Published in Biopolymers on January 01, 1983
On the use of sequence homologies to predict protein structure: identical pentapeptides can have completely different conformations. Proc Natl Acad Sci U S A (1984) 4.08
Improved prediction of protein secondary structure by use of sequence profiles and neural networks. Proc Natl Acad Sci U S A (1993) 3.92
Cascaded multiple classifiers for secondary structure prediction. Protein Sci (2000) 2.97
The DNA binding site of HMG1 protein is composed of two similar segments (HMG boxes), both of which have counterparts in other eukaryotic regulatory proteins. EMBO J (1992) 2.18
Modeling of the spatial structure of eukaryotic ornithine decarboxylases. Protein Sci (1995) 2.02
Identification of a new class of protein kinases represented by eukaryotic elongation factor-2 kinase. Proc Natl Acad Sci U S A (1997) 1.78
VIP36, a novel component of glycolipid rafts and exocytic carrier vesicles in epithelial cells. EMBO J (1994) 1.67
Prediction of protein folding rates from the amino acid sequence-predicted secondary structure. Proc Natl Acad Sci U S A (2004) 1.28
MyfF, an element of the network regulating the synthesis of fibrillae in Yersinia enterocolitica. J Bacteriol (1995) 1.22
Structure-based conformational preferences of amino acids. Proc Natl Acad Sci U S A (1999) 1.13
Members of the zinc finger protein gene family sharing a conserved N-terminal module. Nucleic Acids Res (1991) 1.12
Antigenic domains of the open reading frame 2-encoded protein of hepatitis E virus. J Clin Microbiol (1999) 1.08
Primary and secondary structure of the pore-forming peptide of pathogenic Entamoeba histolytica. EMBO J (1992) 1.04
Computational studies reveal phosphorylation-dependent changes in the unstructured R domain of CFTR. J Mol Biol (2008) 1.01
Interaction of the 47-kDa talin fragment and the 32-kDa vinculin fragment with acidic phospholipids: a computer analysis. Biophys J (1995) 0.97
The in situ spatial arrangement of the influenza A virus matrix protein M1 assessed by tritium bombardment. Proc Natl Acad Sci U S A (1999) 0.95
Pseudodihedrals: simplified protein backbone representation with knowledge-based energy. Protein Sci (1994) 0.93
Characteristics of a de novo designed protein. Protein Sci (1994) 0.89
Acetylcholine receptor-alpha-bungarotoxin interactions: determination of the region-to-region contacts by peptide-peptide interactions and molecular modeling of the receptor cavity. Proc Natl Acad Sci U S A (1990) 0.87
A hybrid genetic-neural system for predicting protein secondary structure. BMC Bioinformatics (2005) 0.81
Studies on secondary structure of caldesmon and its C-terminal fragments. Biochem J (1993) 0.80
Intrinsically disordered human C/EBP homologous protein regulates biological activity of colon cancer cells during calcium stress. J Mol Biol (2008) 0.79
Conformation of a protein kinase C substrate NG(28-43), and its analog in aqueous and sodium dodecyl sulfate micelle solutions. Biophys J (1997) 0.77
Unfolding of CPR3 Gets Initiated at the Active Site and Proceeds via Two Intermediates. Biophys J (2017) 0.75
A theoretical search for folding/unfolding nuclei in three-dimensional protein structures. Proc Natl Acad Sci U S A (1999) 3.02
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
The classification and origins of protein folding patterns. Annu Rev Biochem (1990) 2.30
A model of myoglobin self-organization. Biophys Chem (1975) 2.23
Theory of cooperative transitions in protein molecules. I. Why denaturation of globular protein is a first-order phase transition. Biopolymers (1989) 1.94
Similarities of protein topologies: evolutionary divergence, functional convergence or principles of folding? Q Rev Biophys (1980) 1.76
What is the probability of a chance prediction of a protein structure with an rmsd of 6 A? Fold Des (1998) 1.64
Thermodynamic parameters of helix-coil transitions in polypeptide chains. Pure Appl Chem (1972) 1.41
The 'molten globule' state is involved in the translocation of proteins across membranes? FEBS Lett (1988) 1.41
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
Comparison of predicted and experimentally determined secondary structure of adenyl kinase. Nature (1974) 1.21
Molten globule-like state of cytochrome c under conditions simulating those near the membrane surface. Biochemistry (1996) 1.21
Theory of cooperative transitions in protein molecules. II. Phase diagram for a protein molecule in solution. Biopolymers (1989) 1.20
General architecture of the alpha-helical globule. J Mol Biol (1988) 1.19
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
'Molten-globule' state accumulates in carbonic anhydrase folding. FEBS Lett (1984) 0.98
Physical nature of the phase transition in globular proteins. Calorimetric study of human alpha-lactalbumin. FEBS Lett (1986) 0.98
'All-or-none' mechanism of the molten globule unfolding. FEBS Lett (1992) 0.96
Folding nuclei in proteins. FEBS Lett (2001) 0.95
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
Folding of circular permutants with decreased contact order: general trend balanced by protein stability. J Mol Biol (2001) 0.93
All-or-none solvent-induced transitions between native, molten globule and unfolded states in globular proteins. Fold Des (1996) 0.93
Residue-residue mean-force potentials for protein structure recognition. Protein Eng (1997) 0.93
Optimization of protein structure on lattices using a self-consistent field approach. J Comput Biol (1998) 0.93
