrate determines differential phospholipid hydroperoxide peroxidase and phospholipase A(2) activities
-
Manevich, Y., Shuvaeva, T., Dodia, C., Kazi, A., Feinstein, S. I., and Fisher, A. B. (2009) Binding of peroxiredoxin 6 to substrate determines differential phospholipid hydroperoxide peroxidase and phospholipase A(2) activities Arch. Biochem. Biophys. 485, 139-149
-
(2009)
Arch. Biochem. Biophys.
, vol.485
, pp. 139-149
-
-
Manevich, Y.1
Shuvaeva, T.2
Dodia, C.3
Kazi, A.4
Feinstein, S.I.5
Fisher, A.B.6
-
10
-
-
79953199438
-
Peroxiredoxin 6 phosphorylation and subsequent phospholipase A2 activity are required for agonist-mediated activation of NADPH oxidase in mouse pulmonary microvascular endothelium and alveolar macrophages
-
Chatterjee, S., Feinstein, S. I., Dodia, C., Sorokina, E., Lien, Y. C., Nguyen, S., Debolt, K., Speicher, D., and Fisher, A. B. (2011) Peroxiredoxin 6 phosphorylation and subsequent phospholipase A2 activity are required for agonist-mediated activation of NADPH oxidase in mouse pulmonary microvascular endothelium and alveolar macrophages J. Biol. Chem. 286, 11696-11701
-
(2011)
J. Biol. Chem.
, vol.286
, pp. 11696-11701
-
-
Chatterjee, S.1
Feinstein, S.I.2
Dodia, C.3
Sorokina, E.4
Lien, Y.C.5
Nguyen, S.6
Debolt, K.7
Speicher, D.8
Fisher, A.B.9
-
11
-
-
1642326559
-
Activation of the antioxidant enzyme 1-CYS peroxiredoxin requires glutathionylation mediated by heterodimerization with GST
-
DOI 10.1073/pnas.0400181101
-
Manevich, Y., Feinstein, S. I., and Fisher, A. B. (2004) Activation of the antioxidant enzyme 1-CYS peroxiredoxin requires glutathionylation mediated by heterodimerization with À GST Proc. Natl. Acad. Sci. U.S.A. 101, 3780-3785 (Pubitemid 38381055)
-
(2004)
Proceedings of the National Academy of Sciences of the United States of America
, vol.101
, Issue.11
, pp. 3780-3785
-
-
Manevich, Y.1
Feinstein, S.I.2
Fisher, A.B.3
-
12
-
-
0002844767
-
Systematic analysis of peptide recoveries from in-gel digestions for protein identifications in proteome studies
-
Speicher, K. D., Kolbas, O., Harper, S., and Speicher, D. W. (2000) Systematic analysis of peptide recoveries from in-gel digestions for protein identifications in proteome studies J. Biomol. Tech. 11, 74-86
-
(2000)
