Nucleotide sequencing of the Proteus mirabilis calcium-independent hemolysin genes (hpmA and hpmB) reveals sequence similarity with the Serratia marcescens hemolysin genes (shlA and shlB).
about
Complete genomic sequence of Pasteurella multocida, Pm70Proteus mirabilis and Urinary Tract Infections.Structural and Functional Studies of Truncated Hemolysin A from Proteus mirabilisSequential unfolding of the hemolysin two-partner secretion domain from Proteus mirabilis.Type V Secretion: the Autotransporter and Two-Partner Secretion PathwaysCharacterization of a novel two-partner secretion system in Escherichia coli O157:H7.Complicated catheter-associated urinary tract infections due to Escherichia coli and Proteus mirabilisA genomic sample sequence of the entomopathogenic bacterium Photorhabdus luminescens W14: potential implications for virulence.Type V protein secretion pathway: the autotransporter storyShared amino acid sequences between major histocompatibility complex class II glycoproteins, type XI collagen and Proteus mirabilis in rheumatoid arthritis.Origin of a chloroplast protein importer.Two-Partner Secretion: Combining Efficiency and Simplicity in the Secretion of Large Proteins for Bacteria-Host and Bacteria-Bacteria InteractionsHaemophilus ducreyi secretes a filamentous hemagglutinin-like protein.Target cell range of Haemophilus ducreyi hemolysin and its involvement in invasion of human epithelial cellsMapping of binding domains of nontypeable Haemophilus influenzae HMW1 and HMW2 adhesins.Identification of a locus involved in systemic dissemination of Yersinia enterocolitica.The ability of Proteus mirabilis to sense surfaces and regulate virulence gene expression involves FliL, a flagellar basal body protein.The PhlA hemolysin from the entomopathogenic bacterium Photorhabdus luminescens belongs to the two-partner secretion family of hemolysins.Genes encoding high-molecular-weight adhesion proteins of nontypeable Haemophilus influenzae are part of gene clustersDraft Genome Sequence of Chelonobacter oris Strain 1662T, Associated with Respiratory Disease in Hermann's Tortoises.Transcriptome of Proteus mirabilis in the murine urinary tract: virulence and nitrogen assimilation gene expression.Characterization of the hemolytic activity of Haemophilus ducreyiConstruction of a flagellum-negative mutant of Proteus mirabilis: effect on internalization by human renal epithelial cells and virulence in a mouse model of ascending urinary tract infection.Lack of functional complementation between Bordetella pertussis filamentous hemagglutinin and Proteus mirabilis HpmA hemolysin secretion machineriesIdentification of a novel two-partner secretion locus in Moraxella catarrhalis.Proteus mirabilis MR/P fimbriae: molecular cloning, expression, and nucleotide sequence of the major fimbrial subunit gene.Potential virulence factors of Proteus bacilli.The HpmA hemolysin is more common than HlyA among Proteus isolates.Cytotoxic activity of the Proteus hemolysin HpmA.Pore-forming bacterial protein hemolysins (cytolysins).Host-pathogen interactions in urinary tract infection.Pseudomonas aeruginosa ExlA and Serratia marcescens ShlA trigger cadherin cleavage by promoting calcium influx and ADAM10 activation.An Edwardsiella tarda strain containing a mutation in a gene with homology to shlB and hpmB is defective for entry into epithelial cells in culture.A gene cluster involved in the utilization of both free heme and heme:hemopexin by Haemophilus influenzae type b.Distinct roles of the N-terminal and C-terminal precursor domains in the biogenesis of the Bordetella pertussis filamentous hemagglutinin.Cloning, expression, and DNA sequence analysis of genes encoding nontypeable Haemophilus influenzae high-molecular-weight surface-exposed proteins related to filamentous hemagglutinin of Bordetella pertussis.Isolation and molecular characterization of spontaneously occurring cytolysin-negative mutants of Actinobacillus pleuropneumoniae serotype 7.Cloning, partial sequence, expression, and antigenic analysis of the filamentous hemagglutinin gene of Bordetella pertussis.Activation of Serratia marcescens hemolysin through a conformational change.Secretion of the Haemophilus influenzae HMW1 and HMW2 adhesins involves a periplasmic intermediate and requires the HMWB and HMWC proteins.
