Proline residues in two tightly coupled helices of the sulphate transporter, SHST1, are important for sulphate transport - Wikidata - awgldk - TriplyDB

Proline residues in two tightly coupled helices of the sulphate transporter, SHST1, are important for sulphate transport

Proline residues in two tightly coupled helices of the sulphate transporter, SHST1, are important for sulphate transport

http://www.wikidata.org/entity/Q28365617

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Essential helix interactions in the anion transporter domain of prestin revealed by evolutionary trace analysis The cytosolic half of helix III forms the substrate exit route during permeation events of the sodium/bile acid cotransporter ASBT.Role of conserved prolines in the structure and function of the Na+/dicarboxylate cotransporter 1, NaDC1.Conformational flexibility of helix VI is essential for substrate permeation of the human apical sodium-dependent bile acid transporter Residues in the eighth transmembrane domain of the proton-coupled folate transporter (SLC46A1) play an important role in defining the aqueous translocation pathway and in folate substrate binding.Proline residues in transmembrane segment IV are critical for activity, expression and targeting of the Na+/H+ exchanger isoform 1.Conformational Propensities of Peptides Mimicking Transmembrane Helix 5 and Motif C in Wild-type and Mutant Vesicular Acetylcholine Transporters.Sulfate Transporters in Dissimilatory Sulfate Reducing Microorganisms: A Comparative Genomics Analysis.

P2860

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P2860

Proline residues in two tightly coupled helices of the sulphate transporter, SHST1, are important for sulphate transport

http://www.wikidata.org/entity/Q28365617

description

2001 nî lūn-bûn

@nan

2001 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

2001 թվականի հունիսին հրատարակված գիտական հոդված

@hy

2001年の論文

@ja

2001年論文

@yue

2001年論文

@zh-hant

2001年論文

@zh-hk

2001年論文

@zh-mo

2001年論文

@zh-tw

2001年论文

@wuu

name

Proline residues in two tightl ...... portant for sulphate transport

@ast

Proline residues in two tightl ...... portant for sulphate transport

@en

Proline residues in two tightl ...... portant for sulphate transport

@nl

type

label

Proline residues in two tightl ...... portant for sulphate transport

@ast

Proline residues in two tightl ...... portant for sulphate transport

@en

Proline residues in two tightl ...... portant for sulphate transport

@nl

prefLabel

Proline residues in two tightl ...... portant for sulphate transport

@ast

Proline residues in two tightl ...... portant for sulphate transport

@en

Proline residues in two tightl ...... portant for sulphate transport

@nl

P1433

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P1476

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P2860

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P932

Q28365617-14DE7BDB-D813-4690-A116-4DD5FE0CC9DB

P1433

Biochemical Journal

P1476

Proline residues in two tightl ...... portant for sulphate transport

@en

P2093

M C Shelden

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

M L Tierney

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

P Loughlin

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

S M Howitt

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

P2860

The structure of Fis mutant Pro61Ala illustrates that the kink within the long alpha-helix is not due to the presence of the proline residue

Isolation of a cDNA from Saccharomyces cerevisiae that encodes a high affinity sulphate transporter at the plasma membrane.

Studies on the transformation of intact yeast cells by the LiAc/SS-DNA/PEG procedure

Mutational analysis of the Escherichia coli phosphate-specific transport system, a member of the traffic ATPase (or ABC) family of membrane transporters. A role for proline residues in transmembrane helices

Prediction of protein conformation

Glycophorin A dimerization is driven by specific interactions between transmembrane alpha-helices

Amino acid preferences for specific locations at the ends of alpha helices

The GxxxG motif: a framework for transmembrane helix-helix association.

Phylogenetic characterization of novel transport protein families revealed by genome analyses.

A family of mammalian anion transporters and their involvement in human genetic diseases.

P304

589-94

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

P31

scholarly article

P407

P433

Pt 2

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

P478

356

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P577

2001-06-01T00:00:00Z

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

P698

11368789

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P932

1221873

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