J. Biomol. Tech.
, vol.11
, pp. 74-86
-
-
Speicher, K.D.1
Kolbas, O.2
Harper, S.3
Speicher, D.W.4
-
13
-
-
78650981490
-
Deciphering the human platelet sheddome
-
Fong, K. P., Barry, C., Tran, A. N., Traxler, E. A., Wannemacher, K. M., Tang, H. Y., Speicher, K. D., Blair, I. A., Speicher, D. W., Grosser, T., and Brass, L. F. (2011) Deciphering the human platelet sheddome Blood 117, e15-26
-
(2011)
Blood
, vol.117
, pp. 15-26
-
-
Fong, K.P.1
Barry, C.2
Tran, A.N.3
Traxler, E.A.4
Wannemacher, K.M.5
Tang, H.Y.6
Speicher, K.D.7
Blair, I.A.8
Speicher, D.W.9
Grosser, T.10
Brass, L.F.11
-
14
-
-
24944523382
-
2
-
DOI 10.1194/jlr.M400499-JLR200
-
Fisher, A. B., Dodia, C., Feinstein, S. I., and Ho, Y. S. (2005) Altered lung phospholipid metabolism in mice with targeted deletion of lysosomal-type phospholipase A2 J. Lipid Res. 46, 1248-1256 (Pubitemid 43109839)
-
(2005)
Journal of Lipid Research
, vol.46
, Issue.6
, pp. 1248-1256
-
-
Fisher, A.B.1
Dodia, C.2
Feinstein, S.I.3
Ho, Y.-S.4
-
15
-
-
33646358970
-
2 activity
-
DOI 10.1074/jbc.M504525200
-
Wu, Y. Z., Manevich, Y., Baldwin, J. L., Dodia, C., Yu, K., Feinstein, S. I., and Fisher, A. B. (2006) Interaction of surfactant protein A with peroxiredoxin 6 regulates phospholipase A2 activity J. Biol. Chem. 281, 7515-7525 (Pubitemid 43847522)
-
(2006)
Journal of Biological Chemistry
, vol.281
, Issue.11
, pp. 7515-7525
-
-
Wu, Y.-Z.1
Manevich, Y.2
Baldwin, J.L.3
Dodia, C.4
Yu, K.5
Feinstein, S.I.6
Fisher, A.B.7
-
16
-
-
0017081322
-
An investigation of the electronic and steric environments of tyrosyl residues in ribonuclease A and Erwinia carotovora l -asparaginase through fluorescence quenching by caesium, iodide and phosphate ions
-
Homer, R. B. and Allsopp, S. R. (1976) An investigation of the electronic and steric environments of tyrosyl residues in ribonuclease A and Erwinia carotovora l -asparaginase through fluorescence quenching by caesium, iodide and phosphate ions Biochim. Biophys. Acta 434, 297-310
-
(1976)
Biochim. Biophys. Acta
, vol.434
, pp. 297-310
-
-
Homer, R.B.1
Allsopp, S.R.2
-
17
-
-
0015230409
-
Solute perturbation of protein fluorescence. The quenching of the tryptophyl fluorescence of model compounds and of lysozyme by iodide ion
-
Lehrer, S. S. (1971) Solute perturbation of protein fluorescence. The quenching of the tryptophyl fluorescence of model compounds and of lysozyme by iodide ion Biochemistry 10, 3254-3263
-
(1971)
Biochemistry
, vol.10
, pp. 3254-3263
-
-
Lehrer, S.S.1
-
18
-
-
0022973842
-
Acrylamide and iodide fluorescence quenching as a structural probe of tryptophan microenvironment in bovine lens crystallins
-
Phillips, S. R., Wilson, L. J., and Borkman, R. F. (1986) Acrylamide and iodide fluorescence quenching as a structural probe of tryptophan microenvironment in bovine lens crystallins Curr. Eye Res. 5, 611-619 (Pubitemid 17173736)
-
(1986)
Current Eye Research
, vol.5
, Issue.8
, pp. 611-619
-
-
Phillips, S.R.1
Wilson, L.J.2
Borkman, R.F.3
-
20
-
-
0015937178
-
Interaction of an apolipoprotein (apoLP-alanine) with phosphatidylcholine
-
Morrisett, J. D., Davis, J. S., Pownall, H. J., and Gotto, A. M. (1973) Interaction of an apolipoprotein (apoLP-alanine) with phosphatidylcholine Biochemistry 12, 1290-1299
-
(1973)
Biochemistry
, vol.12
, pp. 1290-1299
-
-
Morrisett, J.D.1
Davis, J.S.2
Pownall, H.J.3
Gotto, A.M.4
-
21
-
-
0023697408
-
Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl ñ-chymotrypsin using different denaturants
-
Santoro, M. M. and Bolen, D. W. (1988) Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl ñ-chymotrypsin using different denaturants Biochemistry 27, 8063-8068
-
(1988)
Biochemistry
, vol.27
, pp. 8063-8068
-
-
Santoro, M.M.1
Bolen, D.W.2
-
22
-
-
67649529020
-
A single mutation induces molten globule formation and a drastic destabilization of wild-type cytochrome c at pH 6.0
-
Alam Khan, M. K., Das, U., Rahaman, M. H., Hassan, M. I., Srinivasan, A., Singh, T. P., and Ahmad, F. (2009) A single mutation induces molten globule formation and a drastic destabilization of wild-type cytochrome c at pH 6.0 J. Biol. Inorg. Chem. 14, 751-760
-
(2009)
