Activation of adenylate cyclase by heat-labile Escherichia coli enterotoxin. Evidence for ADP-ribosyltransferase activity similar to that of choleragen
about
Bacterial toxins: cellular mechanisms of actionCoordinated assembly of multisubunit proteins: oligomerization of bacterial enterotoxins in vivo and in vitro.Membrane receptors for bacterial toxins.Reversibility of arginine-specific mono(ADP-ribosyl)ation: identification in erythrocytes of an ADP-ribose-L-arginine cleavage enzyme.Conformation of protein secreted across bacterial outer membranes: a study of enterotoxin translocation from Vibrio cholerae.Role of trypsin-like cleavage at arginine 192 in the enzymatic and cytotonic activities of Escherichia coli heat-labile enterotoxinAlkaline pH Is a signal for optimal production and secretion of the heat labile toxin, LT in enterotoxigenic Escherichia coli (ETEC).Production by Clostridium spiroforme of an iotalike toxin that possesses mono(ADP-ribosyl)transferase activity: identification of a novel class of ADP-ribosyltransferases.Heat-labile enterotoxin: beyond G(m1) bindingEvaluation of the LTK63 adjuvant effect on cellular immune responses to measles virus nucleoprotein.Structure and function of cholera toxin and the related Escherichia coli heat-labile enterotoxinCloning, nucleotide sequence, and hybridization studies of the type IIb heat-labile enterotoxin gene of Escherichia coliYghG (GspSβ) is a novel pilot protein required for localization of the GspSβ type II secretion system secretin of enterotoxigenic Escherichia coliEscherichia coli in postweaning diarrhea in pigs: an update on bacterial types, pathogenesis, and prevention strategies.Alterations at the carboxyl terminus change assembly and secretion properties of the B subunit of Escherichia coli heat-labile enterotoxin.Genetics of type IIa heat-labile enterotoxin of Escherichia coli: operon fusions, nucleotide sequence, and hybridization studies.Purification and some properties of a non-o1 Vibrio cholerae enterotoxin that is identical to cholera enterotoxin.Vascular permeability activity in Escherichia coli heat-stable enterotoxin.Subunit number and arrangement in Escherichia coli heat-labile enterotoxin.Isolation and characterization of hypertoxinogenic (htx) mutants of Escherichia coli KL320(pCG86).Effect of site-directed mutagenic alterations on ADP-ribosyltransferase activity of the A subunit of Escherichia coli heat-labile enterotoxin.Partial characterization of the enzymatic activity associated with the binary toxin (type C2) produced by Clostridium botulinum.Molecular basis for the pathological actions of Clostridium perfringens iota toxinGangliosides sensitize unresponsive fibroblasts to Escherichia coli heat-labile enterotoxin.Evidence that a non-O1 Vibrio cholerae produces enterotoxin that is similar but not identical to cholera enterotoxinAssay of heat-labile enterotoxins by their ADP-ribosyltransferase activitiesEvaluation of the adjuvant effect of Escherichia coli heat-labile enterotoxin mutant (LTK63) on the systemic immune responses to intranasally co-administered measles virus nucleoprotein. Part I: antibody responses.Intermolecular interactions between the A and B subunits of heat-labile enterotoxin from Escherichia coli promote holotoxin assembly and stability in vivo.The Virulence Regulator Rns Activates the Expression of CS14 Pili.Mechanism of toxin secretion by Vibrio cholerae investigated in strains harboring plasmids that encode heat-labile enterotoxins of Escherichia coli.Post-translational modifications in host cells during bacterial infection.Novel bacterial ADP-ribosylating toxins: structure and function.Recent advances in nontoxic Escherichia coli heat-labile toxin and its derivative adjuvants.Environmental contaminants and intestinal functionTransient entry of enterotoxin subunits into the periplasm occurs during their secretion from Vibrio cholerae.Cellular location of heat-labile enterotoxin in Escherichia coli.NAD metabolism in Vibrio cholerae.Nucleotide sequence comparison between heat-labile toxin B-subunit cistrons from Escherichia coli of human and porcine origin.Mapping of a gene in Vibrio cholerae that determines the antigenic structure of cholera toxin.Residues of heat-labile enterotoxin involved in bacterial cell surface binding.