[Relation of the secondary structure of globular proteins to their primary structure]. Biofizika (1970) 0.92
Accurate general method for lattice approximation of three-dimensional structure of a chain molecule. Proteins (1995) 0.92
Averaging interaction energies over homologs improves protein fold recognition in gapless threading. Proteins (1999) 0.91
Predicted beta-structure stability parameters under experimental test. Protein Eng (1995) 0.91
Statistical significance of protein structure prediction by threading. Proc Natl Acad Sci U S A (2000) 0.91
Constructing lattice models of protein chains with side groups. J Comput Biol (1995) 0.90
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
Folding rate dependence on the chain length of RNA-like heteropolymers. Fold Des (1998) 0.87
Binding of the globular domain of linker histones H5/H1 to the nucleosome: a hypothesis. Protein Eng (1989) 0.87
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
[Determination of the secondary structure of proteins from their circular dichroism spectra. II. Estimation of the contribution of beta-pleated sheets]. Mol Biol (Mosk) (1980) 0.86
Theoretical study of a landscape of protein folding-unfolding pathways. Folding rates at midtransition. Biochemistry (2001) 0.86
Thermodynamic parameters of helix-coil transition in polypeptide chains. II. Poly-L-lysine. Biopolymers (1971) 0.86
Recognition of protein structure on coarse lattices with residue-residue energy functions. Protein Eng (1997) 0.84
Protein design on computers. Five new proteins: Shpilka, Grendel, Fingerclasp, Leather, and Aida. Proteins (1992) 0.84
Building self-avoiding lattice models of proteins using a self-consistent field optimization. Proteins (1996) 0.83
[Self-organization of the myoglobin molecule]. Dokl Akad Nauk SSSR (1973) 0.83
Inter-domain mobility in proteins and its probable functional role. FEBS Lett (1978) 0.83
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
Prediction of protein secondary structure based on physical theory. Histones. Protein Eng (1989) 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
Noncooperative temperature melting of a globular protein without specific tertiary structure: acid form of bovine carbonic anhydrase B. Biopolymers (1985) 0.82
Principal folding pathway and topology of all-beta proteins. FEBS Lett (1979) 0.82
The structure of ribonuclease in solution does not differ from its crystalline structure. FEBS Lett (1978) 0.81
[The state of unfolded globules of protein molecules is more quickly becoming a rule, rather than an exception]. Biofizika (1993) 0.81
Search for the most stable folds of protein chains: II. Computation of stable architectures of beta-proteins using a self-consistent molecular field theory. Protein Eng (1996) 0.81
Cunning simplicity of protein folding landscapes. Protein Eng (2001) 0.80
Secondary structure of globular proteins at the early and the final stages in protein folding. FEBS Lett (1993) 0.80
Can grafting of an octapeptide improve the structure of a de novo protein? FEBS Lett (1998) 0.79
Theory of protein molecule self-organization. II. A comparison of calculated thermodynamic parameters of local secondary structures with experiments. Biopolymers (1977) 0.79
Molten globule versus variety of intermediates: influence of anions on pH-denatured apomyoglobin. FEBS Lett (1999) 0.79
cI and lexA repressors consist of three cro-like domains. FEBS Lett (1982) 0.78
[Protein as an edited random copolymer]. Mol Biol (Mosk) (1984) 0.78
A synthetic polypeptide with a compact structure and its self-organization. FEBS Lett (1975) 0.78
Recognition of signal sequences. FEBS Lett (1983) 0.78
[Predicting the spiral portions of globular proteins from their primary structure]. Dokl Akad Nauk SSSR (1970) 0.77
[Fluctuating state of the protein globule]. Mol Biol (Mosk) (1983) 0.77
Folding nuclei in 3D protein structures. Pac Symp Biocomput (2000) 0.77
[Protein globule without the unique three-dimensional structure: experimental data for alpha-lactalbumins and general model]. Biofizika (1983) 0.77
Release of retinol and denaturation of its plasma carrier, retinol-binding protein. Fold Des (1998) 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
Folding of chains with random and edited sequences: similarities and differences. Protein Eng (1995) 0.77
[Preparation and study of albebetin, an artificial protein with a given spatial structure]. Dokl Akad Nauk SSSR (1991) 0.76
The structure of hydrophobic cores of globins. Mol Biol (1975) 0.76
How homologs can help to predict protein folds even though they cannot be predicted for individual sequences. J Comput Biol (1998) 0.76
A new approach to the design of a sequence with the highest affinity for a molecular surface. Protein Eng (1992) 0.76
Theory of protein molecule self-organization. III. A calculating method for the probabilities of the secondary structure formation in an unfolded polypeptide chain. Biopolymers (1977) 0.75
[Study of synthetic polypeptides. I. Transformations-intramolecular beta-structure coil in poly-S-carbobenzoxymethyl-L-cysteine]. Biofizika (1965) 0.75
Intermediate States of Apomyoglobin: Are They Parts of the Same Area of Conformations Diagram? Biochemistry (Mosc) (2017) 0.75
[Studies of synethtic polypeptides. II. Beta-structure--coil transition of poly-S-carboxymethyl-L-cysteine under changes of medium pH and temperature]. Biofizika (1966) 0.75
Investigations of synthetic polypeptides: transitions-intramolecular beta-structures-coil in poly-S-carbobenzoxymethyl-L-cysteine. Fed Proc Transl Suppl (1967) 0.75