Published in Mol Biol on March 01, 1974
Alpha-Lactalbumin: compact state with fluctuating tertiary structure? FEBS Lett (1981) 2.84
Why do globular proteins fit the limited set of folding patterns? Prog Biophys Mol Biol (1987) 2.33
A model of myoglobin self-organization. Biophys Chem (1975) 2.23
Theory of protein secondary structure and algorithm of its prediction. Biopolymers (1983) 1.78
Similarities of protein topologies: evolutionary divergence, functional convergence or principles of folding? Q Rev Biophys (1980) 1.76
The 'molten globule' state is involved in the translocation of proteins across membranes? FEBS Lett (1988) 1.41
Thermodynamic parameters of helix-coil transitions in polypeptide chains. Pure Appl Chem (1972) 1.41
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The Biorisk experiment: 13-month exposure of resting forms of organism on the outer side of the Russian Segment of the International Space Station: preliminary results. Dokl Biol Sci (2009) 1.39
Sequential mechanism of refolding of carbonic anhydrase B. FEBS Lett (1987) 1.37
"Partly folded" state, a new equilibrium state of protein molecules: four-state guanidinium chloride-induced unfolding of beta-lactamase at low temperature. Biochemistry (1994) 1.30
Compact state of a protein molecule with pronounced small-scale mobility: bovine alpha-lactalbumin. Eur Biophys J (1985) 1.29
Empirical solvent-mediated potentials hold for both intra-molecular and inter-molecular inter-residue interactions. Protein Sci (1998) 1.26
A study of apo- and holo-forms of horse liver alcohol dehydrogenase in solution by diffuse x-ray scattering. Biopolymers (1986) 1.23
Molten globule-like state of cytochrome c under conditions simulating those near the membrane surface. Biochemistry (1996) 1.21
Further evidence on the equilibrium "pre-molten globule state": four-state guanidinium chloride-induced unfolding of carbonic anhydrase B at low temperature. J Mol Biol (1996) 1.16
An early immunoreactive folding intermediate of the tryptophan synthease beta 2 subunit is a 'molten globule'. FEBS Lett (1990) 1.16
[Stages in the mechanism of self-organization of protein molecules]. Dokl Akad Nauk SSSR (1973) 1.14
Retinol-binding protein is in the molten globule state at low pH. Biochemistry (1992) 1.02
Statistical analysis of the distribution of amino acid residues among helical and non-helical regions in globular proteins. J Mol Biol (1969) 1.01
Physical reasons for secondary structure stability: alpha-helices in short peptides. Proteins (1991) 1.00
Physical nature of the phase transition in globular proteins. Calorimetric study of human alpha-lactalbumin. FEBS Lett (1986) 0.98
'Molten-globule' state accumulates in carbonic anhydrase folding. FEBS Lett (1984) 0.98
'All-or-none' mechanism of the molten globule unfolding. FEBS Lett (1992) 0.96
De novo design, synthesis and study of albebetin, a polypeptide with a predetermined three-dimensional structure. Probing the structure at the nanogram level. J Mol Biol (1992) 0.93
All-or-none solvent-induced transitions between native, molten globule and unfolded states in globular proteins. Fold Des (1996) 0.93
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An early intermediate of refolding alpha-lactalbumin forms within 20 ms. FEBS Lett (1987) 0.90
Correlation between enzyme activity and hinge-bending domain displacement in 3-phosphoglycerate kinase. Eur J Biochem (1989) 0.88
Direct energy transfer to study the 3D structure of non-native proteins: AGH complex in molten globule state of apomyoglobin. Protein Eng (1999) 0.88
A theory of protein molecule self-organization. IV. Helical and irregular local structures of unfolded protein chains. J Mol Biol (1976) 0.87
Folding intermediates are involved in genetic diseases? FEBS Lett (1995) 0.87
Binding of the globular domain of linker histones H5/H1 to the nucleosome: a hypothesis. Protein Eng (1989) 0.87
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Thermodynamic parameters of helix-coil transition in polypeptide chains. II. Poly-L-lysine. Biopolymers (1971) 0.86
Inter-domain mobility in proteins and its probable functional role. FEBS Lett (1978) 0.83
[Self-organization of the myoglobin molecule]. Dokl Akad Nauk SSSR (1973) 0.83
[Low-deuterium water effect on transplantable tumors]. Vopr Onkol (2005) 0.83
Principal folding pathway and topology of all-beta proteins. FEBS Lett (1979) 0.82
Noncooperative temperature melting of a globular protein without specific tertiary structure: acid form of bovine carbonic anhydrase B. Biopolymers (1985) 0.82
Nanosecond dynamics of tryptophans in different conformational states of apomyoglobin proteins. Biochemistry (2000) 0.82
Theory of protein molecule self-organization. I. Thermodynamic parameters of local secondary structures in the unfolded protein chain. Biopolymers (1977) 0.82
Statistical analysis of the correlation among amino acid residues in helical, beta-structural and non-regular regions of globular proteins. J Mol Biol (1971) 0.82
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The structure of ribonuclease in solution does not differ from its crystalline structure. FEBS Lett (1978) 0.81
Secondary structure of globular proteins at the early and the final stages in protein folding. FEBS Lett (1993) 0.80
[Consideration of the deuterium-free water supply to an expedition to Mars]. Aviakosm Ekolog Med (2003) 0.80
Theory of protein molecule self-organization. II. A comparison of calculated thermodynamic parameters of local secondary structures with experiments. Biopolymers (1977) 0.79
