Translocator proteins in the two-partner secretion family have multiple domains. - Wikidata - wikimedia - TriplyDB

Translocator proteins in the two-partner secretion family have multiple domains.

Translocator proteins in the two-partner secretion family have multiple domains.

http://www.wikidata.org/entity/Q30159816

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The structure of the Haemophilus influenzae HMW1 pro-piece reveals a structural domain essential for bacterial two-partner secretion Protein domain of unknown function 3233 is a translocation domain of autotransporter secretory mechanism in gamma proteobacteria Type V Secretion: the Autotransporter and Two-Partner Secretion Pathways The TpsB translocator HMW1B of haemophilus influenzae forms a large conductance channel.Structure of the Haemophilus influenzae HMW1B translocator protein: evidence for a twin pore.The HMW1C-like glycosyltransferases--an enzyme family with a sweet tooth for simple sugars.Structural determinants of the interaction between the TpsA and TpsB proteins in the Haemophilus influenzae HMW1 two-partner secretion system.

P2860

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P2860

Translocator proteins in the two-partner secretion family have multiple domains.

http://www.wikidata.org/entity/Q30159816

description

2006 nî lūn-bûn

@nan

2006 թուականի Ապրիլին հրատարակուած գիտական յօդուած

@hyw

2006 թվականի ապրիլին հրատարակված գիտական հոդված

@hy

2006年の論文

@ja

2006年論文

@yue

2006年論文

@zh-hant

2006年論文

@zh-hk

2006年論文

@zh-mo

2006年論文

@zh-tw

2006年论文

@wuu

name

Translocator proteins in the two-partner secretion family have multiple domains.

@ast

Translocator proteins in the two-partner secretion family have multiple domains.

@en

type

label

Translocator proteins in the two-partner secretion family have multiple domains.

@ast

Translocator proteins in the two-partner secretion family have multiple domains.

@en

prefLabel

Translocator proteins in the two-partner secretion family have multiple domains.

@ast

Translocator proteins in the two-partner secretion family have multiple domains.

@en

P1433

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P1476

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P2093

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P2860

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P31

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P356

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P407

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P433

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P478

Q30159816-5A461352-DC29-4311-851D-805B218B8F58

P50

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P577

Q30159816-96E4A37F-039E-4E13-B52B-69812721A987

P5875

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P698

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P356

P1433

Journal of Biological Chemistry

P1476

Translocator proteins in the two-partner secretion family have multiple domains

@en

P2093

Amy Z Buscher

http://www.w3.org/2001/XMLSchema#string

Gail G Hardy

http://www.w3.org/2001/XMLSchema#string

Joseph W St Geme

http://www.w3.org/2001/XMLSchema#string

Neeraj K Surana

http://www.w3.org/2001/XMLSchema#string

Susan Grass

http://www.w3.org/2001/XMLSchema#string

P2860

Crystal structures explain functional properties of two E. coli porins

Siderophore-mediated iron transport: crystal structure of FhuA with bound lipopolysaccharide

Crystal structure of the outer membrane active transporter FepA from Escherichia coli

Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes

Prediction of protein secondary structure at better than 70% accuracy

High efficiency transformation of E. coli by high voltage electroporation

Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set

Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form

Topology of the outer membrane usher PapC determined by site-directed fluorescence labeling.

The pore size of the autotransporter domain is critical for the active translocation of the passenger domain.

P304

18051-18058

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1074/JBC.M600036200

http://www.w3.org/2001/XMLSchema#string

P407

P433

26

http://www.w3.org/2001/XMLSchema#string

P478

281

http://www.w3.org/2001/XMLSchema#string

P50

Thomas E Kehl-Fie

P577

2006-04-28T00:00:00Z

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P5875

7131993

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P698

16648638

http://www.w3.org/2001/XMLSchema#string