about
The catalytic aspartate is protonated in the Michaelis complex formed between trypsin and an in vitro evolved substrate-like inhibitor: a refined mechanism of serine protease actionDirected 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 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-2Selective 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 activationReexamination of the recognition preference of the specificity pocket of the Abl SH3 domain.Revised mechanism of complement lectin-pathway activation revealing the role of serine protease MASP-1 as the exclusive activator of MASP-2Specificity assay of serine proteinases by reverse-phase high-performance liquid chromatography analysis of competing oligopeptide substrate library.When the surface tells what lies beneath: combinatorial phage-display mutagenesis reveals complex networks of surface-core interactions in the pacifastin protease inhibitor family.Comprehensive and quantitative mapping of energy landscapes for protein-protein interactions by rapid combinatorial scanning.High affinity small protein inhibitors of human chymotrypsin C (CTRC) selected by phage display reveal unusual preference for P4' acidic residues.Functional promiscuity of squirrel monkey growth hormone receptor toward both primate and nonprimate growth hormones.Determination of the energetics governing the regulatory step in growth hormone-induced receptor homodimerization.In silico detection of tRNA sequence features characteristic to aminoacyl-tRNA synthetase class membershipOverlapping Specificity of Duplicated Human Pancreatic Elastase 3 Isoforms and Archetypal Porcine Elastase 1 Provides Clues to Evolution of Digestive Enzymes.MASP-3 is the exclusive pro-factor D activator in resting blood: the lectin and the alternative complement pathways are fundamentally linkedDYNLL/LC8: a light chain subunit of the dynein motor complex and beyond.The emerging roles of mannose-binding lectin-associated serine proteases (MASPs) in the lectin pathway of complement and beyond.Proteinase inhibitors from desert locust, Schistocerca gregaria: engineering of both P(1) and P(1)' residues converts a potent chymotrypsin inhibitor to a potent trypsin inhibitor.Human cationic trypsinogen. Arg(117) is the reactive site of an inhibitory surface loop that controls spontaneous zymogen activation.The first semi-synthetic serine protease made by native chemical ligation.Mutant rat trypsin selectively cleaves tyrosyl peptide bonds.Novel linear motif filtering protocol reveals the role of the LC8 dynein light chain in the Hippo pathway.MASP-1 of the complement system enhances clot formation in a microvascular whole blood flow model.Cutting Edge: A New Player in the Alternative Complement Pathway, MASP-1 Is Essential for LPS-Induced, but Not for Zymosan-Induced, Alternative Pathway Activation.Structural determinants governing S100A4-induced isoform-selective disassembly of nonmuscle myosin II filaments.Two mutations in rat trypsin confer resistance against autolysis.Alteration of the specificity of ecotin, an E. coli serine proteinase inhibitor, by site directed mutagenesis.Cholesterol Crystals Activate the Lectin Complement Pathway via Ficolin-2 and Mannose-Binding Lectin: Implications for the Progression of AtherosclerosisNovel MASP-2 inhibitors developed via directed evolution of human TFPI1 are potent lectin pathway inhibitorsIntramolecular cooperativity in a protein binding site assessed by combinatorial shotgun scanning mutagenesisA redesigned genetic code for selective labeling in protein NMRDirected Evolution of Canonical Loops and Their Swapping between Unrelated Serine Proteinase Inhibitors Disprove the Interscaffolding Additivity ModelEcotin, a microbial inhibitor of serine proteases, blocks multiple complement dependent and independent microbicidal activities of human serum
P50
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P50
description
researcher ORCID ID = 0000-0001-7868-7971
@en
wetenschapper
@nl
name
Gábor Pál
@ast
Gábor Pál
@en
Gábor Pál
@es
Gábor Pál
@nl
type
label
Gábor Pál
@ast
Gábor Pál
@en
Gábor Pál
@es
Gábor Pál
@nl
prefLabel
Gábor Pál
@ast
Gábor Pál
@en
Gábor Pál
@es
Gábor Pál
@nl
P106
P1153
7005651724
P31
P496
0000-0001-7868-7971