-
2
-
-
0036809333
-
sHsps and their role in the chaperone network
-
Haslbeck M. sHsps and their role in the chaperone network. Cell Mol. Life Sci. 59 (2002) 1649-1657
-
(2002)
Cell Mol. Life Sci.
, vol.59
, pp. 1649-1657
-
-
Haslbeck, M.1
-
3
-
-
0036558366
-
Structure and properties of small heat shock proteins (sHsp) and their interaction with cytoskeleton proteins
-
Gusev N.B., Bogatcheva N.V., and Marston S.B. Structure and properties of small heat shock proteins (sHsp) and their interaction with cytoskeleton proteins. Biochemistry (Moscow) 67 (2002) 511-519
-
(2002)
Biochemistry (Moscow)
, vol.67
, pp. 511-519
-
-
Gusev, N.B.1
Bogatcheva, N.V.2
Marston, S.B.3
-
4
-
-
0035920143
-
HSP22, a new member of the small heat shock protein superfamily, interacts with mimic of phosphorylated HSP27 ((3D)HSP27)
-
Benndorf R., Sun X., Gilmont R.R., Biederman K.J., Molloy M.P., Goodmurphy C.W., Cheng H., Andrews P.C., and Welsh M.J. HSP22, a new member of the small heat shock protein superfamily, interacts with mimic of phosphorylated HSP27 ((3D)HSP27). J. Biol. Chem. 276 (2001) 26753-26761
-
(2001)
J. Biol. Chem.
, vol.276
, pp. 26753-26761
-
-
Benndorf, R.1
Sun, X.2
Gilmont, R.R.3
Biederman, K.J.4
Molloy, M.P.5
Goodmurphy, C.W.6
Cheng, H.7
Andrews, P.C.8
Welsh, M.J.9
-
6
-
-
3242776825
-
Mammalian Hsp22 is a heat-inducible small heat-shock protein with chaperone-like activity
-
Chowdary T.K., Raman B., Ramakrishna T., and Rao C.M. Mammalian Hsp22 is a heat-inducible small heat-shock protein with chaperone-like activity. Biochem. J. 381 (2004) 379-387
-
(2004)
Biochem. J.
, vol.381
, pp. 379-387
-
-
Chowdary, T.K.1
Raman, B.2
Ramakrishna, T.3
Rao, C.M.4
-
7
-
-
20544446917
-
H11 has dose-dependent and dual hypertrophic and proapoptotic function in cardiac myocytes
-
Hase M., Depre C., Vatner S.F., and Sadoshima J. H11 has dose-dependent and dual hypertrophic and proapoptotic function in cardiac myocytes. Biochem. J. 388 (2005) 475-483
-
(2005)
Biochem. J.
, vol.388
, pp. 475-483
-
-
Hase, M.1
Depre, C.2
Vatner, S.F.3
Sadoshima, J.4
-
8
-
-
38849180142
-
Structure, properties, and functions of the human small heat-shock protein HSP22 (HspB8, H11, E2IG1): a critical review
-
Shemetov A.A., Seit-Nebi A.S., and Gusev N.B. Structure, properties, and functions of the human small heat-shock protein HSP22 (HspB8, H11, E2IG1): a critical review. J. Neurosci. Res. 86 (2007) 264-269
-
(2007)
J. Neurosci. Res.
, vol.86
, pp. 264-269
-
-
Shemetov, A.A.1
Seit-Nebi, A.S.2
Gusev, N.B.3
-
9
-
-
33748892808
-
Structure and properties of K141E mutant of small heat shock protein HSP22 (HspB8, H11) that is expressed in human neuromuscular disorders
-
Kim M.V., Kasakov A.S., Seit-Nebi A.S., Marston S.B., and Gusev N.B. Structure and properties of K141E mutant of small heat shock protein HSP22 (HspB8, H11) that is expressed in human neuromuscular disorders. Arch. Biochem. Biophys. 454 (2006) 32-41
-
(2006)
Arch. Biochem. Biophys.
, vol.454
, pp. 32-41
-
-
Kim, M.V.1
Kasakov, A.S.2
Seit-Nebi, A.S.3
Marston, S.B.4
Gusev, N.B.5
-
10
-
-
35448989800
-
Effect of mutations in the β5-β7 loop on the structure and properties of human small heat shock protein HSP22 (HspB8, H11)
-
Kasakov A.S., Bukach O.V., Seit-Nebi A.S., Marston S.B., and Gusev N.B. Effect of mutations in the β5-β7 loop on the structure and properties of human small heat shock protein HSP22 (HspB8, H11). FEBS J. 274 (2007) 5628-5642
-
(2007)
FEBS J.
