-
1
-
-
0032973950
-
New insights into an old protein: The functional diversity of mammalian glyceraldehyde-3-phosphate dehydrogenase
-
DOI 10.1016/S0167-4838(99)00119-3, PII S0167483899001193
-
M.A. Sirover New insights into an old protein: the functional diversity of mammalian glyceraldehyde-3-phosphate dehydrogenase Biochimica et Biophysica Acta 1432 1999 159 184 (Pubitemid 29304525)
-
(1999)
Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology
, vol.1432
, Issue.2
, pp. 159-184
-
-
Sirover, M.A.1
-
2
-
-
79959226194
-
On the functional diversity of glyceraldehyde-3-phosphate dehydrogenase: Biochemical mechanisms and regulatory control
-
M.A. Sirover On the functional diversity of glyceraldehyde-3-phosphate dehydrogenase: biochemical mechanisms and regulatory control Biochimica et Biophysica Acta 1810 2011 741 751
-
(2011)
Biochimica et Biophysica Acta
, vol.1810
, pp. 741-751
-
-
Sirover, M.A.1
-
3
-
-
0026070055
-
A human nuclear uracil DNA glycosylase is the 37-kDa subunit of glyceraldehyde-3-phosphate dehydrogenase
-
K. Meyer-Siegler, D.J. Mauro, G. Seal, J. Wurzer, J.K. deRiel, and M.A. Sirover A human nuclear uracil DNA glycosylase is the 37-kDa subunit of glyceraldehyde-3-phosphate dehydrogenase Proceedings of the National Academy of Sciences of the United States of America 88 1991 8460 8464 (Pubitemid 21915376)
-
(1991)
Proceedings of the National Academy of Sciences of the United States of America
, vol.88
, Issue.19
, pp. 8460-8464
-
-
Meyer-Siegler, K.1
Mauro, D.J.2
Seal, G.3
Wurzer, J.4
Deriel, J.K.5
Sirover, M.A.6
-
4
-
-
0027518424
-
Sequence-specific binding of transfer RNA by glyceraldehyde-3-phosphate dehydrogenase
-
R. Singh, and M.R. Green Sequence-specific binding of transfer RNA by glyceraldehyde-3-phosphate dehydrogenase Science 259 1993 365 368 (Pubitemid 23055678)
-
(1993)
Science
, vol.259
, Issue.5093
, pp. 365-368
-
-
Singh, R.1
Green, M.R.2
-
5
-
-
0035951872
-
Glyceraldehyde-3-phosphate dehydrogenase is required for vesicular transport in the early secretory pathway
-
E.J. Tisdale Glyceraldehyde-3-phosphate dehydrogenase is required for vesicular transport in the early secretory pathway Journal of Biological Chemistry 276 2001 2480 2486
-
(2001)
Journal of Biological Chemistry
, vol.276
, pp. 2480-2486
-
-
Tisdale, E.J.1
-
6
-
-
0020758755
-
A porcine brain protein (35 K protein) which bundles microtubules and its identification as glyceraldehyde 3-phosphate dehydrogenase
-
H. Kumagai, and H. Sakai A porcine brain protein (35 K protein) which bundles microtubules and its identification as glyceraldehyde 3-phosphate dehydrogenase Journal of Biochemistry 93 1983 1259 1269
-
(1983)
Journal of Biochemistry
, vol.93
, pp. 1259-1269
-
-
Kumagai, H.1
Sakai, H.2
-
7
-
-
22144477159
-
S-nitrosylated GAPDH initiates apoptotic cell death by nuclear translocation following Siah1 binding
-
DOI 10.1038/ncb1268
-
M.R. Hara, N. Agrawal, S.F. Kim, M.B. Cascio, M. Fujimuro, Y. Ozeki, M. Takahashi, J.H. Cheah, S.K. Tankou, L.D. Hester, C.D. Ferris, S.D. Hayward, S.H. Snyder, and A. Sawa S-nitrosylated GAPDH initiates apoptotic cell death by nuclear translocation following Siah 1 binding Nature Cell Biology 7 2005 665 674 (Pubitemid 40975747)
-
(2005)
Nature Cell Biology
, vol.7
, Issue.7
, pp. 665-674
-
-
Hara, M.R.1
Agrawal, N.2
Kim, S.F.3
Cascio, M.B.4
Fujimuro, M.5
Ozeki, Y.6
Takahashi, M.7
Cheah, J.H.8
Tankou, S.K.9
Hester, L.D.10
Ferris, C.D.11
Hayward, S.D.12
Snyder, S.H.13
Sawa, A.14
-
8
-
-
78649842470
-
The diverse functions of GAPDH: Views from different subcellular compartments
-
C. Tristan, N. Shahani, T.W. Sedlak, and A. Sawa The diverse functions of GAPDH: views from different subcellular compartments Cellular Signalling 23 2011 317 323
-
