Structure of the streptococcal endopeptidase IdeS, a cysteine proteinase with strict specificity for IgG. - Wikidata - awgldk - TriplyDB

Structure of the streptococcal endopeptidase IdeS, a cysteine proteinase with strict specificity for IgG.

Structure of the streptococcal endopeptidase IdeS, a cysteine proteinase with strict specificity for IgG.

http://www.wikidata.org/entity/Q37714099

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A New Autocatalytic Activation Mechanism for Cysteine Proteases Revealed by Prevotella intermedia Interpain A B. subtilis ykuD protein at 2.0 A resolution: insights into the structure and function of a novel, ubiquitous family of bacterial enzymes IdeS: a bacterial proteolytic enzyme with therapeutic potential The solution structure of the Josephin domain of ataxin-3: structural determinants for molecular recognition.Novel Sample Preparation for Mass Spectral Analysis of Complex Biological Samples.A papain-like enzyme at work: native and acyl-enzyme intermediate structures in phytochelatin synthesis.A new tool for monoclonal antibody analysis: application of IdeS proteolysis in IgG domain-specific characterization.The Streptococcus pneumoniae capsule inhibits complement activity and neutrophil phagocytosis by multiple mechanisms Complete Removal of Extracellular IgG Antibodies in a Randomized Dose-Escalation Phase I Study with the Bacterial Enzyme IdeS--A Novel Therapeutic Opportunity Immunoglobulin cleavage by the streptococcal cysteine protease IdeS can be detected using protein G capture and mass spectrometry.Generation and Characterization of an IgG4 Monomeric Fc Platform.Time-Dependent Structural Alteration of Rituximab Analyzed by LC/TOF-MS after a Systemic Administration to Rats.Identification and Characterization of IgdE, a Novel IgG-degrading Protease of Streptococcus suis with Unique Specificity for Porcine IgG.The origin and functional transition of P34 Tumor-associated and microbial proteases compromise host IgG effector functions by a single cleavage proximal to the hinge.Streptococcal IdeS and its impact on immune response and inflammation.Bioanalytical approaches for characterizing catabolism of antibody-drug conjugates.The Bacterial Enzyme IdeS Cleaves the IgG-Type of B Cell Receptor (BCR), Abolishes BCR-Mediated Cell Signaling, and Inhibits Memory B Cell Activation.Rapid and improved characterization of therapeutic antibodies and antibody related products using IdeS digestion and subunit analysis.Characterization of alanine to valine sequence variants in the Fc region of nivolumab biosimilar produced in Chinese hamster ovary cells.Antibody-drug conjugate model fast characterization by LC-MS following IdeS proteolytic digestion.Streptococcus pneumoniae resistance to complement-mediated immunity is dependent on the capsular serotype A hingeless Fc fusion system for site-specific cleavage by IdeS 3-aminopiperidine-based peptide analogues as the first selective noncovalent inhibitors of the bacterial cysteine protease IdeS.The intrinsic immunoglobulin g endopeptidase activity of streptococcal Mac-2 proteins implies a unique role for the enzymatically impaired Mac-2 protein of M28 serotype strains.IdeS, a highly specific immunoglobulin G (IgG)-cleaving enzyme from Streptococcus pyogenes, is inhibited by specific IgG antibodies generated during infection.Structural comparison of two anti-CD20 monoclonal antibody drug products using middle-down mass spectrometry.Rapid IgG heavy chain cleavage by the streptococcal IgG endopeptidase IdeS is mediated by IdeS monomers and is not due to enzyme dimerization.Implementation of Glycan Remodeling to Plant-Made Therapeutic Antibodies.Streptococcus pyogenes Infection and the Human Proteome with a Special Focus on the Immunoglobulin G-cleaving Enzyme IdeS.Opposing roles of B lymphocyte subsets in atherosclerosis.Antibody-mediated rejection: New approaches in prevention and management.Proteolytic single hinge cleavage of pertuzumab impairs its Fc effector function and antitumor activity in vitro and in vivo.

P2860

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P2860

Structure of the streptococcal endopeptidase IdeS, a cysteine proteinase with strict specificity for IgG.

http://www.wikidata.org/entity/Q37714099

description

article científic

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article scientifique

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articolo scientifico

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artigo científico

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bilimsel makale

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scientific article published on December 2004

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vedecký článok

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vetenskaplig artikel

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videnskabelig artikel

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vědecký článek

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name

Structure of the streptococcal ...... th strict specificity for IgG.

@en

Structure of the streptococcal ...... th strict specificity for IgG.

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type

label

Structure of the streptococcal ...... th strict specificity for IgG.

@en

Structure of the streptococcal ...... th strict specificity for IgG.

@nl

prefLabel

Structure of the streptococcal ...... th strict specificity for IgG.

@en

Structure of the streptococcal ...... th strict specificity for IgG.

@nl

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Proceedings of the National Academy of Sciences of the United States of America

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Structure of the streptococcal ...... th strict specificity for IgG.

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P2093

Katja Wenig

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Lars Björck

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Lorenz Chatwell

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Peter Sondermann

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Robert Huber

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Ulrich von Pawel-Rammingen

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P2860

L-trans-Epoxysuccinyl-leucylamido(4-guanidino)butane (E-64) and its analogues as inhibitors of cysteine proteinases including cathepsins B, H and L

Improved methods for building protein models in electron density maps and the location of errors in these models

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PROCHECK: a program to check the stereochemical quality of protein structures

MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

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Crystal structure of the zymogen form of the group A Streptococcus virulence factor SpeB: An integrin-binding cysteine protease

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P304

17371-17376

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10.1073/PNAS.0407965101

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2004-12-01T00:00:00Z

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8154119

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15574492

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536041

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