Lista de obras -

Amyloidogenic Propensities of Ribosomal S1 Proteins: Bioinformatics Screening and Experimental Checking

scientific article published on 22 July 2020

Antimicrobial and Amyloidogenic Activity of Peptides Synthesized on the Basis of the Ribosomal S1 Protein from Thermus Thermophilus

scientific article published on 02 September 2020

Antimicrobial and Amyloidogenic Activity of Peptides. Can Antimicrobial Peptides Be Used against SARS-CoV-2?

artículo científico publicado en 2020

Comparative Analysis of Proteomes of a Number of Nosocomial Pathogens by KEGG Modules and KEGG Pathways

artículo científico publicado en 2020

Determination of amyloid core regions of insulin analogues fibrils

artículo científico publicado en 2020

Disordered Residues and Patterns in the Protein Data Bank

scientific article published on 27 March 2020

How Quickly Do Proteins Fold and Unfold, and What Structural Parameters Correlate with These Values?

artículo científico publicado en 2020

Investigation of the Relationship between the S1 Domain and Its Molecular Functions Derived from Studies of the Tertiary Structure

artículo científico publicado en 2019

Is there codon usage bias for poly-Q stretches in the human proteome?

scientific article published on 01 February 2019

New Model for Stacking Monomers in Filamentous Actin from Skeletal Muscles of Oryctolagus cuniculus

scientific article published on 06 November 2020

Phyloproteomic Analysis of 11780 Six-Residue-Long Motifs Occurrences.

artículo científico publicado en 2015

Repeats in S1 Proteins: Flexibility and Tendency for Intrinsic Disorder.

artículo científico publicado en 2019

Structural and Functional Peculiarities of α-Crystallin

artículo científico publicado en 2020

Taxonomic distribution, repeats, and functions of the S1 domain-containing proteins as members of the OB-fold family.

artículo científico publicado en 2017

The number of domains in the ribosomal protein S1 as a hallmark of the phylogenetic grouping of bacteria

scientific article published on 22 August 2019

To Be Fibrils or To Be Nanofilms? Oligomers Are Building Blocks for Fibril and Nanofilm Formation of Fragments of Aβ Peptide.

artículo científico publicado en 2018

What is Responsible for Atypical Dependence of the Rate of Amyloid Formation on Protein Concentration: Fibril-Catalyzed Initiation of New Fibrils or Competition with Oligomers?

artículo científico publicado en 2018

Lista de obras de

Amyloidogenic Propensities of Ribosomal S1 Proteins: Bioinformatics Screening and Experimental Checking

Antimicrobial and Amyloidogenic Activity of Peptides Synthesized on the Basis of the Ribosomal S1 Protein from Thermus Thermophilus

Antimicrobial and Amyloidogenic Activity of Peptides. Can Antimicrobial Peptides Be Used against SARS-CoV-2?

Comparative Analysis of Proteomes of a Number of Nosocomial Pathogens by KEGG Modules and KEGG Pathways

Determination of amyloid core regions of insulin analogues fibrils

Disordered Residues and Patterns in the Protein Data Bank

How Quickly Do Proteins Fold and Unfold, and What Structural Parameters Correlate with These Values?

Investigation of the Relationship between the S1 Domain and Its Molecular Functions Derived from Studies of the Tertiary Structure

Is there codon usage bias for poly-Q stretches in the human proteome?

New Model for Stacking Monomers in Filamentous Actin from Skeletal Muscles of Oryctolagus cuniculus

Phyloproteomic Analysis of 11780 Six-Residue-Long Motifs Occurrences.

Repeats in S1 Proteins: Flexibility and Tendency for Intrinsic Disorder.

Structural and Functional Peculiarities of α-Crystallin

Taxonomic distribution, repeats, and functions of the S1 domain-containing proteins as members of the OB-fold family.

The number of domains in the ribosomal protein S1 as a hallmark of the phylogenetic grouping of bacteria

To Be Fibrils or To Be Nanofilms? Oligomers Are Building Blocks for Fibril and Nanofilm Formation of Fragments of Aβ Peptide.

What is Responsible for Atypical Dependence of the Rate of Amyloid Formation on Protein Concentration: Fibril-Catalyzed Initiation of New Fibrils or Competition with Oligomers?