A serratial protease causes vascular permeability reaction by activation of the Hageman factor-dependent pathway in guinea pigs
about
Coral pathogens identified for White Syndrome (WS) epizootics in the Indo-PacificNanomedicine for drug targeting: strategies beyond the enhanced permeability and retention effect.Activation of matrix-metalloproteinase-2 and membrane-type-1-matrix-metalloproteinase in endothelial cells and induction of vascular permeability in vivo by human immunodeficiency virus-1 Tat protein and basic fibroblast growth factorBacterial extracellular zinc-containing metalloproteasesMolecular characterization of protease activity in Serratia sp. strain SCBI and its importance in cytotoxicity and virulenceVascular permeability in cancer and infection as related to macromolecular drug delivery, with emphasis on the EPR effect for tumor-selective drug targeting.Activation of the plasma kallikrein-kinin system by Candida albicans proteinase.Pseudomonas elastase acts as a virulence factor in burned hosts by Hageman factor-dependent activation of the host kinin cascade.Pathogenic capacity of proteases from Serratia marcescens and Pseudomonas aeruginosa and their suppression by chicken egg white ovomacroglobulin.Proteomics in the Study of Bacterial Keratitis.Involvement of bradykinin generation in intravascular dissemination of Vibrio vulnificus and prevention of invasion by a bradykinin antagonist.Identification of the Serratia marcescens hemolysin determinant by cloning into Escherichia coli.Molecular mechanism of complex infection by bacteria and virus analyzed by a model using serratial protease and influenza virus in mice.Inactivation of chemotactic activity of C5a by the serratial 56-kilodalton protease.Cleavage of immunoglobulin G (IgG) and IgA around the hinge region by proteases from Serratia marcescens.Role of cell-bound hemolysin as a pathogenicity factor for Serratia infections.Activation of the plasma kallikrein-kinin system by Vibrio vulnificus protease.Degradation of protease inhibitors, immunoglobulins, and other serum proteins by Serratia protease and its toxicity to fibroblast in culture.Comparison of four hemolysin-producing organisms (Escherichia coli, Serratia marcescens, Aeromonas hydrophila, and Listeria monocytogenes) for release of inflammatory mediators from various cells.Inactivation of various proteinase inhibitors and the complement system in human plasma by the 56-kilodalton proteinase from Serratia marcescens.Enhanced vascular permeability in solid tumor involving peroxynitrite and matrix metalloproteinases.CpxR-dependent thermoregulation of Serratia marcescens PrtA metalloprotease expression and its contribution to bacterial biofilm formation.Involvement of the kinin-generating cascade in enhanced vascular permeability in tumor tissue.Pluronic-based nano-self-assemblies of bacitracin A with a new mechanism of action for an efficient in vivo therapeutic effect against bacterial peritonitis
P2860
Q27301085-96716B26-8E24-4121-AFC4-9F053A164813Q33689872-870407F2-BF46-4067-ADA3-B92D4B4562D3Q33948194-48AEDD2B-CF34-41C2-B863-BA42E40A02D9Q34061222-A0985756-914F-4B4D-8B84-6F816F64E1A4Q34593296-A52AFE90-FCBE-4DF2-A2EC-00A99B17840AQ36001530-09F63AE7-924B-41BB-8F1F-1721A0E2B992Q36985539-53AA441D-864A-4E34-88C5-3A8DD1A155FDQ37005058-570B5B6C-FF56-4CCF-A419-ACE9C6696928Q37024274-525B973F-C3AA-48BC-A906-01537F149332Q39156160-41F705CC-9C7B-448D-85B4-DE8D96A8C034Q39570174-B16BD458-AB8A-4AD3-A96F-E8281A58B669Q39956814-41D4ABC4-F575-4F0F-AFB8-3BD8C8610A9DQ40115113-45CCC057-C822-43E8-9375-B4D5307818E6Q40154067-9CA480CA-09AC-4484-A512-4572A048BEDAQ40157897-50922334-C8CF-47FA-9662-EA595C352FDEQ40160488-624A1C63-A80E-4D32-B12F-F1EAC08F82D0Q40163878-9B8B83F4-1ECC-48F3-BA2D-DD7FE9263E3EQ40164777-C8A0D66E-5F67-4432-A613-8A2878E6940FQ40191764-33E0A45E-A097-41FE-97F9-633E19B18E62Q40427326-1DCF5CA5-AE40-4480-9D3D-33BA33445FEEQ43603046-BB2F9077-42CA-4667-BD13-78D768355758Q49597184-26AEE8EC-40C7-4880-8F69-76D6AFD61122Q55002348-684E171F-1ADD-4441-B6AC-314CE706DFFFQ58752596-74CD1B14-5AAA-4EFA-B7B1-60B47ED8B455
P2860
A serratial protease causes vascular permeability reaction by activation of the Hageman factor-dependent pathway in guinea pigs
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on June 1985
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
A serratial protease causes va ...... pendent pathway in guinea pigs
@en
A serratial protease causes va ...... endent pathway in guinea pigs.
@nl
type
label
A serratial protease causes va ...... pendent pathway in guinea pigs
@en
A serratial protease causes va ...... endent pathway in guinea pigs.
@nl
prefLabel
A serratial protease causes va ...... pendent pathway in guinea pigs
@en
A serratial protease causes va ...... endent pathway in guinea pigs.
@nl
P2093
P2860
P1476
A serratial protease causes va ...... pendent pathway in guinea pigs
@en
P2093
P2860
P304
P407
P577
1985-06-01T00:00:00Z