About: Sergii Afonin

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An Entity of Type : wikibase:Item, within Data Space : wikidata.demo.openlinksw.com associated with source document(s)

researcher

Attributes	Values
rdf:type	Item
description	researcher (en) 연구원 (ko) ricercatore (it) গবেষক (bn) 研究者 (ja) ഗവേഷകൻ (ml) araştırmacı (tr) wetenschapper (nl) дослідник (uk) эрдэмтэн (mn) वैज्ञानिक (hi) 研究者 (zh) հետազոտող (hy) hulumtues (sq)
rdfs:label	Sergii Afonin (en) Sergii Afonin (es) Sergii Afonin (nl) Sergii Afonin (sl) Sergii Afonin (ast)
skos:prefLabel	Sergii Afonin (en) Sergii Afonin (es) Sergii Afonin (nl) Sergii Afonin (sl) Sergii Afonin (ast)
name	Sergii Afonin (en) Sergii Afonin (es) Sergii Afonin (nl) Sergii Afonin (sl) Sergii Afonin (ast)
Scopus author ID	wds:Q42199053-10176753-B101-4D04-9A60-D8CC843E1D26
Scopus author ID	7004356499
given name	wds:Q42199053-CDE0D40E-E198-43D4-AF82-F3BCFBC4395D
given name	Sergii
instance of	wds:Q42199053-A27D7283-8E08-4254-BF74-F8519EE8FD8B
instance of	Homo sapiens
Loop ID	wds:Q42199053-954EB221-6938-46A2-ADE2-F9D0EF8A7CB7
Loop ID	348524
Nationale Thesaurus voor Auteursnamen ID	wds:Q42199053-def3f24b-ab19-4f8a-8d73-88f32eee3b82
occupation	wds:Q42199053-347E7E21-817A-4996-8E5D-B490F158DE2F
NUKAT ID	wds:Q42199053-3662CB21-6F98-41EF-A244-2BFE6E46258A
sex or gender	wds:Q42199053-9BD458B9-FE15-4706-AB75-75E96032591B
ISNI	wds:Q42199053-E1675459-2744-4B25-9831-322940D19738
VIAF ID	wds:Q42199053-F5DA9450-CC95-40D0-B867-743BBB1174CB
Library of Congress authority ID	wds:Q42199053-CB8F7149-5BA9-4735-A58F-ABA31C710845
IdRef ID	wds:Q42199053-9C7B0AC2-7E75-4F41-B6A5-FDE361742E1F
family name	wds:Q42199053-79179739-9B5E-44FE-90D1-8F24CB2506AD
WorldCat Identities ID (superseded)	wds:Q42199053-AB2AF27C-6632-483B-9FBF-9F79160DFBB7
Nationale Thesaurus voor Auteursnamen ID	http://data.bibliotheken.nl/id/thes/p338803335
VIAF ID	http://viaf.org/viaf/102629530
Library of Congress authority ID	http://id.loc.gov/authorities/names/no2011173533
IdRef ID	http://www.idref.fr/164632182/id
Nationale Thesaurus voor Auteursnamen ID	338803335
occupation	researcher
NUKAT ID	n2008036831
sex or gender	male
ISNI	0000000116950527
VIAF ID	102629530
Library of Congress authority ID	no2011173533
IdRef ID	164632182
family name	Afonin
WorldCat Identities ID (superseded)	lccn-no2011173533
ORCID iD	wds:Q42199053-456369A0-5B33-477F-8971-02B90D78D541
ORCID iD	https://orcid.org/0000-0002-2356-4226
ORCID iD	0000-0002-2356-4226
Mendeley person ID	wds:Q42199053-86C64529-42A1-4B07-9C76-17E965C380E9
Mendeley person ID	sergii-afonin
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q42199053
is author of	Spatial structure of heptapeptide Aβ(16-22) (beta-amyloid Aβ(1-40) active fragment) in solution and in complex with a biological membrane model Structural role of tyrosine in Bombyx mori silk fibroin, studied by solid-state NMR and molecular mechanics on a model peptide prepared as silk I and II. Structure analysis of the membrane-bound PhoD signal peptide of the Tat translocase shows an N-terminal amphiphilic helix. Chemical labeling strategy with (R)- and (S)-trifluoromethylalanine for solid state 19F NMR analysis of peptaibols in membranes 19F NMR Analysis of the Antimicrobial Peptide PGLa Bound to Native Cell Membranes from Bacterial Protoplasts and Human Erythrocytes Peptoidic amino- and guanidinium-carrier systems: targeted drug delivery into the cell cytosol or the nucleus Optimized Protocol for Synthesis of Cyclic Gramicidin S: Starting Amino Acid Is Key to High Yield Concentration-dependent realignment of the antimicrobial peptide PGLa in lipid membranes observed by solid-state 19F-NMR. 'Boomerang'-like insertion of a fusogenic peptide in a lipid membrane revealed by solid-state 19F NMR. Using a Sterically Restrictive Amino Acid as a19F NMR label To Monitor and To Control Peptide Aggregation in Membranes Evaluating the amino acid CF3-bicyclopentylglycine as a new label for solid-state19F-NMR structure analysis of membrane-bound peptides Structure analysis and conformational transitions of the cell penetrating peptide transportan 10 in the membrane-bound state The ability of Aneurinibacillus migulanus (Bacillus brevis) to produce the antibiotic gramicidin S is correlated with phenotype variation Coding and decoding libraries of sequence-defined functional copolymers synthesized via photoligation Erratum: Coding and decoding libraries of sequence-defined functional copolymers synthesized via photoligation 4-fluorophenylglycine as a label for 19F NMR structure analysis of membrane-associated peptides Folding and self-assembly of the TatA translocation pore based on a charge zipper mechanism Compatibility of the conformationally rigid CF3-Bpg side chain with the hydrophobic coiled-coil interface Temperature-dependent transmembrane insertion of the amphiphilic peptide PGLa in lipid bilayers observed by solid state 19F NMR spectroscopy A critical evaluation of the conformational requirements of fusogenic peptides in membranes Structural role of the conserved cysteines in the dimerization of the viral transmembrane oncoprotein E5. The cell-penetrating peptide TAT(48-60) induces a non-lamellar phase in DMPC membranes Highly reactive bis-cyclooctyne-modified diarylethene for SPAAC-mediated cross-linking Controlling biological activity with light: diarylethene-containing cyclic peptidomimetics Solid-state (19)F-NMR of peptides in native membranes. Fermentation and Cost-Effective 13C/15N Labeling of the Nonribosomal Peptide Gramicidin S for Nuclear Magnetic Resonance Structure Analysis 19F NMR screening of unrelated antimicrobial peptides shows that membrane interactions are largely governed by lipids Solid State NMR Structure Analysis of the Antimicrobial Peptide Gramicidin S in Lipid Membranes: Concentration-Dependent Re-alignment and Self-Assembly as a β-Barrel Synthesis of trifluoromethyl-substituted proline analogues as 19F NMR labels for peptides in the polyproline II conformation Conformationally Rigid Trifluoromethyl-Substituted α-Amino Acid Designed for Peptide Structure Analysis by Solid-State19F NMR Spectroscopy Curvature engineering: positive membrane curvature induced by epsin N-terminal peptide boosts internalization of octaarginine. Delivery of SiC-based nanoparticles into live cells driven by cell-penetrating peptides SAP and SAP-E

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