about
A Neisseria meningitidis fbpABC mutant is incapable of using nonheme iron for growthStrategies of Vibrio parahaemolyticus to acquire nutritional iron during host colonizationHigh resolution structure of an alternate form of the ferric ion binding protein from Haemophilus influenzaeCrystal structure of Pasteurella haemolytica ferric ion-binding protein A reveals a novel class of bacterial iron-binding proteinsThe role of the synergistic phosphate anion in iron transport by the periplasmic iron-binding protein from Haemophilus influenzaeCrystal structure of the Tp34 (TP0971) lipoprotein of treponema pallidum: implications of its metal-bound state and affinity for human lactoferrinHigh-affinity binding by the periplasmic iron-binding protein from Haemophilus influenzae is required for acquiring iron from transferrinThe role of vicinal tyrosine residues in the function of Haemophilus influenzae ferric-binding protein AStructural Variations within the Transferrin Binding Site on Transferrin-binding Protein B, TbpBCrystal structure of the N-lobe of lactoferrin binding protein B from Moraxella bovisThe structural basis of transferrin sequestration by transferrin-binding protein BProtein moonlighting in iron metabolism: glyceraldehyde-3-phosphate dehydrogenase (GAPDH)Current progress with Moraxella catarrhalis antigens as vaccine candidatesSolution structure of the immunodominant domain of protective antigen GNA1870 of Neisseria meningitidis.The plug domain of a neisserial TonB-dependent transporter retains structural integrity in the absence of its transmembrane beta-barrel.Mutational analysis of the TonB1 energy coupler of Pseudomonas aeruginosa.Identification of sequences in human transferrin that bind to the bacterial receptor protein, transferrin-binding protein B.Purification and characterization of the Pasteurella haemolytica 35 kilodalton periplasmic iron-regulated protein.Peptide-peptide interactions between human transferrin and transferrin-binding protein B from Moraxella catarrhalisAn ABC transporter system of Yersinia pestis allows utilization of chelated iron by Escherichia coli SAB11.The etiology of periodontal disease revisited by population genetic analysis.The iron/heme regulated genes of Haemophilus influenzae: comparative transcriptional profiling as a tool to define the species core modulon.Iron acquisition systems in the pathogenic Neisseria.Regulatory role of the MisR/S two-component system in hemoglobin utilization in Neisseria meningitidisPreparation and characterization of Neisseria meningitidis mutants deficient in production of the human lactoferrin-binding proteins LbpA and LbpB.The transferrin binding protein B of Moraxella catarrhalis elicits bactericidal antibodies and is a potential vaccine antigen.Mycobacterium tuberculosis Glyceraldehyde-3-Phosphate Dehydrogenase (GAPDH) Functions as a Receptor for Human Lactoferrin.Pathogenic neisseriae can use hemoglobin, transferrin, and lactoferrin independently of the tonB locus.Transition metals at the host-pathogen interface: how Neisseria exploit human metalloproteins for acquiring iron and zinc.Conservation of expression and N-terminal sequences of the Pasteurella haemolytica 31-kilodalton and Pasteurella trehalosi 29-kilodalton periplasmic iron-regulated proteins.Identification and functional characterization of the Neisseria gonorrhoeae lbpB gene product.A 55-kilodalton immunodominant antigen of Porphyromonas gingivalis W50 has arisen via horizontal gene transfer.Identification of pneumococcal surface protein A as a lactoferrin-binding protein of Streptococcus pneumoniaeHuman opsonins induced during meningococcal disease recognize transferrin binding protein complexes.Recombinant Neisseria meningitidis transferrin binding protein A protects against experimental meningococcal infectionCharacterization of binding of human lactoferrin to pneumococcal surface protein AAntigenic and sequence diversity in gonococcal transferrin-binding protein A.Ferric dicitrate transport system (Fec) of Shigella flexneri 2a YSH6000 is encoded on a novel pathogenicity island carrying multiple antibiotic resistance genes.Replication of Neisseria meningitidis within epithelial cells requires TonB-dependent acquisition of host cell iron.Structural basis for iron binding and release by a novel class of periplasmic iron-binding proteins found in gram-negative pathogens.