J. Biol. Inorg. Chem.
, vol.14
, pp. 751-760
-
-
Alam Khan, M.K.1
Das, U.2
Rahaman, M.H.3
Hassan, M.I.4
Srinivasan, A.5
Singh, T.P.6
Ahmad, F.7
-
23
-
-
0031945918
-
Crystal structure of a novel human peroxidase enzyme at 2.0 À, resolution
-
DOI 10.1038/nsb0598-400
-
Choi, H. J., Kang, S. W., Yang, C. H., Rhee, S. G., and Ryu, S. E. (1998) Crystal structure of a novel human peroxidase enzyme at 2.0 Å resolution Nat. Struct. Biol. 5, 400-406 (Pubitemid 28211179)
-
(1998)
Nature Structural Biology
, vol.5
, Issue.5
, pp. 400-406
-
-
Choi, H.-J.1
Kang, S.W.2
Yang, C.-H.3
Rhee, S.G.4
Ryu, S.-E.5
-
25
-
-
0033597885
-
Phospholipid hydroperoxides are substrates for non-selenium glutathione peroxidase
-
Fisher, A. B., Dodia, C., Manevich, Y., Chen, J. W., and Feinstein, S. I. (1999) Phospholipid hydroperoxides are substrates for non-selenium glutathione peroxidase J. Biol. Chem. 274, 21326-21334
-
(1999)
J. Biol. Chem.
, vol.274
, pp. 21326-21334
-
-
Fisher, A.B.1
Dodia, C.2
Manevich, Y.3
Chen, J.W.4
Feinstein, S.I.5
-
26
-
-
0022503457
-
Calculation of protein conformation from circular dichroism
-
Yang, J. T., Wu, C. S., and Martinez, H. M. (1986) Calculation of protein conformation from circular dichroism Methods Enzymol. 130, 208-269
-
(1986)
Methods Enzymol.
, vol.130
, pp. 208-269
-
-
Yang, J.T.1
Wu, C.S.2
Martinez, H.M.3
-
27
-
-
23444456924
-
How to study proteins by circular dichroism
-
DOI 10.1016/j.bbapap.2005.06.005, PII S1570963905001792
-
Kelly, S. M., Jess, T. J., and Price, N. C. (2005) How to study proteins by circular dichroism Biochim. Biophys. Acta 1751, 119-139 (Pubitemid 41112231)
-
(2005)
Biochimica et Biophysica Acta - Proteins and Proteomics
, vol.1751
, Issue.2
, pp. 119-139
-
-
Kelly, S.M.1
Jess, T.J.2
Price, N.C.3
-
28
-
-
0015997959
-
Aromatic contributions to circular dichroism spectra of proteins
-
Strickland, E. H. (1974) Aromatic contributions to circular dichroism spectra of proteins CRC Crit. Rev. Biochem. 2, 113-175
-
(1974)
CRC Crit. Rev. Biochem.
, vol.2
, pp. 113-175
-
-
Strickland, E.H.1
-
29
-
-
0035028745
-
Mechanisms of tryptophan fluorescence shifts in proteins
-
Vivian, J. T. and Callis, P. R. (2001) Mechanisms of tryptophan fluorescence shifts in proteins Biophys. J. 80, 2093-2109 (Pubitemid 32401976)
-
(2001)
Biophysical Journal
, vol.80
, Issue.5
, pp. 2093-2109
-
-
Vivian, J.T.1
Callis, P.R.2
-
30
-
-
0013800421
-
The interaction of a naphthalene dye with apomyoglobin and apohemoglobin. A fluorescent probe of non-polar binding sites
-
Stryer, L. (1965) The interaction of a naphthalene dye with apomyoglobin and apohemoglobin. A fluorescent probe of non-polar binding sites J. Mol. Biol. 13, 482-495
-
(1965)