(2011)
Cellular Signalling
, vol.23
, pp. 317-323
-
-
Tristan, C.1
Shahani, N.2
Sedlak, T.W.3
Sawa, A.4
-
9
-
-
13844318224
-
Glyceraldehyde-3-phosphate dehydrogenase, apoptosis, and neurodegenerative diseases
-
DOI 10.1146/annurev.pharmtox.45.120403.095902
-
D.M. Chuang, C. Hough, and V.V. Senatorov Glyceraldehyde-3-phosphate dehydrogenase, apoptosis, and neurodegenerative diseases Annual Review of Pharmacology and Toxicology 45 2005 269 290 (Pubitemid 40261806)
-
(2005)
Annual Review of Pharmacology and Toxicology
, vol.45
, pp. 269-290
-
-
Chuang, D.-M.1
Hough, C.2
Senatorov, V.V.3
-
10
-
-
77954497959
-
Oxidatively modified glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and Alzheimer's disease: Many pathways to neurodegeneration
-
D.A. Butterfield, S.S. Hardas, and M.L. Lange Oxidatively modified glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and Alzheimer's disease: many pathways to neurodegeneration Journal of Alzheimer's Disease 20 2010 369 393
-
(2010)
Journal of Alzheimer's Disease
, vol.20
, pp. 369-393
-
-
Butterfield, D.A.1
Hardas, S.S.2
Lange, M.L.3
-
11
-
-
0021723672
-
Glyceraldehyde 3-phosphate dehydrogenase activity in rat and human lenses and the fate of enzyme molecules in the aging lens
-
DOI 10.1016/0047-6374(84)90019-8
-
A. Dovrat, J. Scharf, and D. Gershon Glyceraldehyde 3-phosphate dehydrogenase activity in rat and human lenses and the fate of enzyme molecules in the aging lens Mechanisms of Ageing and Development 28 1984 187 191 (Pubitemid 15175753)
-
(1984)
Mechanisms of Ageing and Development
, vol.28
, Issue.2-3
, pp. 187-191
-
-
Dovrat, A.1
Scharf, J.2
Gershon, D.3
-
12
-
-
0022647395
-
Human lens enzyme alterations with age and cataract: Glyceraldehyde-3-P dehydrogenase and triose phosphate isomerase
-
J.A. Jedziniak, L.M. Arredondo, and M. Meys Human lens enzyme alterations with age and cataract: glyceraldehyde-3-P dehydrogenase and triose phosphate isomerase Current Eye Research 5 1986 119 126 (Pubitemid 16125525)
-
(1986)
Current Eye Research
, vol.5
, Issue.2
, pp. 119-126
-
-
Jedziniak, J.A.1
Arredondo, L.M.2
Meys, M.3
-
13
-
-
0347062276
-
Structure of rabbit-muscle glyceraldehyde-3-phosphate dehydrogenase
-
DOI 10.1107/S0907444903020493
-
S.W. Cowan-Jacob, M. Kaufmann, A.N. Anselmo, W. Stark, and M.G. Grutter Structure of rabbit-muscle glyceraldehyde-3-phosphate dehydrogenase Acta Crystallographica Section D: Biological Crystallography 59 2003 2218 2227 (Pubitemid 38024856)
-
(2003)
Acta Crystallographica Section D: Biological Crystallography
, vol.59
, Issue.12
, pp. 2218-2227
-
-
Cowan-Jacob, S.W.1
Kaufmann, M.2
Anselmo, A.N.3
Stark, W.4
Grutter, M.G.5
-
14
-
-
0042198801
-
Redox regulation in the lens
-
DOI 10.1016/S1350-9462(03)00050-8
-
M.F. Lou Redox regulation in the lens Progress in Retinal and Eye Research 22 2003 657 682 (Pubitemid 36936805)
-
(2003)
Progress in Retinal and Eye Research
, vol.22
, Issue.5
, pp. 657-682
-
-
Lou, M.F.1
-
15
-
-
2942538081
-
Revival of inactive glyceraldehyde 3-phosphate dehydrogenase in human cataract lenses by reduction
-
DOI 10.1016/j.exer.2004.02.013, PII S0014483504000685
-
D. Rachdan, M.F. Lou, and J.J. Harding Revival of inactive glyceraldehyde 3-phosphate dehydrogenase in human cataract lenses by reduction Experimental Eye Research 79 2004 105 109 (Pubitemid 38737387)
-
(2004)
Experimental Eye Research
, vol.79
, Issue.1
, pp. 105-109
-
-
Rachdan, D.1
Lou, M.F.2
Harding, J.J.3
-
16
-
-
33749447728
-
Thioredoxin, thioredoxin reductase, and α-crystallin revive inactivated glyceraldehyde 3-phosphate dehydrogenase in human aged and cataract lens extracts
-