P2860
Q24522378-AA24E295-6B13-4916-8401-42A6FA4D8014Q26798537-2DF89668-989C-42D3-A4C0-F927D776A661Q27640323-ED0D2160-3B42-40B1-AB06-F161DD248851Q27641739-E7D7A221-BA27-4B01-8B63-2E5735F040A2Q27643213-4719641B-7B07-4603-8EAB-3F3587410CAAQ27643436-07948264-DF34-44B0-9232-E3CBD43AC477Q27643871-490A68D4-3906-48AE-8642-FD76439646A8Q27664200-68BD2EE6-C42F-4CE0-98EF-601344827BF3Q27666858-BFCF7736-6E6E-4F9E-AEC1-80269B04954AQ27677261-16E6254B-96CE-429B-A1E3-BFB934C20E17Q27677337-942412A8-CDD2-45D0-9AEF-0ACB2A3E5E7AQ28251639-37D1578B-AEA7-4F76-9C7B-3A976A8E687BQ28304447-D39409EA-0D04-4EFE-92EF-8ACC7B6BFED3Q30159962-90CDA277-D863-4B12-8481-01300ECC8F10Q30164110-71B99235-AD70-4A18-B6CE-A5F84A171110Q30453261-562836D9-0C48-4E41-840C-8A8086EE4D2DQ30674770-4513C7FC-D4F6-4DC0-90E2-B819021D31A7Q30956358-ED4B2954-C7AE-4878-8AD7-8B49B691091EQ31137188-4D724C15-1E19-438D-9E0F-FA11F0BF2030Q32100563-35B5A95A-38FE-48A1-B858-1361AB570C20Q33255114-CBE73E83-5A1D-406A-BB39-FF2E2B357B69Q33398155-4B051C27-1F91-4F5B-B919-C8F1A7EF702BQ33670869-56591A6D-AF0D-43CB-95FF-076CAFB57542Q33675878-FA088857-4D10-473A-B57D-D13FC2B397FFQ33745291-F02C3524-5A0A-4652-ADCA-B1F67B7DDF5EQ33761483-EA807BEB-6178-4B1A-8A33-C8A7630353E5Q33774924-895672FF-04B1-49C6-9B73-5F15370502DFQ33787521-153CD1F9-6A0B-4139-8E0E-FFDF80664613Q33914938-4402E670-CEB8-4219-A053-BFFD649D8AC6Q33997804-3EB6C8D1-7F79-4118-AFA1-157CB1F0116BQ34000118-10CAB5B3-4A71-4C30-922A-8E27C5E31ABEQ34000564-693FA690-B2D0-4ED5-A91A-2563EE149D9CQ34000817-E64661F2-4D75-48E3-84DD-2EEEA628531BQ34002783-8E9F422E-DCE1-49C1-B5DF-5CEB65D9EB0EQ34006346-063FC338-6DB6-4D0E-A86A-516CAF709AAEQ34007403-9F88972D-41A6-42C1-A5CF-1841055730B1Q34007901-2BF64D4E-9A62-4C45-AC4D-F2BFFA0CADE1Q34009180-A170E5E0-2A24-4D19-98FE-D54EFCCF0F40Q34120589-C792413B-BF1E-4086-9597-2CDBC7A87591Q34349646-FA16FF28-47FC-4F7F-91A8-4597898B364E
P2860
description
1996 nî lūn-bûn
@nan
1996年の論文
@ja
1996年学术文章
@wuu
1996年学术文章
@zh-cn
1996年学术文章
@zh-hans
1996年学术文章
@zh-my
1996年学术文章
@zh-sg
1996年學術文章
@yue
1996年學術文章
@zh
1996年學術文章
@zh-hant
name
Bacterial transferrin and lactoferrin receptors.
@en
type
label
Bacterial transferrin and lactoferrin receptors.
@en
prefLabel
Bacterial transferrin and lactoferrin receptors.
@en
P1476
Bacterial transferrin and lactoferrin receptors.
@en
P2093
Schryvers AB
P304
P356
10.1016/0966-842X(96)10025-1
P577
1996-05-01T00:00:00Z