scholarly article | Q13442814 |
P50 | author | Helen Saibil | Q11251973 |
Elena V. Orlova | Q53517900 | ||
Remi Fronzes | Q56810548 | ||
P2093 | author name string | Gabriel Waksman | |
Luchun Wang | |||
Eva Schäfer | |||
P2860 | cites work | Structural insights into the assembly of the type III secretion needle complex. | Q24547949 |
NMR structure of a complex between the VirB9/VirB7 interaction domains of the pKM101 type IV secretion system | Q27643638 | ||
The Agrobacterium T-DNA transport pore proteins VirB8, VirB9, and VirB10 interact with one another | Q28492355 | ||
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Structures of two core subunits of the bacterial type IV secretion system, VirB8 from Brucella suis and ComB10 from Helicobacter pylori | Q33934401 | ||
Detergent extraction identifies different VirB protein subassemblies of the type IV secretion machinery in the membranes of Agrobacterium tumefaciens | Q34038505 | ||
Peptide linkage mapping of the Agrobacterium tumefaciens vir-encoded type IV secretion system reveals protein subassemblies | Q34038979 | ||
Biogenesis, architecture, and function of bacterial type IV secretion systems | Q34449723 | ||
The Agrobacterium tumefaciens virB7 gene product, a proposed component of the T-complex transport apparatus, is a membrane-associated lipoprotein exposed at the periplasmic surface | Q35607950 | ||
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Agrobacterium VirB10, an ATP energy sensor required for type IV secretion | Q37704821 | ||
Functional Subsets of the VirB Type IV Transport Complex Proteins Involved in the Capacity of Agrobacterium tumefaciens To Serve as a Recipient in virB -Mediated Conjugal Transfer of Plasmid RSF1010 | Q39753926 | ||
The lipoprotein VirB7 interacts with VirB9 in the membranes of Agrobacterium tumefaciens | Q39844534 | ||
Definition of a bacterial type IV secretion pathway for a DNA substrate | Q41853646 | ||
Agrobacterium tumefaciens VirB9, an outer-membrane-associated component of a type IV secretion system, regulates substrate selection and T-pilus biogenesis | Q42754911 | ||
P433 | issue | 5911 | |
P407 | language of work or name | English | Q1860 |
P304 | page(s) | 266-268 | |
P577 | publication date | 2009-01-01 | |
P1433 | published in | Science | Q192864 |
P1476 | title | Structure of a type IV secretion system core complex | |
P478 | volume | 323 |
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Q28484806 | Cag3 is a novel essential component of the Helicobacter pylori Cag type IV secretion system outer membrane subcomplex |
Q39429210 | Caught in the act: the dialogue between bacteriophage R17 and the type IV secretion machine of plasmid R1. |
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Q57804824 | Cryo-EM structure of the bacteria-killing type IV secretion system core complex from Xanthomonas citri |
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Q39104032 | DNA Transfer and Toll-like Receptor Modulation by Helicobacter pylori |
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Q40151222 | Defining Assembly Pathways by Fluorescence Microscopy. |
Q42174044 | Delineation of polar localization domains of Agrobacterium tumefaciens type IV secretion apparatus proteins VirB4 and VirB11. |
Q33617984 | Diversity of secretion systems associated with virulence characteristics of the classical bordetellae |
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Q45944000 | Effective prediction of bacterial type IV secreted effectors by combined features of both C-termini and N-termini. |
Q89968113 | Electrostatic Switching Controls Channel Dynamics of the Sensor Protein VirB10 in A. tumefaciens Type IV Secretion System |
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Q33817650 | Expression and functional characterization of the Agrobacterium VirB2 amino acid substitution variants in T-pilus biogenesis, virulence, and transient transformation efficiency |
Q39414724 | F plasmid TraF and TraH are components of an outer membrane complex involved in conjugation |
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Q47865720 | Going round in circles: the structural biology of type III secretion systems |
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Q34016256 | Helicobacter pylori exploits a unique repertoire of type IV secretion system components for pilus assembly at the bacteria-host cell interface |
Q35999402 | Immunogenicity of Outer Membrane Proteins VirB9-1 and VirB9-2, a Novel Nanovaccine against Anaplasma marginale |
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Q40728044 | Isolation of bacterial type IV machine subassemblies. |
Q48014045 | Labeling of Membrane Complexes for Electron Microscopy. |
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