H. Yan, M.F. Lou, M.R. Fernando, and J.J. Harding Thioredoxin, thioredoxin reductase, and alpha-crystallin revive inactivated glyceraldehyde 3-phosphate dehydrogenase in human aged and cataract lens extracts Molecular Vision 12 2006 1153 1159 (Pubitemid 44509621)
-
(2006)
Molecular Vision
, vol.12
, pp. 1153-1159
-
-
Yan, H.1
Lou, M.F.2
Fernando, M.R.3
Harding, J.J.4
-
17
-
-
0017649191
-
Mechanism of reactivation and refolding of glyceraldehyde-3-phosphate dehydrogenase from yeast after denaturation and dissociation
-
R. Rudolph, I. Heider, and R. Jaenicke Mechanism of reactivation and refolding of glyceraldehyde-3-phosphate dehydrogenase from yeast after denaturation and dissociation European Journal of Biochemistry 81 1977 563 570 (Pubitemid 8236033)
-
(1977)
European Journal of Biochemistry
, vol.81
, Issue.3
, pp. 563-570
-
-
Rudolph, R.1
Heider, I.2
Jaenicke, R.3
-
18
-
-
0034845915
-
Aggregated proteins accelerate but do not increase the aggregation of d-glyceraldehyde-3-phosphate dehydrogenase. Specificity of protein aggregation
-
J. Li, Z. Lin, and C.C. Wang Aggregated proteins accelerate but do not increase the aggregation of d-glyceraldehyde-3-phosphate dehydrogenase. Specificity of protein aggregation Journal of Protein Chemistry 20 2001 155 163
-
(2001)
Journal of Protein Chemistry
, vol.20
, pp. 155-163
-
-
Li, J.1
Lin, Z.2
Wang, C.C.3
-
19
-
-
33750685996
-
Mechanism of thermal aggregation of rabbit muscle glyceraldehyde-3- phosphate dehydrogenase
-
DOI 10.1021/bi0610707
-
K.A. Markossian, H.A. Khanova, S.Y. Kleimenov, D.I. Levitsky, N.A. Chebotareva, R.A. Asryants, V.I. Muronetz, L. Saso, I.K. Yudin, and B.I. Kurganov Mechanism of thermal aggregation of rabbit muscle glyceraldehyde-3- phosphate dehydrogenase Biochemistry 45 2006 13375 13384 (Pubitemid 44707698)
-
(2006)
Biochemistry
, vol.45
, Issue.44
, pp. 13375-13384
-
-
Markossian, K.A.1
Khanova, H.A.2
Kleimenov, S.Yu.3
Levitsky, D.I.4
Chebotareva, N.A.5
Asryants, R.A.6
Muronetz, V.I.7
Saso, L.8
Yudin, I.K.9
Kurganov, B.I.10
-
20
-
-
0030696211
-
Hierarchy of lens proteins requiring protection against heat-induced precipitation by the α crystallin chaperone
-
DOI 10.1006/exer.1997.0358
-
P.T. Velasco, T.J. Lukas, S.N. Murthy, Y. Duglas-Tabor, D.L. Garland, and L. Lorand Hierarchy of lens proteins requiring protection against heat-induced precipitation by the alpha crystallin chaperone Experimental Eye Research 65 1997 497 505 (Pubitemid 27454950)
-
(1997)
Experimental Eye Research
, vol.65
, Issue.4
, pp. 497-505
-
-
Velasco, P.T.1
Lukas, T.J.2
Prasanna Murthy, S.N.3
Duglas-Tabor, Y.4
Garland, D.L.5
Lorand, L.6
-
21
-
-
15244355766
-
Misfolded forms of glyceraldehyde-3-phosphate dehydrogenase interact with GroEL and inhibit chaperonin-assisted folding of the wild-type enzyme
-
DOI 10.1110/ps.041211205
-
O.V. Polyakova, O. Roitel, R.A. Asryants, A.A. Poliakov, G. Branlant, and V.I. Muronetz Misfolded forms of glyceraldehyde-3-phosphate dehydrogenase interact with GroEL and inhibit chaperonin-assisted folding of the wild-type enzyme Protein Science 14 2005 921 928 (Pubitemid 40389361)
-
(2005)
Protein Science
, vol.14
, Issue.4
, pp. 921-928
-
-
Polyakova, O.V.1
Roitel, O.2
Asryants, R.A.3
Poliakov, A.A.4
Branlant, G.5
Muronetz, V.I.6
-
22
-
-
33846298505
-
Effect of α-crystallin on thermal denaturation and aggregation of rabbit muscle glyceraldehyde-3-phosphate dehydrogenase
-
DOI 10.1016/j.bpc.2006.11.002, PII S030146220600336X
-
H.A. Khanova, K.A. Markossian, S.Y. Kleimenov, D.I. Levitsky, N.A. Chebotareva, N.V. Golub, R.A. Asryants, V.I. Muronetz, L. Saso, I.K. Yudin, K.O. Muranov, M.A. Ostrovsky, and B.I. Kurganov Effect of alpha-crystallin on thermal denaturation and aggregation of rabbit muscle glyceraldehyde-3-phosphate dehydrogenase Biophysical Chemistry 125 2007 521 531 (Pubitemid 46123786)
-
(2007)