J. Mol. Biol.
, vol.13
, pp. 482-495
-
-
Stryer, L.1
-
31
-
-
0026096545
-
Study of the €œmolten globule€  intermediate state in protein folding by a hydrophobic fluorescent probe
-
Semisotnov, G. V., Rodionova, N. A., Razgulyaev, O. I., Uversky, V. N., Gripas, A. F., and Gilmanshin, R. I. (1991) Study of the € œmolten globule€Â? intermediate state in protein folding by a hydrophobic fluorescent probe Biopolymers 31, 119-128
-
(1991)
Biopolymers
, vol.31
, pp. 119-128
-
-
Semisotnov, G.V.1
Rodionova, N.A.2
Razgulyaev, O.I.3
Uversky, V.N.4
Gripas, A.F.5
Gilmanshin, R.I.6
-
32
-
-
0014589353
-
Dimer formation from 1-amino-8-naphthalenesulfonate catalyzed by bovine serum albumin. A new fluorescent molecule with exceptional binding properties
-
Rosen, C. G. and Weber, G. (1969) Dimer formation from 1-amino-8-naphthalenesulfonate catalyzed by bovine serum albumin. A new fluorescent molecule with exceptional binding properties Biochemistry 8, 3915-3920
-
(1969)
Biochemistry
, vol.8
, pp. 3915-3920
-
-
Rosen, C.G.1
Weber, G.2
-
33
-
-
0028820703
-
Denaturant M values and heat capacity changes: Relation to changes in accessible areas of protein unfolding
-
Myers, J. K., Pace, C. N., and Scholtz, J. M. (1995) Denaturant M values and heat capacity changes: Relation to changes in accessible areas of protein unfolding Protein Sci. 4, 2138-2148
-
(1995)
Protein Sci.
, vol.4
, pp. 2138-2148
-
-
Myers, J.K.1
Pace, C.N.2
Scholtz, J.M.3
-
34
-
-
0032992391
-
The paradox between m values and δCp's for denaturation of ribonuclease T1 with disulfide bonds intact and broken
-
2 for denaturation of ribonuclease T1 with disulfide bonds intact and broken Protein Sci. 8, 1314-1319 (Pubitemid 29264962)
-
(1999)
Protein Science
, vol.8
, Issue.6
, pp. 1314-1319
-
-
Baskakov, I.V.1
Bolen, D.W.2
-
35
-
-
0035798681
-
Lipid binding-induced conformational change in human apolipoprotein E. Evidence for two lipid-bound states on spherical particles
-
Saito, H., Dhanasekaran, P., Baldwin, F., Weisgraber, K. H., Lund-Katz, S., and Phillips, M. C. (2001) Lipid binding-induced conformational change in human apolipoprotein E. Evidence for two lipid-bound states on spherical particles J. Biol. Chem. 276, 40949-40954
-
(2001)
J. Biol. Chem.
, vol.276
, pp. 40949-40954
-
-
Saito, H.1
Dhanasekaran, P.2
Baldwin, F.3
Weisgraber, K.H.4
Lund-Katz, S.5
Phillips, M.C.6
-
36
-
-
2442656408
-
α-helix formation is required for high affinity binding of human apolipoprotein A-I to lipids
-
DOI 10.1074/jbc.M402043200
-
Saito, H., Dhanasekaran, P., Nguyen, D., Deridder, E., Holvoet, P., Lund-Katz, S., and Phillips, M. C. (2004) Ã?±-Helix formation is required for high affinity binding of human apolipoprotein A-I to lipids J. Biol. Chem. 279, 20974-20981 (Pubitemid 38656497)
-
(2004)
Journal of Biological Chemistry
, vol.279
, Issue.20
, pp. 20974-20981
-
-
Saito, H.1
Dhanasekaran, P.2
Nguyen, D.3
Deridder, E.4
Holvoet, P.5
Lund-Katz, S.6
Phillips, M.C.7
-
37
-
-
0034383949
-
The regulation of protein function by multisite phosphorylation: A 25 year update
-
Cohen, P. (2000) The regulation of protein function by multisite phosphorylation: A 25 year update Trends Biochem. Sci. 25, 596-601
-
(2000)
Trends Biochem. Sci.
