about
A novel zinc-binding fold in the helicase interaction domain of the Bacillus subtilis DnaI helicase loaderNMR Structure of the SARS-CoV Nonstructural Protein 7 in Solution at pH 6.5NMR structure of the protein NP_247299.1: comparison with the crystal structureComparison of NMR and crystal structures for the proteins TM1112 and TM1367Comparison of NMR and crystal structures highlights conformational isomerism in protein active sitespH-dependent dimerization of spider silk N-terminal domain requires relocation of a wedged tryptophan side chainStructural basis for 5'-end-specific recognition of single-stranded DNA by the R3H domain from human Sμbp-2Plasmepsin Inhibitory Activity and Structure-Guided Optimization of a Potent Hydroxyethylamine-Based Antimalarial HitCarbonic anhydrase generates CO2 and H+ that drive spider silk formation via opposite effects on the terminal domainsSequential pH-driven dimerization and stabilization of the N-terminal domain enables rapid spider silk formationStructural characterization of CspZ, a complement regulator factor H and FHL-1 binding protein from Borrelia burgdorferiDiscovery and structure-activity relationship studies of irreversible benzisothiazolinone-based inhibitors against Staphylococcus aureus sortase A transpeptidaseDiversified Structural Basis of a Conserved Molecular Mechanism for pH-Dependent Dimerization in Spider Silk N-Terminal DomainsStructural and functional analysis of BB0689 from Borrelia burgdorferi, a member of the bacterial CAP superfamilyFragment-Based Discovery of 2-Aminoquinazolin-4(3H)-ones As Novel Class Nonpeptidomimetic Inhibitors of the Plasmepsins I, II, and IVStructure of AP205 Coat Protein Reveals Circular Permutation in ssRNA BacteriophagesHigh-resolution proton-detected NMR of proteins at very fast MAS.Structure of fully protonated proteins by proton-detected magic-angle spinning NMREfficient protein production inspired by how spiders make silkRapid proton-detected NMR assignment for proteins with fast magic angle spinning.J-UNIO protocol used for NMR structure determination of the 206-residue protein NP_346487.1 from Streptococcus pneumoniae TIGR4.Structural studies of amyloid-β peptides: Unlocking the mechanism of aggregation and the associated toxicity.Transmissible amyloid.Lunasin is a redox sensitive intrinsically disordered peptide with two transiently populated α-helical regions.Structures of plasmepsin II from Plasmodium falciparum in complex with two hydroxyethylamine-based inhibitors.Out-and-back 13C-13C scalar transfers in protein resonance assignment by proton-detected solid-state NMR under ultra-fast MAS.Inhibition of carnitine acetyltransferase by mildronate, a regulator of energy metabolism.O-tert-Butyltyrosine, an NMR tag for high-molecular-weight systems and measurements of submicromolar ligand binding affinities.Is protein deuteration beneficial for proton detected solid-state NMR at and above 100 kHz magic-angle spinning?Crystal structure of Plasmodium falciparum proplasmepsin IV: the plasticity of proplasmepsins.Degree of Biomimicry of Artificial Spider Silk Spinning Assessed by NMR Spectroscopy.N-Leucinyl Benzenesulfonamides as