Biophysical Chemistry
, vol.125
, Issue.2-3
, pp. 521-531
-
-
Khanova, H.A.1
Markossian, K.A.2
Kleimenov, S.Yu.3
Levitsky, D.I.4
Chebotareva, N.A.5
Golub, N.V.6
Asryants, R.A.7
Muronetz, V.I.8
Saso, L.9
Yudin, I.K.10
Muranov, K.O.11
Ostrovsky, M.A.12
Kurganov, B.I.13
-
24
-
-
75049084608
-
Comparative analysis of the effects of alpha-crystallin and GroEL on the kinetics of thermal aggregation of rabbit muscle glyceraldehyde-3-phosphate dehydrogenase
-
K.A. Markossian, N.V. Golub, N.A. Chebotareva, R.A. Asryants, I.N. Naletova, V.I. Muronetz, K.A. Muranov, and B.I. Kurganov Comparative analysis of the effects of alpha-crystallin and GroEL on the kinetics of thermal aggregation of rabbit muscle glyceraldehyde-3-phosphate dehydrogenase The Protein Journal 29 2010 11 25
-
(2010)
The Protein Journal
, vol.29
, pp. 11-25
-
-
Markossian, K.A.1
Golub, N.V.2
Chebotareva, N.A.3
Asryants, R.A.4
Naletova, I.N.5
Muronetz, V.I.6
Muranov, K.A.7
Kurganov, B.I.8
-
25
-
-
70349499353
-
Antichaperone activity of cyclodextrin derivatives
-
O.I. Maloletkina, K.A. Markosyan, R.A. Asriyants, V.N. Orlov, and B.I. Kurganov Antichaperone activity of cyclodextrin derivatives Doklady Biochemistry and Biophysics 427 2009 199 201
-
(2009)
Doklady Biochemistry and Biophysics
, vol.427
, pp. 199-201
-
-
Maloletkina, O.I.1
Markosyan, K.A.2
Asriyants, R.A.3
Orlov, V.N.4
Kurganov, B.I.5
-
26
-
-
77952545560
-
Effect of 2-hydroxypropyl-beta-cyclodextrin on thermal inactivation, denaturation and aggregation of glyceraldehyde-3-phosphate dehydrogenase from rabbit skeletal muscle
-
O.I. Maloletkina, K.A. Markossian, R.A. Asryants, P.I. Semenyuk, V.F. Makeeva, and B.I. Kurganov Effect of 2-hydroxypropyl-beta-cyclodextrin on thermal inactivation, denaturation and aggregation of glyceraldehyde-3-phosphate dehydrogenase from rabbit skeletal muscle International Journal of Biological Macromolecules 46 2010 487 492
-
(2010)
International Journal of Biological Macromolecules
, vol.46
, pp. 487-492
-
-
Maloletkina, O.I.1
Markossian, K.A.2
Asryants, R.A.3
Semenyuk, P.I.4
Makeeva, V.F.5
Kurganov, B.I.6
-
27
-
-
0347768402
-
The effect of dansyl-modified β-cyclodextrin on the chaperone activity of heat shock proteins
-
DOI 10.1023/A:1011179228040
-
F. Hamada, M. Narita, A. Makabe, and H. Itoh The effect of dansyl-modified β-cyclodextrin on the chaperone activity of heat shock proteins Journal of Inclusion Phenomena and Macrocyclic Chemistry 40 2001 83 88 (Pubitemid 33654934)
-
(2001)
Journal of Inclusion Phenomena
, vol.40
, Issue.1-2
, pp. 83-88
-
-
Hamada, F.1
Narita, M.2
Makabe, A.3
Itoh, H.4
-
28
-
-
33846576140
-
HSP90-like artificial chaperone activity based on indole β-cyclodextrin
-
DOI 10.1016/j.bmc.2006.12.040, PII S0968089606010455
-
M. Toda, H. Itoh, Y. Kondo, and F. Hamada HSP90-like artificial chaperone activity based on indole beta-cyclodextrin Bioorganic & Medicinal Chemistry 15 2007 1983 1988 (Pubitemid 46176632)
-
(2007)
Bioorganic and Medicinal Chemistry
, vol.15
, Issue.5
, pp. 1983-1988
-
-
Toda, M.1
Itoh, H.2
Kondo, Y.3
Hamada, F.4
-
29
-
-
42549129620
-
The mechanisms underlying the effect of α-cyclodextrin on the aggregation and stability of alcohol dehydrogenase
-
DOI 10.1042/BA20070031
-
A. Barzegar, A.A. Moosavi-Movahedi, S. Rezaei-Zarchi, A.A. Saboury, M.R. Ganjali, P. Norouzi, G.H. Hakimelahi, and F.Y. Tsai The mechanisms underlying the effect of alpha-cyclodextrin on the aggregation and stability of alcohol dehydrogenase Biotechnology and Applied Biochemistry 49 2008 203 211 (Pubitemid 351579072)
-
(2008)
Biotechnology and Applied Biochemistry
, vol.49
, Issue.3-4
, pp. 203-211
-
-
Barzegar, A.1
Moosavi-Movahedi, A.A.2
Rezaei-Zarchi, S.3
Saboury, A.A.4
Ganjali, M.R.5
Norouzi, P.6
Hakimelahi, G.H.7
