about
Spatial structure and dimer--monomer equilibrium of the ErbB3 transmembrane domain in DPC micellesToll-like receptor 3 transmembrane domain is able to perform various homotypic interactions: an NMR structural studyLeft-Handed Dimer of EphA2 Transmembrane Domain: Helix Packing Diversity among Receptor Tyrosine KinasesIsolation, structure elucidation, and synergistic antibacterial activity of a novel two-component lantibiotic lichenicidin from Bacillus licheniformis VK21Structural and thermodynamic insight into the process of "weak" dimerization of the ErbB4 transmembrane domain by solution NMRBuckwheat trypsin inhibitor with helical hairpin structure belongs to a new family of plant defence peptidesStructural Similarity between Defense Peptide from Wheat and Scorpion Neurotoxin Permits Rational Functional DesignRecombinant production and solution structure of lipid transfer protein from lentil Lens culinarisThe Membrane Mimetic Affects the Spatial Structure and Mobility of EGFR Transmembrane and Juxtamembrane DomainsHER2 Transmembrane Domain Dimerization Coupled with Self-Association of Membrane-Embedded Cytoplasmic Juxtamembrane RegionsA novel lipid transfer protein from the dill Anethum graveolens L.: isolation, structure, heterologous expression, and functional characteristicsMechanism and color modulation of fungal bioluminescence.Structural investigation of influenza virus hemagglutinin membrane-anchoring peptide.Spatial structure of TLR4 transmembrane domain in bicelles provides the insight into the receptor activation mechanism.Helix-helix interactions in membrane domains of bitopic proteins: Specificity and role of lipid environment.Characterization of Small Isotropic Bicelles with Various Compositions.NMR Dynamics of Transmembrane and Intracellular Domains of p75NTR in Lipid-Protein Nanodiscs.GMDP: unusual physico-chemical and biological properties of the anomeriс forms.New Disulfide-Stabilized Fold Provides Sea Anemone Peptide to Exhibit Both Antimicrobial and TRPA1 Potentiating Properties.Structural Basis of p75 Transmembrane Domain Dimerization.NMR-based approach to measure the free energy of transmembrane helix-helix interactions.The Chemical Basis of Fungal Bioluminescence.NMR relaxation parameters of methyl groups as a tool to map the interfaces of helix-helix interactions in membrane proteins.Structural investigations of recombinant urokinase growth factor-like domain.Yellow and Orange Fluorescent Proteins with Tryptophan-based Chromophores.The Conformation of the Epidermal Growth Factor Receptor Transmembrane Domain Dimer Dynamically Adapts to the Local Membrane Environment.Ligand Binding Properties of the Lentil Lipid Transfer Protein: Molecular Insight into the Possible Mechanism of Lipid Uptake.Phase Transitions in Small Isotropic Bicelles.Structural and functional characterization of alternative transmembrane domain conformations in VEGF receptor 2 activation.CARD domain of rat RIP2 kinase: Refolding, solution structure, pH-dependent behavior and protein-protein interactionsNovel Peptide Chemistry in Terrestrial Animals: Natural Luciferin Analogues from the Bioluminescent EarthwormFridericia heliotaA Novel Lipopeptaibol Emericellipsin