, vol.25
, pp. 596-601
-
-
Cohen, P.1
-
38
-
-
0027254057
-
The molten globule intermediate of apomyoglobin and the process of protein folding
-
Barrick, D. and Baldwin, R. L. (1993) Stein and Moore Award address. The molten globule intermediate of apomyoglobin and the process of protein folding Protein Sci. 2, 869-876 (Pubitemid 23152080)
-
(1993)
Protein Science
, vol.2
, Issue.6
, pp. 869-876
-
-
Barrick, D.1
Baldwin, R.L.2
-
39
-
-
0024417964
-
The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure
-
Kuwajima, K. (1989) The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure Proteins 6, 87-103 (Pubitemid 19286669)
-
(1989)
Proteins: Structure, Function and Genetics
, vol.6
, Issue.2
, pp. 87-103
-
-
Kuwajima, K.1
-
40
-
-
0029124248
-
Molten globule and protein folding
-
Ptitsyn, O. B. (1995) Molten globule and protein folding Adv. Protein Chem. 47, 83-229
-
(1995)
Adv. Protein Chem.
, vol.47
, pp. 83-229
-
-
Ptitsyn, O.B.1
-
41
-
-
0037452560
-
Conformational and thermodynamic characterization of the molten globule state occurring during unfolding of cytochromes-c by weak salt denaturants
-
DOI 10.1021/bi0271042
-
Qureshi, S. H., Moza, B., Yadav, S., and Ahmad, F. (2003) Conformational and thermodynamic characterization of the molten globule state occurring during unfolding of cytochromes-c by weak salt denaturants Biochemistry 42, 1684-1695 (Pubitemid 36205977)
-
(2003)
Biochemistry
, vol.42
, Issue.6
, pp. 1684-1695
-
-
Qureshi, S.H.1
Moza, B.2
Yadav, S.3
Ahmad, F.4
-
42
-
-
0026698924
-
Crystal structure of the phosphotyrosine recognition domain SH2 of v-src complexed with tyrosine-phosphorylated peptides
-
Waksman, G., Kominos, D., Robertson, S. C., Pant, N., Baltimore, D., Birge, R. B., Cowburn, D., Hanafusa, H., Mayer, B. J., Overduin, M., Resh, M. D., Rios, C. B., Silverman, L., and Kuriyan, J. (1992) Crystal structure of the phosphotyrosine recognition domain SH2 of v-src complexed with tyrosine-phosphorylated peptides Nature 358, 646-653
-
(1992)
Nature
, vol.358
, pp. 646-653
-
-
Waksman, G.1
Kominos, D.2
Robertson, S.C.3
Pant, N.4
Baltimore, D.5
Birge, R.B.6
Cowburn, D.7
Hanafusa, H.8
Mayer, B.J.9
Overduin, M.10
Resh, M.D.11
Rios, C.B.12
Silverman, L.13
Kuriyan, J.14
-
43
-
-
13844255387
-
Natively unfolded proteins
-
DOI 10.1016/j.sbi.2005.01.002
-
Fink, A. L. (2005) Natively unfolded proteins Curr. Opin. Struct. Biol. 15, 35-41 (Pubitemid 40249507)
-
(2005)
Current Opinion in Structural Biology
, vol.15
, Issue.1 SPEC. ISS.