Tsai, F.-Y.8
-
30
-
-
77951977567
-
Thermal stability and aggregation of creatine kinase from rabbit skeletal muscle. Effect of 2-hydroxypropyl-beta-cyclodextrin
-
O.I. Maloletkina, K.A. Markossian, L.V. Belousova, S.Y. Kleimenov, V.N. Orlov, V.F. Makeeva, and B.I. Kurganov Thermal stability and aggregation of creatine kinase from rabbit skeletal muscle. Effect of 2-hydroxypropyl-beta- cyclodextrin Biophysical Chemistry 148 2010 121 130
-
(2010)
Biophysical Chemistry
, vol.148
, pp. 121-130
-
-
Maloletkina, O.I.1
Markossian, K.A.2
Belousova, L.V.3
Kleimenov, S.Y.4
Orlov, V.N.5
Makeeva, V.F.6
Kurganov, B.I.7
-
32
-
-
0014954349
-
Enzyme inactivation with ultraviolet laser energy (2650 angstroms)
-
M.W. Berns, S.I. Matsui, R.S. Olson, and D.E. Rounds Enzyme inactivation with ultraviolet laser energy (2650 angstroms) Science 169 1970 1215 1217
-
(1970)
Science
, vol.169
, pp. 1215-1217
-
-
Berns, M.W.1
Matsui, S.I.2
Olson, R.S.3
Rounds, D.E.4
-
33
-
-
0014771842
-
Photochemical reactions in amino acid residues and inactivation of enzymes during U.V.-Irradiation
-
Y.A. Vladimirov, D.I. Roshchupkin, and E.E. Fesenko Photochemical reactions in amino acid residues and inactivation of enzymes during U.V.-irradiation Photochemistry and Photobiology 11 1970 227 246
-
(1970)
Photochemistry and Photobiology
, vol.11
, pp. 227-246
-
-
Vladimirov, Y.A.1
Roshchupkin, D.I.2
Fesenko, E.E.3
-
34
-
-
0036179134
-
High probability of disrupting a disulphide bridge mediated by an endogenous excited tryptophan residue
-
DOI 10.1110/ps.06002
-
M.T. Neves-Petersen, Z. Gryczynski, J. Lakowicz, P. Fojan, S. Pedersen, E. Petersen, and S. Bjorn Petersen High probability of disrupting a disulphide bridge mediated by an endogenous excited tryptophan residue Protein Science 11 2002 588 600 (Pubitemid 34171263)
-
(2002)
Protein Science
, vol.11
, Issue.3
, pp. 588-600
-
-
Neves-Petersen, M.T.1
Gryczynski, Z.2
Lakowicz, J.3
Fojan, P.4
Pedersen, S.5
Petersen, E.6
Petersen, S.B.7
-
35
-
-
34250005406
-
Irradiation of GAPDH: A model for environmentally induced protein damage
-
DOI 10.1515/BC.2007.068
-
P. Voss, H. Hajimiragha, M. Engels, C. Ruhwiedel, C. Calles, P. Schroeder, and T. Grune Irradiation of GAPDH: a model for environmentally induced protein damage Biological Chemistry 388 2007 583 592 (Pubitemid 46883448)
-
(2007)
Biological Chemistry
, vol.388
, Issue.6
, pp. 583-592
-
-
Voss, P.1
Hajimiragha, H.2
Engels, M.3
Ruhwiedel, C.4
Calles, C.5
Schroeder, P.6
Grune, T.7
-
36
-
-
0020439065
-
Purification of all glycolytic enzymes from one muscle extract
-
R.K. Scopes, and A. Stoter Purification of all glycolytic enzymes from one muscle extract Methods in Enzymology 90 Pt E 1982 479 490
-
(1982)
Methods in Enzymology
, vol.90
, Issue.PART E
, pp. 479-490
-
-
Scopes, R.K.1
Stoter, A.2
-
37
-
-
0015257118
-
Molar absorptivity and A 1 cm 1 percent values for proteins at selected wavelengths of the ultraviolet and visible region
-
D.M. Kirschenbaum Molar absorptivity and A 1 cm 1 percent values for proteins at selected wavelengths of the ultraviolet and visible region International Journal of Protein Research 4 1972 63 73
-
(1972)
International Journal of Protein Research
, vol.4
, pp. 63-73
-
-
Kirschenbaum, D.M.1
-
38
-
-
0018413277
-
Isolation and physical characterization of bovine lens crystallins
-
S.H. Chiou, P. Azari, M.E. Himmel, and P.G. Squire Isolation and physical characterization of bovine lens crystallins International Journal of Peptide and Protein Research 13 1979 409 417 (Pubitemid 9184587)
-
(1979)
International Journal of Peptide and Protein Research
, vol.13
, Issue.4
, pp. 409-417
-
-
Chiou, S.H.1
Azari, P.2
Himmel, M.E.3
Squire, P.G.4
-
39
-
-
0038529737
-
low- and individual γ-crystallins
