about
Revisiting the mechanism of the autoactivation of the complement protease C1r in the C1 complex: structure of the active catalytic region of C1rA new potent calmodulin antagonist with arylalkylamine structure: crystallographic, spectroscopic and functional studiesFlexible segments modulate co-folding of dUTPase and nucleocapsid proteinsThe acylaminoacyl peptidase from Aeropyrum pernix K1 thought to be an exopeptidase displays endopeptidase activityC1 inhibitor serpin domain structure reveals the likely mechanism of heparin potentiation and conformational diseaseStructural and kinetic contributions of the oxyanion binding site to the catalytic activity of acylaminoacyl peptidaseProlyl oligopeptidase inhibition by N-acyl-pro-pyrrolidine-type moleculesMASP-1, a promiscuous complement protease: structure of its catalytic region reveals the basis of its broad specificityDirect contacts between conserved motifs of different subunits provide major contribution to active site organization in human and mycobacterial dUTPasesStructure and mechanism of calmodulin binding to a signaling sphingolipid reveal new aspects of lipid-protein interactionsAromatic stacking between nucleobase and enzyme promotes phosphate ester hydrolysis in dUTPaseStructure and Catalysis of Acylaminoacyl Peptidase: CLOSED AND OPEN SUBUNITS OF A DIMER OLIGOPEPTIDASEDirected Evolution Reveals the Binding Motif Preference of the LC8/DYNLL Hub Protein and Predicts Large Numbers of Novel Binders in the Human ProteomeQuantitative Characterization of the Activation Steps of Mannan-binding Lectin (MBL)-associated Serine Proteases (MASPs) Points to the Central Role of MASP-1 in the Initiation of the Complement Lectin PathwayA Self-compartmentalizing Hexamer Serine Protease from Pyrococcus Horikoshii: SUBSTRATE SELECTION ACHIEVED THROUGH MULTIMERIZATIONMonospecific Inhibitors Show That Both Mannan-binding Lectin-associated Serine Protease-1 (MASP-1) and -2 Are Essential for Lectin Pathway Activation and Reveal Structural Plasticity of MASP-2Structure and enzymatic mechanism of a moonlighting dUTPaseCatalytically distinct states captured in a crystal lattice: the substrate-bound and scavenger states of acylaminoacyl peptidase and their implications for functionalitySimultaneous binding of drugs with different chemical structures to Ca2+-calmodulin: crystallographic and spectroscopic studiesThe structure of MBL-associated serine protease-2 reveals that identical substrate specificities of C1s and MASP-2 are realized through different sets of enzyme-substrate interactions.Purification, crystallization and preliminary X-ray analysis of human mannose-binding lectin-associated serine protease-1 (MASP-1) catalytic region.Enzyme:substrate hydrogen bond shortening during the acylation phase of serine protease catalysis.Extended intermolecular interactions in a serine protease-canonical inhibitor complex account for strong and highly specific inhibition.Crystallization and preliminary crystallographic analysis of dUTPase from the φ11 helper phage of Staphylococcus aureus.Origin of problems related to Staudinger reduction in carbopeptoid syntheses.Lipophilicity of aminopyridazinone regioisomers.The structure of the complex of calmodulin with KAR-2: a novel mode of binding explains the unique pharmacology of the drug.A true autoactivating enzyme. Structural insight into mannose-binding lectin-associated serine protease-2 activations.Characterization of a novel acylaminoacyl peptidase with hexameric structure and endopeptidase activity.Structural Evidence for Non-canonical Binding of Ca2+to a Canonical EF-hand of a Conventional MyosinRadiation-damage investigation of a DNA 16-mer
P50
Q24300172-927809BD-663E-4964-BE32-046CC5D83881Q27621836-5C4565A0-A31A-43A5-8B01-211C5B5FB2C2Q27640764-1099D0E5-3FDC-4E8E-A470-1CC84AD944F8Q27644021-870D288F-FE83-424D-B6E7-94EDF337B9A7Q27644724-4B568708-1FC9-4331-AE01-C6A1A53CB4DFQ27650025-446C0256-4D72-4A34-ADE5-6D837FBE21E8Q27652891-8AA2B7AD-095B-4763-AE53-BE6125E9F25AQ27656287-A66E3A4D-05B4-4BE0-8161-EAADCFF5D8B0Q27661770-9CF3E210-F894-4962-8949-07D585BB29A4Q27662112-28A870D7-8560-4D25-BC33-A79DAB5DBBEEQ27663080-2EE9DB8F-F7BC-411F-9931-9DA718CBCC48Q27665946-5F9AA768-8266-4612-8CB5-F3D08A772D96Q27667635-5AE4EAEC-4432-4C74-A1F6-ED0F47A804A8Q27676187-7675FF3B-C9EB-4D46-B08B-05C40A5A1F00Q27677875-F1728BC8-89F5-4C1F-BB02-1A1B8C7E6C68Q27678585-E48AA726-4DAC-4390-9840-2B719668E889Q27687839-AA6932FF-4EFE-4FEF-B53C-994442817F2FQ27698250-AF5272ED-EF8A-4DC7-BBA8-009F852A040AQ27765762-052256D2-6276-4DF0-9791-01E58983C9CDQ34347919-4F70D68C-8905-4D9E-8DE5-BCDFB2530CC8Q36865997-2876863E-DF61-4409-8BD3-7DA6E44BDF37Q39007070-ABDECD37-E708-4E4C-B1DD-7FA9100B93D2Q39007074-A2A5CB0A-9892-44DD-BE2F-F3ED21B730D8Q39013773-FFC2A67A-A519-4781-A9B0-DD0159D37192Q39580760-5A1B0C81-5D21-41C5-8359-ED1738283C60Q44554618-32E05131-9BE6-463B-9957-EFB044788677Q45185616-14A061E5-BD0A-4045-ADD6-83D17BF6DC62Q46616012-E9B98496-CFDB-460B-B5D0-9A26047C0E34Q51756250-ED3DDABC-700F-4492-9148-D2C6D23E75A8Q60890688-2364C6D6-21EF-4354-B437-E6A1A3FA35C1Q91632003-D160709D-ACD9-4B0F-A035-97AC25EC10EA
P50
description
hulumtuese
@sq
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Veronika Harmat
@ast
Veronika Harmat
@en
Veronika Harmat
@es
Veronika Harmat
@fr
Veronika Harmat
@nl
Veronika Harmat
@sl
type
label
Veronika Harmat
@ast
Veronika Harmat
@en
Veronika Harmat
@es
Veronika Harmat
@fr
Veronika Harmat
@nl
Veronika Harmat
@sl
altLabel
Veronika Harmath
@en
prefLabel
Veronika Harmat
@ast
Veronika Harmat
@en
Veronika Harmat
@es
Veronika Harmat
@fr
Veronika Harmat
@nl
Veronika Harmat
@sl
P1053
B-8033-2016
P106
P1153
6603495570
P21
P31
P3829
P496
0000-0002-1866-9904
P569
2000-01-01T00:00:00Z