, vol.274
, pp. 5628-5642
-
-
Kasakov, A.S.1
Bukach, O.V.2
Seit-Nebi, A.S.3
Marston, S.B.4
Gusev, N.B.5
-
11
-
-
0036803243
-
Intrinsically unstructured proteins
-
Tompa P. Intrinsically unstructured proteins. Trends Biochem. Sci. 27 (2002) 527-533
-
(2002)
Trends Biochem. Sci.
, vol.27
, pp. 527-533
-
-
Tompa, P.1
-
12
-
-
25144472591
-
Showing your ID: intrinsic disorder as an ID for recognition, regulation and cell signaling
-
Uversky V.N., Oldfield C.J., and Dunker A.K. Showing your ID: intrinsic disorder as an ID for recognition, regulation and cell signaling. J. Mol. Recognit. 18 (2005) 343-384
-
(2005)
J. Mol. Recognit.
, vol.18
, pp. 343-384
-
-
Uversky, V.N.1
Oldfield, C.J.2
Dunker, A.K.3
-
13
-
-
0036128797
-
Natively unfolded proteins: a point where biology waits for physics
-
Uversky V.N. Natively unfolded proteins: a point where biology waits for physics. Protein Sci. 11 (2002) 739-756
-
(2002)
Protein Sci.
, vol.11
, pp. 739-756
-
-
Uversky, V.N.1
-
14
-
-
0036153571
-
What does it mean to be natively unfolded?
-
Uversky V.N. What does it mean to be natively unfolded?. Eur. J. Biochem. 269 (2002) 2-12
-
(2002)
Eur. J. Biochem.
, vol.269
, pp. 2-12
-
-
Uversky, V.N.1
-
15
-
-
0037338308
-
Interaction of the small heat shock protein with molecular mass 25 kDa (hsp25) with actin
-
Panasenko O.O., Kim M.V., Marston S.B., and Gusev N.B. Interaction of the small heat shock protein with molecular mass 25 kDa (hsp25) with actin. Eur. J. Biochem. 270 (2003) 892-901
-
(2003)
Eur. J. Biochem.
, vol.270
, pp. 892-901
-
-
Panasenko, O.O.1
Kim, M.V.2
Marston, S.B.3
Gusev, N.B.4
-
17
-
-
0032584298
-
β-Tubulin isotypes purified from bovine brain have different relative stabilities
-
Schwarz P.M., Liggins J.R., and Luduena R.F. β-Tubulin isotypes purified from bovine brain have different relative stabilities. Biochemistry 37 (1998) 4687-4692
-
(1998)
Biochemistry
, vol.37
, pp. 4687-4692
-
-
Schwarz, P.M.1
Liggins, J.R.2
Luduena, R.F.3
-
18
-
-
0017106034
-
Ultra-violet fluorescence of actin. Determination of native actin content in actin preparations
-
Turoverov K.K., Khaitlina S.Yu., and Pinaev G.P. Ultra-violet fluorescence of actin. Determination of native actin content in actin preparations. FEBS Lett. 62 (1976) 4-7
-
(1976)
FEBS Lett.
, vol.62
, pp. 4-7
-
-
Turoverov, K.K.1
Khaitlina, S.Yu.2
Pinaev, G.P.3
-
20
-
-
17144369178
-
Unfolding and refolding of the glutamine-binding protein from Escherichia coli and its complex with glutamine induced by guanidine hydrochloride
-
Staiano M., Scognamiglio V., Rossi M., D'Auria S., Stepanenko O.V., Kuznetsova I.M., and Turoverov K.K. Unfolding and refolding of the glutamine-binding protein from Escherichia coli and its complex with glutamine induced by guanidine hydrochloride. Biochemistry 44 (2005) 5625-5633
-
(2005)
Biochemistry
, vol.44
, pp. 5625-5633
-
-
Staiano, M.1
Scognamiglio, V.2
Rossi, M.3
D'Auria, S.4
Stepanenko, O.V.5
Kuznetsova, I.M.6
Turoverov, K.K.7
-
21
-
-
0021435096
-
Some aspects of studies of thermal transitions in proteins by means of their intrinsic fluorescence
-
Permyakov E.A., and Burstein W.A. Some aspects of studies of thermal transitions in proteins by means of their intrinsic fluorescence. Biophys. Chem. 19 (1984) 265-271
-
(1984)
Biophys. Chem.
, vol.19
, pp. 265-271
-
-
Permyakov, E.A.1
Burstein, W.A.2
-
22
-
-
33644945086
-
Thermal unfolding of smooth muscle and nonmuscle tropomyosin α-homodimers with alternatively spliced exons
-
Kremneva E., Nikolaeva O., Maytum R., Arutyunyan A.M., Kleimenov S.Yu., Geeves M.A., and Levitsky D.I. Thermal unfolding of smooth muscle and nonmuscle tropomyosin α-homodimers with alternatively spliced exons. FEBS J. 272 (2006) 588-600
-
(2006)
FEBS J.