-
DOI 10.1074/jbc.M208157200
-
T. Putilina, F. Skouri-Panet, K. Prat, N.H. Lubsen, and A. Tardieu Subunit exchange demonstrates a differential chaperone activity of calf alpha-crystallin toward beta LOW- and individual gamma-crystallins Journal of Biological Chemistry 278 2003 13747 13756 (Pubitemid 36799911)
-
(2003)
Journal of Biological Chemistry
, vol.278
, Issue.16
, pp. 13747-13756
-
-
Putilina, T.1
Skouri-Panet, F.2
Prat, K.3
Lubsen, N.H.4
Tardieu, A.5
-
40
-
-
33744809773
-
Macromolecular size-and-shape distributions by sedimentation velocity analytical ultracentrifugation
-
DOI 10.1529/biophysj.106.081372
-
P.H. Brown, and P. Schuck Macromolecular size-and-shape distributions by sedimentation velocity analytical ultracentrifugation Biophysical Journal 90 2006 4651 4661 (Pubitemid 43830909)
-
(2006)
Biophysical Journal
, vol.90
, Issue.12
, pp. 4651-4661
-
-
Brown, P.H.1
Schuck, P.2
-
41
-
-
0032014876
-
Kinetics of heat aggregation of proteins
-
B.I. Kurganov Kinetics of heat aggregation of proteins Biochemistry (Mosc) 63 1998 364 366 (Pubitemid 128588274)
-
(1998)
Biochemistry (Moscow)
, vol.63
, Issue.3
, pp. 364-366
-
-
Kurganov, B.I.1
-
43
-
-
0001665043
-
Limits of the fractal dimension for irreversible kinetic aggregation of gold colloids
-
D.A. Weitz, J.S. Huang, M.Y. Lin, and J. Sung Limits of the fractal dimension for irreversible kinetic aggregation of gold colloids Physical Review Letters 54 1985 1416 1419
-
(1985)
Physical Review Letters
, vol.54
, pp. 1416-1419
-
-
Weitz, D.A.1
Huang, J.S.2
Lin, M.Y.3
Sung, J.4
-
44
-
-
28244447465
-
L-crystallin by α-crystallin
-
DOI 10.1021/bi051175u
-
H.A. Khanova, K.A. Markossian, B.I. Kurganov, A.M. Samoilov, S.Y. Kleimenov, D.I. Levitsky, I.K. Yudin, A.C. Timofeeva, K.O. Muranov, and M.A. Ostrovsky Mechanism of chaperone-like activity. Suppression of thermal aggregation of betaL-crystallin by alpha-crystallin Biochemistry 44 2005 15480 15487 (Pubitemid 41706131)
-
(2005)
Biochemistry
, vol.44
, Issue.47
, pp. 15480-15487
-
-
Khanova, H.A.1
Markossian, K.A.2
Kurganov, B.I.3
Samoilov, A.M.4
Kleimenov, S.Y.5
Levitsky, D.I.6
Yudin, I.K.7
Timofeeva, A.C.8
Muranov, K.O.9
Ostrovsky, M.A.10
-
46
-
-
85037669743
-
Scientist for Experimental Data Fitting
-
MicroMath, Inc. Salt Lake City
-
Scientist for Experimental Data Fitting Microsoft Windows Version 2.0 1995 MicroMath, Inc. Salt Lake City
-
(1995)
Microsoft Windows Version 2.0
-
-
-
47
-
-
78650545398
-
Mechanism of aggregation of UV-irradiated beta(L)-crystallin
-
K.O. Muranov, O.I. Maloletkina, N.B. Poliansky, K.A. Markossian, S.Y. Kleymenov, S.P. Rozhkov, A.S. Goryunov, M.A. Ostrovsky, and B.I. Kurganov Mechanism of aggregation of UV-irradiated beta(L)-crystallin Experimental Eye Research 92 2011 76 86
-
(2011)
Experimental Eye Research
, vol.92
, pp. 76-86
-
-
Muranov, K.O.1
Maloletkina, O.I.2
Poliansky, N.B.3
Markossian, K.A.4
Kleymenov, S.Y.5
Rozhkov, S.P.6
Goryunov, A.S.7
Ostrovsky, M.A.8
Kurganov, B.I.9
-
48
-
-
0008457291
-
The effect of temperature on the ultraviolet light inactivation of trypsin
-
R. Setlow, and B. Doyle The effect of temperature on the ultraviolet light inactivation of trypsin Archives of Biochemistry and Biophysics 48 1954 441 447
-
(1954)
Archives of Biochemistry and Biophysics
, vol.48
, pp. 441-447
-
-
Setlow, R.1
Doyle, B.2
-
49
-
-
4243331887
-
The action of monochromatic ultraviolet light on proteins
-
R. Setlow, and B. Doyle The action of monochromatic ultraviolet light on proteins Biochimica et Biophysica Acta 24 1957 27 41
-
(1957)
Biochimica et Biophysica Acta
, vol.24
, pp. 27-41
-
-
Setlow, R.1
Doyle, B.2
-
50
-
-
82955240594
-
Does the crowded cell-like environment reduce the chaperone-like activity of alpha-crystallin?
