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Sergei Permyakov

Leader of Protein research group (Biological sciences)

Protein research group, IBI RAS, Institutskaya str. 7, Pushchino, Moscow region, 142290 Russia

Publications

  • Parvalbumin as a metal-dependent antioxidant. PMID: 24685310
  • Structural characterization of more potent alternatives to HAMLET, a tumoricidal complex of α-lactalbumin and oleic acid. PMID: 23947814
  • Sequence microheterogeneity of parvalbumin, the major fish allergen. PMID: 23632315
  • The impact of alpha-N-acetylation on structural and functional status of parvalbumin. PMID: 22742764
  • Oxidation mimicking substitution of conservative cysteine in recoverin suppresses its membrane association. PMID: 21344177
  • Oleic acid is a key cytotoxic component of HAMLET-like complexes. PMID: 22628302
  • Synergetic effect of recoverin and calmodulin on regulation of rhodopsin kinase. PMID: 22408603
  • Differential scanning microcalorimetry of intrinsically disordered proteins. PMID: 22821532
  • Activation of H+-ATPase of the plasma membrane of Saccharomyces cerevisiae by glucose: the role of sphingolipid and lateral enzyme mobility. PMID: 22359558
  • A novel method for preparation of HAMLET-like protein complexes. PMID: 21596091
  • Intrinsic disorder in S100 proteins. PMID: 21528128
  • Involvement of the recoverin C-terminal segment in recognition of the target enzyme rhodopsin kinase. PMID: 21299498
  • Analysis of Ca2+/Mg2+ selectivity in alpha-lactalbumin and Ca(2+)-binding lysozyme reveals a distinct Mg(2+)-specific site in lysozyme. PMID: 20602456
  • Metal-controlled interdomain cooperativity in parvalbumins. PMID: 19651438
  • Interaction of antitumor alpha-lactalbumin-oleic acid complexes with artificial and natural membranes. PMID: 19588235
  • Sequence microheterogeneity of parvalbumin pI 5.0 of pike: a mass spectrometric study. PMID: 18930845
  • Who is Mr. HAMLET? Interaction of human alpha-lactalbumin with monomeric oleic acid. PMID: 19006329
  • Apo-parvalbumin as an intrinsically disordered protein. PMID: 18260106
  • Recoverin as a redox-sensitive protein. PMID: 17385906
  • The use of the free metal-temperature 'phase diagrams' for studies of single site metal binding proteins. PMID: 17136617
  • Tuning of a neuronal calcium sensor. PMID: 17015448
  • Calcium-binding and temperature induced transitions in equine lysozyme: new insights from the pCa-temperature "phase diagrams". PMID: 17022083
  • How to improve nature: study of the electrostatic properties of the surface of alpha-lactalbumin. PMID: 16093284
  • Conversion of human alpha-lactalbumin to an apo-like state in the complexes with basic poly-amino acids: toward understanding of the molecular mechanism of antitumor action of HAMLET. PMID: 15822935
  • No need to be HAMLET or BAMLET to interact with histones: binding of monomeric alpha-lactalbumin to histones and basic poly-amino acids. PMID: 15134431
  • Natively unfolded C-terminal domain of caldesmon remains substantially unstructured after the effective binding to calmodulin. PMID: 14635127
  • Ultraviolet illumination-induced reduction of alpha-lactalbumin disulfide bridges. PMID: 12784209
  • Recoverin is a zinc-binding protein. PMID: 12643543
  • Conformational prerequisites for alpha-lactalbumin fibrillation. PMID: 12369846
  • Human alpha-fetoprotein as a Zn(2+)-binding protein. Tight cation binding is not accompanied by global changes in protein structure and stability. PMID: 11781144
  • Effect of zinc and temperature on the conformation of the gamma subunit of retinal phosphodiesterase: a natively unfolded protein. PMID: 12643535
  • Mutating aspartate in the calcium-binding site of alpha-lactalbumin: effects on the protein stability and cation binding. PMID: 11739897
  • Effects of mutations in the calcium-binding sites of recoverin on its calcium affinity: evidence for successive filling of the calcium binding sites. PMID: 11161110
  • Zinc binding in bovine alpha-lactalbumin: sequence homology may not be a predictor of subtle functional features. PMID: 10813835
  • Fine tuning the N-terminus of a calcium binding protein: alpha-lactalbumin. PMID: 10451551
  • Cooperative thermal transitions of bovine and human apo-alpha-lactalbumins: evidence for a new intermediate state. PMID: 9276479
  • pH-induced transition and Zn2+-binding properties of bovine prolactin. PMID: 9108303
  • Kinetics of peptide synthesis studied by fluorescence of fluorophenyl esters. PMID: 7896506

Sergei Permyakov's public data