Olga M Selivanova


Ontology type: schema:Person     


Person Info

NAME

Olga M

SURNAME

Selivanova

Publications in SciGraph latest 50 shown

  • 2018-01 Ligand-Induced Reassembly of GroEL/ES Chaperone In Vitro: Visualization by Electron Microscopy in MOLECULAR BIOLOGY
  • 2018-01 Amyloid Core Wild-Type Apomyoglobin and Its Mutant Variants Is Formed by Different Regions of the Polypeptide Chain in MOLECULAR BIOLOGY
  • 2018-01 Analysis of Insulin Analogs and the Strategy of Their Further Development in BIOCHEMISTRY (MOSCOW)
  • 2018-01 Studies of the Process of Amyloid Formation by Aβ Peptide in BIOCHEMISTRY (MOSCOW)
  • 2017-02 α-Crystallins are small heat shock proteins: Functional and structural properties in BIOCHEMISTRY (MOSCOW)
  • 2016-07 Peptide Aβ(16-25) forms nanofilms in the process of its aggregation in BIOCHEMISTRY (MOSCOW)
  • 2016-07 Determination of regions involved in amyloid fibril formation for Aβ(1-40) peptide in BIOCHEMISTRY (MOSCOW)
  • 2016-05 Determination of size of folding nuclei of fibrils formed from recombinant Aβ(1-40) peptide in BIOCHEMISTRY (MOSCOW)
  • 2015-04 Supramolecular organization of Hfq-like proteins in BIOCHEMISTRY (MOSCOW)
  • 2015 Determination of the Size of the Primary and Secondary Folding Nuclei of Protofibrils from the Concentration Dependence of the Rate and the Lag-Time of Their Formation in PHYSICAL BIOLOGY OF PROTEINS AND PEPTIDES
  • 2012-12 Loops and repeats in proteins as footprints of molecular evolution in BIOCHEMISTRY (MOSCOW)
  • 2012-11 Structural polymorphism and possible pathways of amyloid fibril formation on the example of insulin protein in BIOCHEMISTRY (MOSCOW)
  • 2010-08 The S1 ribosomal protein family contains a unique conservative domain in MOLECULAR BIOLOGY
  • 2010-01 YB-1 is capable of forming extended nanofibrils in BIOCHEMISTRY (MOSCOW)
  • 2007-11 Proteolysis of ribosomal protein S1 from Escherichia coli and Thermus thermophilus leads to formation of two different fragments in BIOCHEMISTRY (MOSCOW)
  • 2007-04 Conformation of Thermus thermophilus ribosomal protein S1 in solution at different ionic strengths in BIOPHYSICS
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