P2860
Q22066329-B1CE7D39-707F-4C8C-8AF7-858207450EA8Q26779002-0680E278-73F8-4F6A-9192-3E905B82DDDAQ27655729-912D662D-4C57-481D-9467-3107DF81BC30Q30152834-4AE882B9-96D7-4A14-824F-81075B8B1469Q30156047-4D07B69A-0441-46B5-9DA3-FBA45B78CF04Q30158040-DA649402-8C8C-4C18-852E-C4E4B880BC3BQ30491878-2CD67207-263E-46B0-B0D0-C77750F75B6CQ31796749-E52ED094-DB88-45ED-8DB3-1BF64F855067Q33559645-44E609C0-E2D3-4D34-92D8-4C6846BB738FQ33567127-478D79F5-D1E9-4C56-B16D-2012135E6B41Q33617073-A7D4EFF5-5B0D-4CA4-A2D8-B47F616CEDB9Q33650510-6F24DA08-975C-4EF5-ADFA-001A48A8BD9CQ33741949-3ED14381-9FE6-4A39-95B7-D04811DD75B2Q34001309-B9795364-3E00-4A72-AF57-46470891677AQ34005619-D6977EA2-72DE-42FD-A894-BB98596E7962Q34009322-9C414F39-D8DE-46D2-ACA0-B597DCFF92A7Q34077175-8162D082-B719-4FCE-AF40-21C95EF5B88CQ34315257-373D1E34-F2D3-47B7-89CD-85DCC8D17DE5Q34533382-66FF8F00-65DF-4696-9773-46273BFCC284Q34737404-1917D089-2285-42F4-B3E7-BCE3EFBC7CD6Q35328925-A0C66921-DDDC-47F4-8707-6A07C920A703Q35450289-3DC3CD57-A9FE-4E6B-86B5-8BB343491AC9Q35532558-C621E00E-7E30-44F4-81DF-02ADDB1C1FBBQ35619410-D7094017-65F1-4A5F-A464-60B26B017161Q35913464-5440B335-5253-47D0-98B3-960326135765Q35966385-2419A709-6DE7-4753-A953-80526275BE8AQ36574211-FC5E5A1B-4017-4871-A064-91A5184EF042Q36984180-BCAB7F5C-FE12-461E-B98E-757CDAD14B38Q36984238-ACA96534-D556-4360-823D-3D732EC78FF6Q37420799-98AFBB1C-3C92-4913-9035-65EACEBA11D3Q37774543-D9155844-48CC-480B-BDF0-441CAE605194Q38612544-D83E0C3E-F1B0-40E4-BFC2-72DF3AFEDCE3Q39831028-7EADEB83-6908-4B90-A418-5AE6E29EE3EDQ39836689-83C25245-D856-4A65-8F8E-E822CAB9D0C3Q39840301-3DC1F462-0EA6-47D9-BD36-3B626633AAD7Q40146118-58699693-8276-4ED0-90A0-A06142650882Q40155952-78DD32D8-DAED-4684-9483-3ED569A4E587Q40428351-5E052761-5D91-42D4-9ACF-926B5FDFD076Q40582671-DA22B4D4-641D-4881-AA5D-1A0FD054DB32Q41061782-97631C1B-40E8-4229-B461-75BC6DAE602C
P2860
Nucleotide sequencing of the Proteus mirabilis calcium-independent hemolysin genes (hpmA and hpmB) reveals sequence similarity with the Serratia marcescens hemolysin genes (shlA and shlB).
description
1990 nî lūn-bûn
@nan
1990年の論文
@ja
1990年論文
@yue
1990年論文
@zh-hant
1990年論文
@zh-hk
1990年論文
@zh-mo
1990年論文
@zh-tw
1990年论文
@wuu
1990年论文
@zh
1990年论文
@zh-cn
name
Nucleotide sequencing of the P ...... molysin genes (shlA and shlB).
@en
Nucleotide sequencing of the Proteus mirabilis calcium-independent hemolysin genes
@nl
type
label
Nucleotide sequencing of the P ...... molysin genes (shlA and shlB).
@en
Nucleotide sequencing of the Proteus mirabilis calcium-independent hemolysin genes
@nl
prefLabel
Nucleotide sequencing of the P ...... molysin genes (shlA and shlB).
@en
Nucleotide sequencing of the Proteus mirabilis calcium-independent hemolysin genes
@nl
P2860
P1476
Nucleotide sequencing of the P ...... molysin genes (shlA and shlB).
@en
P2093
P2860
P304
P356
10.1128/JB.172.3.1206-1216.1990
P577
1990-03-01T00:00:00Z