, vol.272
, pp. 588-600
-
-
Kremneva, E.1
Nikolaeva, O.2
Maytum, R.3
Arutyunyan, A.M.4
Kleimenov, S.Yu.5
Geeves, M.A.6
Levitsky, D.I.7
-
23
-
-
0022555893
-
Scanning microcalorimetry in studying temperature-induced changes in proteins
-
Privalov P.L., and Potekhin S.A. Scanning microcalorimetry in studying temperature-induced changes in proteins. Methods Enzymol. 131 (1986) 4-51
-
(1986)
Methods Enzymol.
, vol.131
, pp. 4-51
-
-
Privalov, P.L.1
Potekhin, S.A.2
-
24
-
-
0037943192
-
A new set of peptide-based group heat capacities for use in protein stability calculations
-
Hackel M., Hinz H.J., and Hedwig G.R. A new set of peptide-based group heat capacities for use in protein stability calculations. J. Mol. Biol. 291 (1999) 197-213
-
(1999)
J. Mol. Biol.
, vol.291
, pp. 197-213
-
-
Hackel, M.1
Hinz, H.J.2
Hedwig, G.R.3
-
25
-
-
18844417388
-
Effects of small heat shock proteins on the thermal denaturation and aggregation of F-actin
-
Pivovarova A.V., Mikhailova V.V., Chernik I.S., Chebotareva N.A., Levitsky D.I., and Gusev N.B. Effects of small heat shock proteins on the thermal denaturation and aggregation of F-actin. Biochem. Biophys. Res. Commun. 331 (2005) 1548-1553
-
(2005)
Biochem. Biophys. Res. Commun.
, vol.331
, pp. 1548-1553
-
-
Pivovarova, A.V.1
Mikhailova, V.V.2
Chernik, I.S.3
Chebotareva, N.A.4
Levitsky, D.I.5
Gusev, N.B.6
-
26
-
-
35748965834
-
Small heat shock protein Hsp27 prevents heat-induced aggregation of F-actin by forming soluble complexes with denatured actin
-
Pivovarova A.V., Chebotareva N.A., Chernik I.S., Gusev N.B., and Levitsky D.I. Small heat shock protein Hsp27 prevents heat-induced aggregation of F-actin by forming soluble complexes with denatured actin. FEBS J. 274 (2007) 5937-5948
-
(2007)
FEBS J.
, vol.274
, pp. 5937-5948
-
-
Pivovarova, A.V.1
Chebotareva, N.A.2
Chernik, I.S.3
Gusev, N.B.4
Levitsky, D.I.5
-
28
-
-
0036382925
-
Unfolding of a leucine zipper is not a simple two-state transition
-
Dragan A.I., and Privalov P.L. Unfolding of a leucine zipper is not a simple two-state transition. J. Mol. Biol. 321 (2002) 891-908
-
(2002)
J. Mol. Biol.
, vol.321
, pp. 891-908
-
-
Dragan, A.I.1
Privalov, P.L.2
-
29
-
-
47349125891
-
Apo-parvalbumin as an intrinsically disordered protein
-
Permyakov S.E., Bakunts A.G., Denesyuk A.I., Knyazeva E.L., Uversky V.N., and Permyakov E.A. Apo-parvalbumin as an intrinsically disordered protein. Proteins 72 (2008) 822-836
-
(2008)
Proteins
, vol.72
, pp. 822-836
-
-
Permyakov, S.E.1
Bakunts, A.G.2
Denesyuk, A.I.3
Knyazeva, E.L.4
Uversky, V.N.5
Permyakov, E.A.6
-
30
-
-
63149100950
-
A designed protein as experimental model of primordial folding
-
Sadqi M., de Alba E., Perez-Jimenez R., Sanchez-Ruiz J.M., and Munoz V. A designed protein as experimental model of primordial folding. Proc. Natl. Acad. Sci. U. S. A. 106 (2009) 4127-4132
-
(2009)
Proc. Natl. Acad. Sci. U. S. A.
