About: The Pore-forming Toxin Proaerolysin Is Activated by Furin

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scientific article published in Journal of Biological Chemistry

Attributes	Values
rdf:type	Item
description	artículu científicu (ast) wetenschappelijk artikel (nl) наукова стаття, опублікована в грудні 1998 (uk) article publié dans la revue scientifique Journal of Biological Chemistry (fr) im Dezember 1998 veröffentlichter wissenschaftlicher Artikel (de) scientific article published in Journal of Biological Chemistry (en)
publication date	wds:Q57268746-62D70E67-E92F-4640-A56F-D927BECF99D7
publication date	1998-12-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q57268746-0F2DC0F1-B493-4A46-8607-43AA25B59B51
language of work or name	English
cites work	wds:Q57268746-0138CEB0-AEFD-4C16-B64E-029DCA9B412B wds:Q57268746-0BDE014D-3FEC-410B-A321-418FB3CC846D wds:Q57268746-0BF78C1C-C6E3-479E-9DCA-35453BE5D8F7 wds:Q57268746-145BE700-AC00-45B2-A755-C8DF7CBD953F wds:Q57268746-14E92EC2-C863-470F-83EE-A7914C9BF69E wds:Q57268746-16573A0A-C0A2-41AA-A3EA-E9D61FFEF47A wds:Q57268746-1EB48AFC-46C0-42ED-A5E6-B8521670F874 wds:Q57268746-299E296A-2805-4F38-B041-30F7C978C217 wds:Q57268746-39765120-4402-4864-A630-B3DA2A913C59 wds:Q57268746-3C4C0718-92ED-4CA8-921A-402A3A6BA381 wds:Q57268746-432C29DA-F665-4667-8F83-CD5D18FD6B6E wds:Q57268746-44F05625-EE15-4F14-9B3A-2271DD49C8AE wds:Q57268746-45E63C9A-D45A-48DA-8582-C9238EBB0281 wds:Q57268746-4AD624A5-D28A-4534-B57D-6BB960E7132F wds:Q57268746-4B174364-5679-4127-835C-176F98E9B4B8 wds:Q57268746-4BB4B0F7-DF67-4B87-8672-F37BB3102FAB wds:Q57268746-4C6CF180-E8C8-47BE-9592-CC8D20AEDAC0 wds:Q57268746-4D01FB14-0F5D-474D-83D5-6CC97E759C01 wds:Q57268746-4D1AEAD0-E5D4-479E-8505-85750D7C7976 wds:Q57268746-505D597E-BFF1-4DE5-8870-553E26C923D4 wds:Q57268746-5BEF5D74-F725-4E7A-92BC-36FEC380EAE7 wds:Q57268746-5C3326F3-5C27-4578-883F-6DE00649E433 wds:Q57268746-6B54DF98-C4C5-4E87-8FD3-00F157648D63 wds:Q57268746-6FE708F0-F0AC-43AE-8A59-E9A77BEC5B9C wds:Q57268746-7DC985C0-6FE2-4777-A7D8-D8916EA1DE0A wds:Q57268746-89316851-6898-48A0-A7AE-2AD8C217DE3B wds:Q57268746-8CBAA890-236C-4248-B82C-5311B9E87EDF wds:Q57268746-952EF809-E198-42FA-89EC-0BCC8DEEBF4D wds:Q57268746-9831B605-620F-4B70-9280-BC29415E0292 wds:Q57268746-98A0E811-1DC3-4014-85B2-445BBBA8ADCA wds:Q57268746-9C190F92-CE5A-4BE7-9196-80A7AEFBAF18 wds:Q57268746-9C4DD3A1-FEB1-4ED7-ABAE-A8EBC9B1CD40 wds:Q57268746-A171FE1A-671B-405E-B2FF-8CC0F03186C9 wds:Q57268746-B0226EEB-EF4A-40E0-A2E7-8C4C816CC555 wds:Q57268746-B16F0926-41F3-4C4A-80E9-1A4A53AAFDF5 wds:Q57268746-B39AEBBC-93A0-4EC0-AA5C-FB5E4E22C217 wds:Q57268746-C956B7BA-9BAC-4B77-9C4D-4C96EA62673B wds:Q57268746-D611FAA0-B7F7-4A1A-8502-807F1DE857D0 wds:Q57268746-EC2614B0-50CF-4227-98B4-BB535B3080AA wds:Q57268746-F363A89A-5422-4924-AE84-560B5D6F2832 wds:Q57268746-FBD5A6EB-B404-4629-A498-547F9261C7EB
cites work	Transformation of rat cells by DNA of human adenovirus 5 Cytoskeletal protein ABP-280 directs the intracellular trafficking of furin and modulates proprotein processing in the endocytic pathway The isoforms of proprotein convertase PC5 are sorted to different subcellular compartments Disruptions in Golgi structure and membrane traffic in a conditional lethal mammalian cell mutant are corrected by epsilon-COP. Characterisation of the heptameric pore-forming complex of the Aeromonas toxin aerolysin using MALDI-TOF mass spectrometry Calnexin: a membrane-bound chaperone of the endoplasmic reticulum A single point mutation in epsilon-COP results in temperature-sensitive, lethal defects in membrane transport