A with Antimicrobial and Antitumor Activity Produced by the Extremophilic FungusLipid-protein nanodiscs for cell-free production of integral membrane proteins in a soluble and folded state: comparison with detergent micelles, bicelles and liposomesBehavior of Most Widely Spread Lipids in Isotropic BicellesImidazol-5-one as an Acceptor in Donor-Acceptor Cyclopropanes: Cycloaddition with AldehydesStructural basis of the transmembrane domain dimerization and rotation in the activation mechanism of the TRKA receptor by nerve growth factorArchaeal cyclopentane fragment in a surfactant's hydrophobic tail decreases the Krafft point
P50
Q24302561-2561DD37-6317-4192-86B2-F482B820D4E1Q24304035-2BB14A86-BECA-4BDC-9884-939D4E20AD61Q27660088-AC189A96-6A98-454A-B3F7-211FB63E7A07Q27662755-85E7913F-4E28-461E-9022-CAC2E2FBF715Q27679060-64A691C5-8D43-4F7F-AB7C-219E49454EF5Q27679212-837207B0-916D-4C12-BCD6-43C66E6596C6Q27682550-31F70421-374C-4F26-A966-28503D8E3594Q27685438-5A9BE667-8963-4B0F-A60E-62E5ED63D3B9Q27702254-CA97389F-D8E7-4855-980F-1D5B43D89BC8Q27702650-BD2F1111-36E3-465A-9E6B-853EBB3D9520Q27703168-79522CBA-D0D5-4F4D-BA5D-4CC633DCF3BBQ33606441-CF28C8E5-3E72-47B1-8A1E-F2E4B9200E1AQ34844439-A77EA375-C6F1-4179-82AF-24DAF6FA6508Q38650678-824880E9-800E-434A-84CD-F0A84C8A2B49Q39019152-3E962671-633D-415C-BEE2-417856FF8CA6Q39693743-C5DCC545-D886-496D-B3C6-AD64310A346FQ40627988-47CD45EC-E2C1-4192-9F6F-50198BA78636Q40760094-918DB9E4-F35A-4440-8168-8EB0CCF7F9DEQ41902001-70611D38-8B50-40A1-A925-D7AD9EFDBD49Q42431864-24B5574B-CB4C-466A-9CD0-788EB1254C32Q46687468-86A22775-A519-4C77-86F0-1B13CF3C7CC1Q46712182-5DE19D37-A3FE-4222-B28A-EA86227ACA6CQ47612253-00CC6303-0801-4FBC-B09E-728E8CBA9C95Q48019778-FC04B2D0-59DF-42D0-9E4F-7F5A0724CE81Q48120852-FDDF3040-501D-4E68-B2C7-AB2039A729C5Q48131032-4CD303D3-8C5E-4357-ADB2-08ABA133EEFCQ48155649-27BB1477-7E84-43A0-8EC6-05CA1A533024Q53445975-34A9CE37-2866-4884-8BC4-F103D6324DB8Q54341152-F8717A4C-652C-40F4-8BFC-90E4CE911A51Q57799362-524100AD-74A7-48B2-9786-78F2080DF290Q57833438-082E36AB-AE2A-438C-B175-C8891719E253Q58111875-37CED02D-E7E6-43E5-A6E8-9C479ABA5FF3Q82366185-245EE103-6A1C-475D-ACCC-E1409D01DA7DQ89166735-A8D6EA20-E3C3-4A38-81FC-39138A1D9295Q90420532-7B4B12F2-1EDC-4984-A925-ADB74CC38D8DQ91697186-7594A092-8624-4CAF-8AFB-310F5C765713Q92622973-CCC22212-892E-41A8-AECA-36EA14CE91C8
P50
description
hulumtues
@sq
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Konstantin Mineev
@en
Konstantin S. Mineev
@ast
Konstantin S. Mineev
@es
Konstantin S. Mineev
@nl
Konstantin S. Mineev
@sl
Konstantin Sergejewitsch Minejew
@de
Константин Сергеевич Минеев
@ru
type
label
Konstantin Mineev
@en
Konstantin S. Mineev
@ast
Konstantin S. Mineev
@es
Konstantin S. Mineev
@nl
Konstantin S. Mineev
@sl
Konstantin Sergejewitsch Minejew
@de
Константин Сергеевич Минеев
@ru
altLabel
Konstantin Minejew
@de
Konstantin Mineyev
@en
Konstantin S. Mineev
@en
Konstantin Sergeyevich Mineyev
@en
prefLabel
Konstantin Mineev
@en
Konstantin S. Mineev
@ast
Konstantin S. Mineev
@es
Konstantin S. Mineev
@nl
Konstantin S. Mineev
@sl
Konstantin Sergejewitsch Minejew
@de
Константин Сергеевич Минеев
@ru
P1053
E-4151-2010
P106
P1153
24279929400
P21
P31
P3829
P496
0000-0002-2418-9421