, pp. 35-41
-
-
Fink, A.L.1
-
44
-
-
0035022941
-
Intrinsically disordered protein
-
DOI 10.1016/S1093-3263(00)00138-8, PII S1093326300001388
-
Dunker, A. K., Lawson, J. D., Brown, C. J., Williams, R. M., Romero, P., Oh, J. S., Oldfield, C. J., Campen, A. M., Ratliff, C. M., Hipps, K. W., Ausio, J., Nissen, M. S., Reeves, R., Kang, C., Kissinger, C. R., Bailey, R. W., Griswold, M. D., Chiu, W., Garner, E. C., and Obradovic, Z. (2001) Intrinsically disordered protein J. Mol. Graphics Modell. 19, 26-59 (Pubitemid 32411501)
-
(2001)
Journal of Molecular Graphics and Modelling
, vol.19
, Issue.1
, pp. 26-59
-
-
Dunker, A.K.1
Lawson, J.D.2
Brown, C.J.3
Williams, R.M.4
Romero, P.5
Oh, J.S.6
Oldfield, C.J.7
Campen, A.M.8
Ratliff, C.M.9
Hipps, K.W.10
Ausio, J.11
Nissen, M.S.12
Reeves, R.13
Kang, C.14
Kissinger, C.R.15
Bailey, R.W.16
Griswold, M.D.17
Chiu, W.18
Garner, E.C.19
Obradovic, Z.20
more..
-
45
-
-
44349125600
-
Biological function in a non-native partially folded state of a protein
-
DOI 10.1038/emboj.2008.82, PII EMBOJ200882
-
Bemporad, F., Gsponer, J., Hopearuoho, H. I., Plakoutsi, G., Stati, G., Stefani, M., Taddei, N., Vendruscolo, M., and Chiti, F. (2008) Biological function in a non-native partially folded state of a protein EMBO J. 27, 1525-1535 (Pubitemid 351733337)
-
(2008)
EMBO Journal
, vol.27
, Issue.10
, pp. 1525-1535
-
-
Bemporad, F.1
Gsponer, J.2
Hopearuoho, H.I.3
Plakoutsi, G.4
Stati, G.5
Stefani, M.6
Taddei, N.7
Vendruscolo, M.8
Chiti, F.9
-
46
-
-
28244483285
-
Biologically active novel conformational state of botulinum, the most poisonous poison
-
DOI 10.1074/jbc.M508463200
-
Kukreja, R. and Singh, B. (2005) Biologically active novel conformational state of botulinum, the most poisonous poison J. Biol. Chem. 280, 39346-39352 (Pubitemid 41713891)
-
(2005)
Journal of Biological Chemistry
, vol.280
, Issue.47
, pp. 39346-39352
-
-
Kukreja, R.1
Singh, B.2
-
48
-
-
0034581327
-
Role of the molten globule state in protein folding
-
DOI 10.1016/S0065-3233(00)53005-8
-
Arai, M. and Kuwajima, K. (2000) Role of the molten globule state in protein folding Adv. Protein Chem. 53, 209-282 (Pubitemid 34194295)
-
(2000)
Advances in Protein Chemistry
, vol.53
, pp. 209-282
-
-
Arai, M.1
Kuwajima, K.2
-
49
-
-
36849044219
-
Structure and dynamics of a molten globular enzyme
-
DOI 10.1038/nsmb1325, PII NSMB1325
-
Pervushin, K., Vamvaca, K., Vogeli, B., and Hilvert, D. (2007) Structure and dynamics of a molten globular enzyme Nat. Struct. Mol. Biol. 14, 1202-1206 (Pubitemid 350223332)
-
(2007)
Nature Structural and Molecular Biology
, vol.14
, Issue.12
, pp. 1202-1206
-
-
Pervushin, K.1
Vamvaca, K.2
Vogeli, B.3
Hilvert, D.4
-
50
-
-
0029786618
-
Circularly permuted dihydrofolate reductase possesses all the properties of the molten globule state, but can resume functional tertiary structure by interaction with its ligands
-
Uversky, V. N., Kutyshenko, V. P., Protasova, N., Rogov, V. V., Vassilenko, K. S., and Gudkov, A. T. (1996) Circularly permuted dihydrofolate reductase possesses all the properties of the molten globule state, but can resume functional tertiary structure by interaction with its ligands Protein Sci. 5, 1844-1851 (Pubitemid 26303488)
-
(1996)
Protein Science
, vol.5
, Issue.9
, pp. 1844-1851
-
-
Uversky, V.N.1
Kutyshenko, V.P.2
Protasova, N.Yu.3
Rogov, V.V.4
Vassilenko, K.S.5
Gudkov, A.T.6
|