in a Chinese hamster ovary cell mutant Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4 Functional dissection of COP-I subunits in the biogenesis of multivesicular endosomes Eukaryotic protein processing: endoproteolysis of precursor proteins Comparative functional role of PC7 and furin in the processing of the HIV envelope glycoprotein gp160 A pore-forming toxin interacts with a GPI-anchored protein and causes vacuolation of the endoplasmic reticulum. Identification of the paired basic convertases implicated in HIV gp160 processing based on in vitro assays and expression in CD4(+) cell lines Endoprotease activities other than furin and PACE4 with a role in processing of HIV-I gp160 glycoproteins in CHO-K1 cells The family of subtilisin/kexin like pro-protein and pro-hormone convertases: divergent or shared functions Anthrax toxin protective antigen is activated by a cell surface protease with the sequence specificity and catalytic properties of furin Enzymic characterization of murine and human prohormone convertase-1 (mPC1 and hPC1) expressed in mammalian GH4C1 cells Inhibition of furin-mediated cleavage activation of HIV-1 glycoprotein gp160 Quality control in the secretory pathway ATP is required for receptor-mediated endocytosis in intact cells Membrane glycoprotein receptor and hole-forming properties of a cytolytic protein toxin The erythrocyte receptor for the channel-forming toxin aerolysin is a novel glycosylphosphatidylinositol-anchored protein alpha1-Antitrypsin Portland, a bioengineered serpin highly selective for furin: application as an antipathogenic agent Glycosylphosphatidylinositol anchors of membrane glycoproteins are binding determinants for the channel-forming toxin aerolysin. The glycosylphosphatidylinositol-anchored surface glycoprotein Thy-1 is a receptor for the channel-forming toxin aerolysin. Furin-induced cleavage and activation of Shiga toxin. Structure of the Aeromonas toxin proaerolysin in its water-soluble and membrane-channel states Membrane insertion: The strategies of toxins (review). Aeromonas as a human pathogen Aerolysin, a hemolysin fromAeromonas hydrophila, forms voltage-gated channels in planar lipid bilayers COPs regulating membrane traffic Conformational changes in aerolysin during the transition from the water-soluble protoxin to the membrane channel High efficiency gene transfer into mammalian cells by a double transfection protocol Oligomerization of the channel-forming toxin aerolysin precedes insertion into lipid bilayers. Spectroscopic study of the activation and oligomerization of the channel-forming toxin aerolysin: identification of the site of proteolytic activation. Vibrio spp. secrete proaerolysin as a folded dimer without the need for disulphide bond formation. Purification of cloned proaerolysin released by a low protease mutant of Aeromonas salmonicida Aerolysin--the ins and outs of a model channel-forming toxin. Cationic liposomes enhanced firefly bioluminescent assay of adenosine 5'-triphosphate disodium salt Partial purification of the rat erythrocyte receptor for the channel-forming toxin aerolysin and reconstitution into planar lipid bilayers Diarrhea associated with Aeromonas species in children in day care centers
author name string	wds:Q57268746-1F6F382F-8A8A-40D6-B88B-CB88D42A1168 wds:Q57268746-7824FB73-10E8-4769-BCF0-0986DDEE5A29 wds:Q57268746-EECEA1D2-1E63-4C0C-AE82-15543DB72B20
author name string	G Thomas F Jean J T Buckley
rdfs:label	The Pore-forming Toxin Proaerolysin Is Activated by Furin (en)

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