Can grafting of an octapeptide improve the structure of a de novo protein? FEBS Lett (1998) 0.79
Molten globule versus variety of intermediates: influence of anions on pH-denatured apomyoglobin. FEBS Lett (1999) 0.79
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[Medical studies during an 8-month flight on the orbital complex "Saliut-7"--"Soiuz-T"]. Kosm Biol Aviakosm Med (1990) 0.78
A synthetic polypeptide with a compact structure and its self-organization. FEBS Lett (1975) 0.78
[Protein as an edited random copolymer]. Mol Biol (Mosk) (1984) 0.78
Study of the structure of streptokinase conjugates with a hydrophilic vinylpyrrolidone copolymer. Biophys Chem (1990) 0.78
[Water-salt homeostasis and space flight]. Probl Kosm Biol (1986) 0.78
cI and lexA repressors consist of three cro-like domains. FEBS Lett (1982) 0.78
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Mechanisms of gravitational sensitivity of osteogenic precursor cells. Acta Naturae (2010) 0.78
[Fluctuating state of the protein globule]. Mol Biol (Mosk) (1983) 0.77
Release of retinol and denaturation of its plasma carrier, retinol-binding protein. Fold Des (1998) 0.77
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[Investigation into fractionating of hydrogen and oxygen stable isotopes aboard the international space station]. Aviakosm Ekolog Med (2006) 0.77
[Predicting the spiral portions of globular proteins from their primary structure]. Dokl Akad Nauk SSSR (1970) 0.77
[Medical studies concerning the program of long-term manned space flights on "Saliut-7"-"Soiuz-T" orbital complex]. Kosm Biol Aviakosm Med (1990) 0.77
[Protein globule without the unique three-dimensional structure: experimental data for alpha-lactalbumins and general model]. Biofizika (1983) 0.77
[Determination of the secondary structure of proteins from their circular dichroism spectra. I. Protein reference spectra for alpha-, beta- and irregular structures]. Mol Biol (Mosk) (1980) 0.77
[Study of calcitonin and parathyroid hormone in patients with bronchial asthma with steroid-induced osteoporosis]. Probl Endokrinol (Mosk) (1984) 0.77
[Changes in titin and myosin heavy chain isoform composition in skeletal muscles of Mongolian gerbil (Meriones unguiculatus) after 12-day spaceflight]. Biofizika (2012) 0.76
Cytotoxic activity of natural killer cells in vitro under microgravity. Dokl Biol Sci (2008) 0.76
Effect of duration of bed rest on water and mineral metabolism and kidney function. Hum Physiol (1980) 0.76
The structure of hydrophobic cores of globins. Mol Biol (1975) 0.76
[Preparation and study of albebetin, an artificial protein with a given spatial structure]. Dokl Akad Nauk SSSR (1991) 0.76
[Impact of the impaired intestinal microflora on the course of acne vulgaris]. Klin Med (Mosk) (2001) 0.75
[The optimization of the management of a general hospital]. Voen Med Zh (1995) 0.75
Folding and binding. From theory to therapy. Curr Opin Struct Biol (1997) 0.75
[Folding and topology of parallel beta-structure]. Biofizika (1979) 0.75
[Self-organization of protein structures--a bridge between physics and biology]. Mol Biol (Mosk) (2000) 0.75
Prediction of the three-dimensional structure for ribosomal protein L25. FEBS Lett (1975) 0.75
[Identification of alpha-spiral structure of polypeptide chains in solution by x-ray diffusion scattering]. Dokl Akad Nauk SSSR (1971) 0.75
[X-ray diffuse scattering by polypeptides and proteins in solution. IV. Consideration of the solvent effect for globular protein solutions]. Mol Biol (1976) 0.75
Dipole-dipole interaction and the beta structure of synthetic polypeptides. Biopolymers (1967) 0.75
[Compact structure of random copolymers of hydrophobic and hydrophilic amino acid residues]. Mol Biol (Mosk) (1980) 0.75
[Multicenter mechanism of self-organization of globular proteins and cooperativity of their denaturation and renaturation]. Dokl Akad Nauk SSSR (1975) 0.75
[Predicting the three-dimensional structure of alpha- and beta-interferons]. Mol Biol (Mosk) (1986) 0.75
[Protein engineering of artificial proteins]. Mol Biol (Mosk) (1996) 0.75
Structural model for interferons. FEBS Lett (1985) 0.75
[Three-stage equilibrium unfolding of small globular proteins by denaturing agents. I. Carboanhydrase B]. Mol Biol (Mosk) (1997) 0.75
[The physical principles of the self-organization of protein bonds]. Usp Sovrem Biol (1971) 0.75
[Three-stage equilibrium unfolding of small globular proteins by denaturing agents. II. Beta-lactamase and general model]. Mol Biol (Mosk) (1997) 0.75
[Letter: Helical structure of unfolded protein chains]. Biofizika (1975) 0.75
[Study of synthetic polypeptides. I. Transformations-intramolecular beta-structure coil in poly-S-carbobenzoxymethyl-L-cysteine]. Biofizika (1965) 0.75
Thermodynamic parameters of the helix-coil transition in polypeptide chains. III. Random copolymers of L-leucine and L-glutamic acid. Biopolymers (1975) 0.75
[Effect of a biologically active interferon fragment on the structure of the synthetic protein carrier]. Biofizika (1998) 0.75
[Determination of protein secondary structure from circular dichroism spectra. III. Protein-derived base spectra of circular dichroism for antiparallel and parallel beta-structures]. Mol Biol (Mosk) (1982) 0.75
[Hydrophobic interactions and nucleoprotein structure]. Biofizika (1966) 0.75
Prediction of the secondary structure of the L7, L12 proteins of the E. coli ribosome. FEBS Lett (1973) 0.75