about
Effect of the methionine ligand on the reorganization energy of the type-1 copper site of nitrite reductaseOligomeric structure and autophosphorylation of nucleoside diphosphate kinase from rat mucosal mast cellsA cromoglycate binding protein from rat mast cells of a leukemia line is a nucleoside diphosphate kinaseA secretion inhibitory signal transduction molecule on mast cells is another C-type lectin.Long-range intramolecular electron transfer in azurinsAn unusual inhibitory receptor--the mast cell function-associated antigen (MAFA).Enhanced rate of intramolecular electron transfer in an engineered purple CuA azurinTransmembrane domains in the functions of Fc receptors.Allosteric control of internal electron transfer in cytochrome cd1 nitrite reductase.Direct binding of myelin basic protein and synthetic copolymer 1 to class II major histocompatibility complex molecules on living antigen-presenting cells--specificity and promiscuity.Trivalent antigens for degranulation of mast cells.What else can the immune system recognize?Kinetic evidence for a ligand-binding-induced conformational transition in the T cell receptorSpatial coordination of CD8 and TCR molecules controls antigen recognition by CD8+ T-cells.Electron transfer reactivity of type zero Pseudomonas aeruginosa azurin.Cloning and sequence of the cDNA coding for rat type II Fc gamma receptor of mast cells.Regulation of the mast cell response to the type 1 Fc epsilon receptor.Designed azurins show lower reorganization free energies for intraprotein electron transferTuning electronic transport via hepta-alanine peptides junction by tryptophan doping.Nitrite reduction: a ubiquitous function from a pre-aerobic past.Multicopper oxidases: intramolecular electron transfer and O2 reduction.A common mechanism of hapten binding to immunoglobulins and their heterologous chain recombinants.Long-Range Electron Transfer in Engineered Azurins Exhibits Marcus Inverted Region Behavior.Electron Transfer Proteins as Electronic Conductors: Significance of the Metal and Its Binding Site in the Blue Cu Protein, Azurin.Nanoscale electron transport and photodynamics enhancement in lipid-depleted bacteriorhodopsin monomers.C3a-derived peptide binds to the type I FcepsilonR and inhibits proximal-coupling signal processes and cytokine secretion by mast cells.Compartmentalization of the Type I Fc epsilon receptor and MAFA on mast cell membranes.Desensitization of mast cells' secretory response to an immuno-receptor stimulus.CD8 kinetically promotes ligand binding to the T-cell antigen receptor.Regulation of mast cells' secretory response by co-clustering the Type 1 Fcepsilon receptor with the mast cell function-associated antigen.Interaction of a monoclonal IgE-specific antibody with cell-surface IgE-Fc epsilon RI: characterization of equilibrium binding and secretory response.The protein tyrosine kinase syk activity is reduced by clustering the mast cell function-associated antigen.An immunoreceptor tyrosine-based inhibitory motif, with serine at site Y-2, binds SH2-domain-containing phosphatases.Efficient induction of cytotoxic CD8+ T cells against exogenous proteins: establishment and characterization of a T cell line specific for the membrane protein ActA of Listeria monocytogenes.Purification and preliminary characterization of an Fc epsilon-receptor-activated protein-tyrosine phosphatase from mast cells.Characterizing immunodominant and protective influenza hemagglutinin epitopes by functional activity and relative binding to major histocompatibility complex class II sites.Immobilization of the type I receptor for IgE initiates signal transduction in mast cells.Proximity relationships between the type I receptor for Fc epsilon (Fc epsilon RI) and the mast cell function-associated antigen (MAFA) studied by donor photobleaching fluorescence resonance energy transfer microscopy.Characterization of Fc gamma receptors on rat mucosal mast cells using a mutant Fc epsilon RI-deficient rat basophilic leukemia line.86Rb+ ion fluxes in resting and immunologically stimulated mucosal mast cells.
P50
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P50
description
(1937–) biológus, biokémikus
@hu
researcher ORCID ID = 0000-0002-1883-9547
@en
wetenschapper
@nl
name
Israel Pecht
@ast
Israel Pecht
@en
Israel Pecht
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Israel Pecht
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Israel Pecht
@hu
Israel Pecht
@nl
Israel Pecht
@sl
Israel Pecht
@sq
type
label
Israel Pecht
@ast
Israel Pecht
@en
Israel Pecht
@es
Israel Pecht
@ga
Israel Pecht
@hu
Israel Pecht
@nl
Israel Pecht
@sl
Israel Pecht
@sq
prefLabel
Israel Pecht
@ast
Israel Pecht
@en
Israel Pecht
@es
Israel Pecht
@ga
Israel Pecht
@hu
Israel Pecht
@nl
Israel Pecht
@sl
Israel Pecht
@sq
P1006
P214
P1006
P19
P21
P213
0000 0001 1783 6881
P214
P31
P496
0000-0002-1883-9547
P5463
Pecht_Israel
P569
1937-06-28T00:00:00Z
P7859
viaf-162300431