Acylation of the 47-kilodalton major membrane immunogen of Treponema pallidum determines its hydrophobicity.
about
Spirochaetal lipoproteins and pathogenesisThe leptospiral major outer membrane protein LipL32 is a lipoprotein expressed during mammalian infectionIdentification and mapping of an immunogenic region of Mycoplasma hyopneumoniae p65 surface lipoprotein expressed in Escherichia coli from a cloned genomic fragment.Molecular cloning and characterization of a 35.5-kilodalton lipoprotein of Treponema pallidumLipid modification of the 17-kilodalton membrane immunogen of Treponema pallidum determines macrophage activation as well as amphiphilicity.Purification of immature cores of mouse mammary tumor virus and immunolocalization of protein domains.Major integral membrane protein immunogens of Treponema pallidum are proteolipidsMolecular cloning and sequence analysis of the gene encoding LipL41, a surface-exposed lipoprotein of pathogenic Leptospira speciesIdentification and characterization of the Treponema pallidum tpn50 gene, an ompA homologSimilarity between the 38-kilodalton lipoprotein of Treponema pallidum and the glucose/galactose-binding (MglB) protein of Escherichia coli.Molecular cloning and characterization of the 15-kilodalton major immunogen of Treponema pallidumThe 47-kDa major lipoprotein immunogen of Treponema pallidum is a penicillin-binding protein with carboxypeptidase activityIsolation of the outer membranes from Treponema pallidum and Treponema vincentii.Fatty acids of Treponema pallidum and Borrelia burgdorferi lipoproteins.Chemical and biological activities of a 64-kilodalton outer sheath protein from Treponema denticola strains.Localization of outer surface proteins A and B in both the outer membrane and intracellular compartments of Borrelia burgdorferiExpression and purification of the mouse mammary tumor virus gag-pro transframe protein p30 and characterization of its dUTPase activity.Analysis of the N-terminal region of the 47-kilodalton integral membrane lipoprotein of Treponema pallidum.The outer membrane, not a coat of host proteins, limits antigenicity of virulent Treponema pallidum.The 34-kilodalton membrane immunogen of Treponema pallidum is a lipoprotein.Immunogenic integral membrane proteins of Borrelia burgdorferi are lipoproteins.Characterization of the 35-kilodalton Treponema pallidum subsp. pallidum recombinant lipoprotein TmpC and antibody response to lipidated and nonlipidated T. pallidum antigensTreponema phagedenis encodes and expresses homologs of the Treponema pallidum TmpA and TmpB proteins.Polypeptides of Treponema pallidum: progress toward understanding their structural, functional, and immunologic roles. Treponema Pallidum Polypeptide Research Group.The Treponema pallidum Outer Membrane.A 16-kilodalton lipoprotein of the outer membrane of Serpulina (Treponema) hyodysenteriae.Molecular cloning, expression, and DNA sequence analysis of the gene that encodes the 16-kilodalton outer membrane lipoprotein of Serpulina hyodysenteriae.
P2860
Q24648165-67D75B40-B8C2-4C6F-BC06-47D8A4655E39Q30847648-E1EC8F41-14E8-47E5-82E9-E34E8A031169Q33256301-7AED7554-F8CB-434D-AECB-8398470754A1Q33335415-C75AE2A7-DCE1-44C3-ACDD-326388CAD6A8Q33618991-B9395438-6ABA-41DC-B44B-206AE70A1523Q33937069-7FC0E00D-768B-4CD3-981D-93DE83E79669Q35102432-9FDA3E11-05DB-4EB2-B8A4-0C8C04899ABAQ35500578-A776C7BF-739F-4EBA-B363-1A0F8EF6DE1CQ35775291-A8774396-2EF5-42B0-B9FD-00152BBBE43AQ35776943-6A73F3A7-0614-4E96-9A6D-6A7B82DAE0E1Q35904261-22F7CE1C-8C84-465A-A6E6-29B89EBBE662Q35925741-22A4C14B-23B7-41C4-89B5-1E9C978EA17FQ35976173-4C0159A7-46B7-4F11-9264-ACDC76991D83Q36106623-38FD7929-D235-48A5-8421-C2070CD2D37BQ36164354-3470AB23-B4E6-4211-BAB5-8470F7E2D60BQ36243024-6A0E40E3-C1B5-4518-B6D9-EE142789D4FCQ36631684-45A12A97-17FE-4EFE-9B7F-A64902388ECAQ36943525-4DB26168-A898-44D6-AC4E-B5A8BF43FE8EQ36956240-364BB31C-429D-444D-AC24-0288DF416E43Q36976608-DBF41DC4-EE2B-4C20-9104-CC59A6A9CF0AQ36979610-37EA2018-8ED2-4A35-889D-AFFDB1A4F92DQ36987883-C10D3881-AC42-4F63-BBC2-92809678BC5AQ36988180-0C9F0DF8-8E0A-4EC7-8291-31562EC7C700Q37059677-1E54A16F-6BCE-4D20-92AC-6598B432001EQ40076415-83288202-0ECC-48AF-9AE8-058F0DD9B41CQ40147471-58104E66-35D7-4207-A6DF-EA10674526AAQ40374383-988B7CD6-CA18-48A4-BE4D-4080794156BF
P2860
Acylation of the 47-kilodalton major membrane immunogen of Treponema pallidum determines its hydrophobicity.
description
1989 nî lūn-bûn
@nan
1989 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
1989 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
1989年の論文
@ja
1989年論文
@yue
1989年論文
@zh-hant
1989年論文
@zh-hk
1989年論文
@zh-mo
1989年論文
@zh-tw
1989年论文
@wuu
name
Acylation of the 47-kilodalton ...... determines its hydrophobicity.
@ast
Acylation of the 47-kilodalton ...... determines its hydrophobicity.
@en
type
label
Acylation of the 47-kilodalton ...... determines its hydrophobicity.
@ast
Acylation of the 47-kilodalton ...... determines its hydrophobicity.
@en
prefLabel
Acylation of the 47-kilodalton ...... determines its hydrophobicity.
@ast
Acylation of the 47-kilodalton ...... determines its hydrophobicity.
@en
P2093
P2860
P1476
Acylation of the 47-kilodalton ...... determines its hydrophobicity.
@en
P2093
C Slaughter
J D Radolf
M V Norgard
N R Chamberlain
P2860
P304
P407
P577
1989-09-01T00:00:00Z