-
S.G. Roman, N.A. Chebotareva, T.B. Eronina, S.Y. Kleymenov, V.F. Makeeva, N.B. Poliansky, K.O. Muranov, and B.I. Kurganov Does the crowded cell-like environment reduce the chaperone-like activity of alpha-crystallin? Biochemistry 50 2011 10607 10623
-
(2011)
Biochemistry
, vol.50
, pp. 10607-10623
-
-
Roman, S.G.1
Chebotareva, N.A.2
Eronina, T.B.3
Kleymenov, S.Y.4
Makeeva, V.F.5
Poliansky, N.B.6
Muranov, K.O.7
Kurganov, B.I.8
-
51
-
-
0004164826
-
Allosteric enzymes
-
John Wiley & Sons Chichester
-
B.I. Kurganov Allosteric enzymes Kinetic Behaviour 1982 John Wiley & Sons Chichester
-
(1982)
Kinetic Behaviour
-
-
Kurganov, B.I.1
-
52
-
-
0013822457
-
Heat denaturation of lactate dehydrogenase (L-lactate: NAD-oxidoreductase, EC 1.1.1.27) and d-glyceraldehyde-3-phosphate dehydrogenase (d-glyceraldehyde-3-phosphate: NAD-oxidoreductase, EC 1.2.1.12) from rabbit muscle
-
B.I. Kurganov, and A.I. Agatova Heat denaturation of lactate dehydrogenase (L-lactate: NAD-oxidoreductase, EC 1.1.1.27) and d-glyceraldehyde-3-phosphate dehydrogenase (d-glyceraldehyde-3-phosphate: NAD-oxidoreductase, EC 1.2.1.12) from rabbit muscle Biofizika 10 1965 755 762
-
(1965)
Biofizika
, vol.10
, pp. 755-762
-
-
Kurganov, B.I.1
Agatova, A.I.2
-
53
-
-
34548120750
-
Evidence for the formation of start aggregates as an initial stage of protein aggregation
-
DOI 10.1016/j.febslet.2007.07.066, PII S0014579307008447
-
N. Golub, A. Meremyanin, K. Markossian, T. Eronina, N. Chebotareva, R. Asryants, V. Muronets, and B. Kurganov Evidence for the formation of start aggregates as an initial stage of protein aggregation FEBS Letters 581 2007 4223 4227 (Pubitemid 47301856)
-
(2007)
FEBS Letters
, vol.581
, Issue.22
, pp. 4223-4227
-
-
Golub, N.1
Meremyanin, A.2
Markossian, K.3
Eronina, T.4
Chebotareva, N.5
Asryants, R.6
Muronets, V.7
Kurganov, B.8
-
54
-
-
33846290093
-
Mechanism of chaperone-like activity
-
T.R. Obalinsky, Nova Science Publishers Inc. NY
-
K.A. Markossian, B.I. Kurganov, D.I. Levitsky, H.A. Khanova, N.A. Chebotareva, A.M. Samoilov, T.B. Eronina, N.V. Fedurkina, L.G. Mitskevich, A.V. Merem'yanin, S.Y. Kleymenov, V.F. Makeeva, V.I. Muronets, I.N. Naletova, I.N. Shalova, R.A. Asryants, E.V. Schmalhausen, L. Saso, Y.V. Panyukov, E.N. Dobrov, I.K. Yudin, K.O. Muranov, A.C. Timofeeva, and M.A. Ostrovsky Mechanism of chaperone-like activity T.R. Obalinsky, Protein Folding: New Research 2006 Nova Science Publishers Inc. NY 89 171
-
(2006)
Protein Folding: New Research
, pp. 89-171
-
-
Markossian, K.A.1
Kurganov, B.I.2
Levitsky, D.I.3
Khanova, H.A.4
Chebotareva, N.A.5
Samoilov, A.M.6
Eronina, T.B.7
Fedurkina, N.V.8
Mitskevich, L.G.9
Merem'Yanin, A.V.10
Kleymenov, S.Y.11
Makeeva, V.F.12
Muronets, V.I.13
Naletova, I.N.14
Shalova, I.N.15
Asryants, R.A.16
Schmalhausen, E.V.17
Saso, L.18
Panyukov, Y.V.19
Dobrov, E.N.20
Yudin, I.K.21
Muranov, K.O.22
Timofeeva, A.C.23
Ostrovsky, M.A.24
more..