P2860
Q24634587-D518D470-5BCA-415F-9CCE-9C75DCE2CA96Q33650535-304DD905-90D1-498E-95AB-AB6F7E39028AQ33721760-4121AAD7-1138-4403-8738-7B9A2C062DC5Q34048571-648AB479-6837-470C-97A9-2E67CDAF109CQ34357011-B5B5432B-8F58-4C82-9A7E-1F817C705E85Q34540148-0C3CCEED-2810-43B3-B0F8-C320929B9F9AQ34994510-D5CDE0F8-F5A1-40A3-99B1-8B976DB090ADQ35089585-03E4C1B1-6848-4334-98A8-F1FE644B1F5CQ35155851-7367D930-0CD2-47D4-9504-70A18C23B192Q35171910-1A883E76-4CED-429C-85BC-8397871BBAEAQ35655408-36294741-8F5A-447A-A442-7371EE50E652Q36181697-C55BF8A3-DAD1-43EB-B2E2-94E8D06224C0Q36211182-CDE371FC-410B-4F34-AA47-D6017C603B83Q36257824-DD9A8AD5-478E-4A28-9E94-FFAB88F1CE5DQ36268265-4456E876-9078-432A-BD07-A96EA58FE4AEQ36271843-7CC21F23-94D5-4E80-845D-DB190DF627C6Q36345937-B518984B-AF83-4A6A-960D-873331BC216AQ36425621-7ACE466B-1ACA-450C-9D54-6AF38A590438Q36426894-EE2B7183-7157-43A6-85CA-CBE75517CA73Q36448597-91F4DFA0-DC87-4C38-A4DE-30092A22F989Q36967442-4021E7E3-11B2-4E15-AC9B-9A7A587C578EQ36992224-5BC50E4A-9F50-4422-8F15-C1BDFCC4866DQ37014992-7FEE9E2E-F010-4919-8B94-2ADAC2872716Q37040283-C0127B18-7ED2-46AF-A983-851E7930C624Q37104750-D14EA946-6759-4C0C-A84A-6571FF88ED66Q37161808-B524360C-9FC6-4004-AED3-A72EC431DB2FQ37247061-E999418B-883A-4165-A51B-5292C10EF4E3Q37352032-5D5938A1-AA8F-4161-AA08-8F035AD8BFBCQ37539498-CD5DFCCA-1D86-4F3E-9F1E-C60C0C343A75Q37580110-80734F84-1CFC-4931-8CF4-C85DC075A93CQ37759341-E3BFC1C7-5479-412C-87DC-C95C645670F1Q38229329-9808E7DB-A3AC-4771-A0C0-437A8192140BQ38818721-CF0B4CF1-E007-4C4D-8220-81BD2729A483Q39162273-CA6BF111-9B83-49A8-898E-3E3A9774A84EQ39956011-4F213B51-EB1E-4B73-B490-75E719C24A5EQ39967815-1D5A5710-89C0-43DA-A5C2-D23458C0B3D3Q39972617-1A29C56D-9850-4200-89EF-B9AA8B2E804FQ40170132-6566FAF6-A5FF-4EEF-A023-3E9DE791EFF2Q40599429-FE525FC9-AE22-4657-A361-9E3A53CF947EQ43127882-C86B9708-6821-433F-BA33-608B9EC7A7AD
P2860
Activation of adenylate cyclase by heat-labile Escherichia coli enterotoxin. Evidence for ADP-ribosyltransferase activity similar to that of choleragen
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on August 1978
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Activation of adenylate cyclas ...... similar to that of choleragen
@en
Activation of adenylate cyclas ...... similar to that of choleragen.
@nl
type
label
Activation of adenylate cyclas ...... similar to that of choleragen
@en
Activation of adenylate cyclas ...... similar to that of choleragen.
@nl
prefLabel
Activation of adenylate cyclas ...... similar to that of choleragen
@en
Activation of adenylate cyclas ...... similar to that of choleragen.
@nl
P2860
P356
P1476
Activation of adenylate cyclas ...... similar to that of choleragen
@en
P2093
P2860
P304
P356
10.1172/JCI109127
P407
P577
1978-08-01T00:00:00Z