Natural substrates and inhibitors of mannan-binding lectin-associated serine protease-1 and -2: a study on recombinant catalytic fragmentsRevisiting the mechanism of the autoactivation of the complement protease C1r in the C1 complex: structure of the active catalytic region of C1rC1 inhibitor serpin domain structure reveals the likely mechanism of heparin potentiation and conformational diseaseMASP-1, a promiscuous complement protease: structure of its catalytic region reveals the basis of its broad specificityAtomic level description of the domain closure in a dimeric enzyme: thermus thermophilus 3-isopropylmalate dehydrogenaseQuantitative 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 PathwayMonospecific 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-2Structural and energetic basis of isopropylmalate dehydrogenase enzyme catalysisGlutamate 270 plays an essential role in K(+)-activation and domain closure of Thermus thermophilus isopropylmalate dehydrogenaseImportance of aspartate residues in balancing the flexibility and fine-tuning the catalysis of human 3-phosphoglycerate kinaseSelective inhibition of the lectin pathway of complement with phage display selected peptides against mannose-binding lectin-associated serine protease (MASP)-1 and -2: significant contribution of MASP-1 to lectin pathway activationCalcium-dependent conformational flexibility of a CUB domain controls activation of the complement serine protease C1r
P50
Q24292975-E3776581-C664-444A-BD9A-7DDC1C4FDCEFQ24300172-C6014314-CCB9-4502-A384-AF93F18FB598Q27644724-F22C0F6C-A703-4EB9-9895-7254EA2934E8Q27656287-7AA40407-F947-4C74-9ECA-CDD1BA5C7F69Q27666894-7AF5032A-1F25-4992-A8C1-DC720105F667Q27676187-A3AA6070-6A05-42F7-9F4D-A89238A2FDE9Q27678585-4E13D070-9037-41F0-B5C7-5E31BCCDF152Q27695606-0BF82FC2-EBE8-4C00-B615-C9B463CED6E5Q27696836-01AC2B2F-ABF7-4376-A52D-670D5D0100E9Q28281258-250A2791-FC64-4E3B-B9E0-7CCACE8B1404Q28292473-0439B73E-500F-4C5F-914B-100E30CD869FQ28910359-3673161E-5C65-4006-ACB7-05A1D63B2585
P50
description
Hongaars onderzoeker (1939-)
@nl
cercetator
@ro
hulumtues
@sq
investigador húngaro
@es
investigador húngaru
@ast
kutató
@hu
researcher
@en
ricercatore
@it
taighdeoir
@ga
հետազոտող
@hy
name
Peter Zavodszky
@sq
Péter Závodszky
@ast
Péter Závodszky
@en
Péter Závodszky
@eo
Péter Závodszky
@es
Péter Závodszky
@fr
Péter Závodszky
@ga
Péter Závodszky
@nl
Péter Závodszky
@ro
Péter Závodszky
@sl
type
label
Peter Zavodszky
@sq
Péter Závodszky
@ast
Péter Závodszky
@en
Péter Závodszky
@eo
Péter Závodszky
@es
Péter Závodszky
@fr
Péter Závodszky
@ga
Péter Závodszky
@nl
Péter Závodszky
@ro
Péter Závodszky
@sl
altLabel
Peter Zavodszky
@en
Péter Závodszky
@sq
prefLabel
Peter Zavodszky
@sq
Péter Závodszky
@ast
Péter Závodszky
@en
Péter Závodszky
@eo
Péter Závodszky
@es
Péter Závodszky
@fr
Péter Závodszky
@ga
Péter Závodszky
@nl
Péter Závodszky
@ro
Péter Závodszky
@sl
P1412
P214
P19
P21
P213
0000 0000 7920 0910
P214
P27
P31
P3973
P569
1939-03-18T00:00:00Z
P735
P7859
viaf-121450232