-
55
-
-
38949188930
-
Kinetics of thermal aggregation of glycogen phosphorylase b from rabbit skeletal muscle: Mechanism of protective action of α-crystallin
-
DOI 10.1002/bip.20872
-
A.V. Meremyanin, T.B. Eronina, N.A. Chebotareva, and B.I. Kurganov Kinetics of thermal aggregation of glycogen phosphorylase b from rabbit skeletal muscle. Mechanism of protective action of alpha-crystallin Biopolymers 89 2008 124 134 (Pubitemid 351211643)
-
(2008)
Biopolymers
, vol.89
, Issue.2
, pp. 124-134
-
-
Meremyanin, A.V.1
Eronina, T.B.2
Chebotareva, N.A.3
Kurganov, B.I.4
-
56
-
-
0025905723
-
Use of 2-hydroxypropyl-beta-cyclodextrin as a solubilizing and stabilizing excipient for protein drugs
-
M.E. Brewster, M.S. Hora, J.W. Simpkins, and N. Bodor Use of 2-hydroxypropyl-beta-cyclodextrin as a solubilizing and stabilizing excipient for protein drugs Pharmaceutical Research 8 1991 792 795
-
(1991)
Pharmaceutical Research
, vol.8
, pp. 792-795
-
-
Brewster, M.E.1
Hora, M.S.2
Simpkins, J.W.3
Bodor, N.4
-
57
-
-
0032949245
-
A central composite design to investigate the thermal stabilization of lysozyme
-
DOI 10.1023/A:1018876625126
-
S. Branchu, R.T. Forbes, P. York, and H. Nyqvist A central composite design to investigate the thermal stabilization of lysozyme Pharmaceutical Research 16 1999 702 708 (Pubitemid 29227101)
-
(1999)
Pharmaceutical Research
, vol.16
, Issue.5
, pp. 702-708
-
-
Branchu, S.1
Forbes, R.T.2
York, P.3
Nyqvist, H.N.4
-
58
-
-
0036084634
-
Structural basis for cyclodextrins' suppression of human growth hormone aggregation
-
DOI 10.1110/ps.0202702
-
D.E. Otzen, B.R. Knudsen, F. Aachmann, K.L. Larsen, and R. Wimmer Structural basis for cyclodextrins' suppression of human growth hormone aggregation Protein Science 11 2002 1779 1787 (Pubitemid 34663557)
-
(2002)
Protein Science
, vol.11
, Issue.7
, pp. 1779-1787
-
-
Otzen, D.E.1
Knudsen, B.R.2
Aachmann, F.3
Larsen, K.L.4
Wimmer, R.5
-
59
-
-
1442359491
-
Structural background of cyclodextrin-protein interactions
-
F.L. Aachmann, D.E. Otzen, K.L. Larsen, and R. Wimmer Structural background of cyclodextrin-protein interactions Protein Engineering 16 2003 905 912 (Pubitemid 38281740)
-
(2003)
Protein Engineering
, vol.16
, Issue.12
, pp. 905-912
-
-
Aachmann, F.L.1
Otzen, D.E.2
Larsen, K.L.3
Wimmer, R.4
-
60
-
-
1842480055
-
Melittin as Model System for Probing Interactions between Proteins and Cyclodextrins
-
DOI 10.1002/prot.20036
-
M. Khajehpour, T. Troxler, V. Nanda, and J.M. Vanderkooi Melittin as model system for probing interactions between proteins and cyclodextrins Proteins 55 2004 275 287 (Pubitemid 38437487)
-
(2004)
Proteins: Structure, Function and Genetics
, vol.55
, Issue.2
, pp. 275-287
-
-
Khajehpour, M.1
Troxler, T.2
Nanda, V.3
Vanderkooi, J.M.4
-
61
-
-
72649083567
-
Chaperone-like activity of alpha-cyclodextrin via hydrophobic nanocavity to protect native structure of ADH
-
A. Barzegar, A.A. Moosavi-Movahedi, K. Mahnam, and S.H. Ashtiani Chaperone-like activity of alpha-cyclodextrin via hydrophobic nanocavity to protect native structure of ADH Carbohydrate Research 345 2010 213 249
-
(2010)
Carbohydrate Research
, vol.345
, pp. 213-249
-
-
Barzegar, A.1
Moosavi-Movahedi, A.A.2
Mahnam, K.3
Ashtiani, S.H.4
-
62
-
-
77951605340
-
The effects of substituted cyclodextrins on the colloidal and conformational stability of selected proteins
-
H.S. Samra, F. He, A. Bhambhani, J.D. Pipkin, R. Zimmerer, S.B. Joshi, and C.R. Middaugh The effects of substituted cyclodextrins on the colloidal and conformational stability of selected proteins Journal of Pharmaceutical Sciences 99 2010 2800 2818
-
(2010)
Journal of Pharmaceutical Sciences
, vol.99
, pp. 2800-2818
-
-
Samra, H.S.1
He, F.2
Bhambhani, A.3
Pipkin, J.D.4
Zimmerer, R.5
Joshi, S.B.6
Middaugh, C.R.7
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