, vol.106
, pp. 4127-4132
-
-
Sadqi, M.1
de Alba, E.2
Perez-Jimenez, R.3
Sanchez-Ruiz, J.M.4
Munoz, V.5
-
31
-
-
0035815664
-
Evidence for a partially folded intermediate in α-synuclein fibril formation
-
Uversky V.N., Li J., and Fink A.L. Evidence for a partially folded intermediate in α-synuclein fibril formation. J. Biol. Chem. 276 (2001) 10737-10744
-
(2001)
J. Biol. Chem.
, vol.276
, pp. 10737-10744
-
-
Uversky, V.N.1
Li, J.2
Fink, A.L.3
-
32
-
-
69249222742
-
Protein secondary structure content in solution, films, and tissues: redundancy and complementarity of the information content in circular dischroism, transmission and ATR FTIR spectra
-
Goormaghtigh E., Gasper R., Benard A., Goldsztein A., and Raussens V. Protein secondary structure content in solution, films, and tissues: redundancy and complementarity of the information content in circular dischroism, transmission and ATR FTIR spectra. Biochim. Biophys. Acta 1794 (2009) 1332-1343
-
(2009)
Biochim. Biophys. Acta
, vol.1794
, pp. 1332-1343
-
-
Goormaghtigh, E.1
Gasper, R.2
Benard, A.3
Goldsztein, A.4
Raussens, V.5
-
33
-
-
0028786465
-
Dimer structure as a minimum cooperative subunit of small heat-shock proteins
-
Dudich I.V., Zav'yalova V.P., Pfeil W., Gaestel M., Zav'yalova G.A., Denesyuk A.I., and Korpela T. Dimer structure as a minimum cooperative subunit of small heat-shock proteins. Biochim. Biophys. Acta 1253 (1995) 163-168
-
(1995)
Biochim. Biophys. Acta
, vol.1253
, pp. 163-168
-
-
Dudich, I.V.1
Zav'yalova, V.P.2
Pfeil, W.3
Gaestel, M.4
Zav'yalova, G.A.5
Denesyuk, A.I.6
Korpela, T.7
-
34
-
-
42049123241
-
Small heat shock protein Hsp27 protects myosin S1 from heat-induced aggregation, but not from thermal denaturation and ATPase inactivation
-
Markov D.I., Pivovarova A.V., Chernik I.S., Gusev N.B., and Levitsky D.I. Small heat shock protein Hsp27 protects myosin S1 from heat-induced aggregation, but not from thermal denaturation and ATPase inactivation. FEBS Lett. 582 (2008) 1407-1412
-
(2008)
FEBS Lett.
, vol.582
, pp. 1407-1412
-
-
Markov, D.I.1
Pivovarova, A.V.2
Chernik, I.S.3
Gusev, N.B.4
Levitsky, D.I.5
-
35
-
-
0030590541
-
The conformational stability of α-crystallin is rather low: calorimetric results
-
Gesierich U., and Pfeil W. The conformational stability of α-crystallin is rather low: calorimetric results. FEBS Lett. 393 (1996) 151-154
-
(1996)
FEBS Lett.
, vol.393
, pp. 151-154
-
-
Gesierich, U.1
Pfeil, W.2
-
36
-
-
33846298505
-
Effect of α-crystallin on thermal denaturation and aggregation of rabbit muscle glyceraldehyde-3-phosphate dehydrogenase
-
Khanova H.A., Markossian K.A., Kleimenov S.Yu., Levitsky D.I., Chebotareva N.A., Golub N.V., Asryants R.A., Muronetz V.I., Saso L., Yudin I.K., Muranov K.O., Ostrovsky M.A., and Kurganov B.I. Effect of α-crystallin on thermal denaturation and aggregation of rabbit muscle glyceraldehyde-3-phosphate dehydrogenase. Biophys. Chem. 125 (2007) 521-531
-
(2007)
Biophys. Chem.
, vol.125
, 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
-
37
-
-
25144461582
-
Wrapping the α-crystallin domain fold in a chaperone assembly
-
Stamler R., Kappe G., Boelens W., and Slingsby C. Wrapping the α-crystallin domain fold in a chaperone assembly. J. Mol. Biol. 353 (2005) 68-79
-
(2005)
J. Mol. Biol.
, vol.353
, pp. 68-79
-
-
Stamler, R.1
Kappe, G.2
Boelens, W.3
Slingsby, C.4
-
38
-
-
0037073934
-
Experimental identifi{ligature}cation of downhill protein folding
-
Garcia-Mira M.M., Sadqi M., Fischer N., Sanchez-Ruiz J.M., and Munoz V. Experimental identifi{ligature}cation of downhill protein folding. Science 298 (2002) 2191-2195
-
(2002)
Science
, vol.298
, pp. 2191-2195
-
-
Garcia-Mira, M.M.1
Sadqi, M.2
Fischer, N.3
Sanchez-Ruiz, J.M.4
Munoz, V.5
-
39
-
-
0037111966
-
Thermodynamics and kinetics of downhill protein folding investigated with a simple statistical mechanical model
-
Munoz V. Thermodynamics and kinetics of downhill protein folding investigated with a simple statistical mechanical model. Int. J. Quant. Chem. 90 (2002) 1522-1528
-
(2002)
Int. J. Quant. Chem.
, vol.90
, pp. 1522-1528
-
-
Munoz, V.1
|