Structurally Simplified Leucyl-tRNA Synthetase Inhibitors.NMR Spectroscopic Assignment of Backbone and Side-Chain Protons in Fully Protonated Proteins: Microcrystals, Sedimented Assemblies, and Amyloid Fibrils.Dynamic Nuclear Polarization-Enhanced Biomolecular NMR Spectroscopy at High Magnetic Field with Fast Magic-Angle Spinning.A spidroin-derived solubility tag enables controlled aggregation of a designed amyloid protein.Azole-based non-peptidomimetic plasmepsin inhibitors2-Aminoquinazolin-4(3H)-one based plasmepsin inhibitors with improved hydrophilicity and selectivityDNP NMR of Biomolecular AssembliesDNP NMR of biomolecular assembliesDegree of Biomimicry of Artificial Spider Silk Spinning Assessed by NMR Spectroscopy
P50
Q27653990-03E9BAC3-AEBE-4BD6-A537-3FCB8BFDEA01Q27664055-022BDB56-6FFC-43CC-80E2-7A8AF37AC984Q27665000-7C76CA72-AC55-4A62-ADAC-ED1C267F9DD7Q27665002-40D51430-1935-40E2-8674-84FD89211044Q27665004-E160155E-75FA-4444-8196-4BB686E4E490Q27681204-16925C5C-31E7-4E93-ABCE-D6FE10882E49Q27682399-95BFD8DC-0126-45E4-B296-D1E297942A71Q27684238-C09A2C0D-A4DA-472A-BA6B-9C5A99583AE7Q27684943-7EC19FE2-1814-492D-BD3F-4CCA28247607Q27689060-652210DE-1261-4200-8427-1BDB5B18D704Q27690007-9CB0E3E5-0A55-415D-B3B7-9D54341350B9Q27695677-864EC09A-A3ED-4E75-9933-B33E306AA635Q27700952-C88C00D2-B70F-419E-902A-2D37D55203FCQ27702207-27C94879-24F9-494A-93E9-EA2BA5C7FDEAQ27703136-9A2B7ACC-FEFA-4C3F-A7AF-C0E804112CFFQ27727982-327B6332-52F8-4D6D-A4A0-FC27F252D49FQ30372919-3C372772-440C-4B29-86A2-84416D06C86DQ30391464-D4FE35FD-4F94-4B13-BABF-98EE40A273DAQ30854561-BCB54BB0-6197-475E-8930-F0A8FE64583CQ34145228-6EA39D73-8F65-4901-A6E9-045F5F8383BBQ35007571-3C01D1F0-0DBD-43F8-BB5C-1DB0B7EAF245Q38656733-0B6D0C45-62C2-4C21-A090-A1B78A1BD5DAQ38784441-49236929-1551-4895-B355-46C777860009Q39378821-D46E482A-0D97-44EC-8E42-3284D92FE5F1Q41916277-84D58C6E-9C29-406E-B2F1-11C726639A01Q42287041-97AF7058-E19B-4A96-8F68-C548A5BFB95EQ43242725-39F44368-C865-448D-AC97-FF26589F7293Q47399114-A20C4D5C-FB27-4002-8B6A-0BB8AE173279Q47960003-281694B4-E3FD-4446-BA13-AC23301D467FQ47971046-AE377C24-38FE-4DAD-8B3E-2DE3C382A40EQ47974557-5F68B8E8-2EDC-4E2F-AC85-B8D13F473647Q49874425-2BA33BBF-DFF2-46F3-A01D-365B7FD059BBQ51316365-67B3CD68-DCCC-4872-B7CF-263980D0A5CEQ52642583-9DBCEF21-519E-4C4B-B7A1-C0FB63B75100Q52722657-E8D30ABC-FAF4-46BC-BF43-606E3DA79695Q56354403-9DD23A38-64AC-4FD9-ABC7-813988C93A5BQ56380390-D6A1927C-506A-4D70-9BAA-36E04A2EA3E4Q57067174-60E67771-6294-4A42-BE08-603DE05B1C5EQ58005328-32CF3E21-B761-4CAA-8B21-5DD1B06951BCQ58005332-84E01FF1-D051-4053-9227-C26394D92AB6
P50
description
hulumtues
@sq
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
Kristaps Jaudzems
@ast
Kristaps Jaudzems
@en
Kristaps Jaudzems
@es
Kristaps Jaudzems
@fr
Kristaps Jaudzems
@nl
Kristaps Jaudzems
@sl
type
label
Kristaps Jaudzems
@ast
Kristaps Jaudzems
@en
Kristaps Jaudzems
@es
Kristaps Jaudzems
@fr
Kristaps Jaudzems
@nl
Kristaps Jaudzems
@sl
prefLabel
Kristaps Jaudzems
@ast
Kristaps Jaudzems
@en
Kristaps Jaudzems
@es
Kristaps Jaudzems
@fr
Kristaps Jaudzems
@nl
Kristaps Jaudzems
@sl
P108
P1053
P-4403-2017
P106
P1153
26535963800
P21
P31
P3829
P496
0000-0003-3922-2447
P569
2000-01-01T00:00:00Z