The cytosolic half of helix III forms the substrate exit route during permeation events of the sodium/bile acid cotransporter ASBT. (Q33877695)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:19653651%20AND%20SRC:MED&resulttype=core&format=json

4 February 2020

title

The cytosolic half of helix III forms the substrate exit route during permeation events of the sodium/bile acid cotransporter ASBT (English)

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4 February 2020

3

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4 February 2020

author name string

Naissan Hussainzada

series ordinal

1

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4 February 2020

Tatiana Claro Da Silva

series ordinal

2

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language of work or name

English

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publication date

1 September 2009

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4 February 2020

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:19653651%20AND%20SRC:MED&resulttype=core&format=json

4 February 2020

volume

48

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issue

36

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4 February 2020

page(s)

8528-8539

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Conformational flexibility of helix VI is essential for substrate permeation of the human apical sodium-dependent bile acid transporter

4 February 2020

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28 July 2018

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28 July 2018

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28 July 2018

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Conformational dynamics of helix S6 from Shaker potassium channel: simulation studies.

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

28 July 2018

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28 July 2018

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28 July 2018

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Conserved aspartic acid residues lining the extracellular loop 1 of sodium-coupled bile acid transporter ASBT Interact with Na+ and 7alpha-OH moieties on the ligand cholestane skeleton.

28 July 2018

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Cytosolic half of transmembrane domain IV of the human bile acid transporter hASBT (SLC10A2) forms part of the substrate translocation pathway

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Electrostatic and potential cation-pi forces may guide the interaction of extracellular loop III with Na+ and bile acids for human apical Na+-dependent bile acid transporter

29 October 2018

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29 October 2018

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Direct evidence that two cysteines in the dopamine transporter form a disulfide bond.

29 October 2018

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29 October 2018

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29 October 2018

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29 October 2018

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29 October 2018

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29 October 2018

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29 October 2018

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29 October 2018

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1-[4-[4[(4R,5R)-3,3-Dibutyl-7-(dimethylamino)-2,3,4,5-tetrahydro-4-hydroxy-1,1-dioxido-1-benzothiepin-5-yl]phenoxy]butyl]-4-aza-1-azoniabicyclo[2.2.2]octane methanesulfonate (SC-435), an ileal apical sodium-codependent bile acid transporter inhibito

29 October 2018

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Proline-induced hinges in transmembrane helices: possible roles in ion channel gating

29 October 2018

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Proline residues in transmembrane alpha helices affect the folding of bacteriorhodopsin

29 October 2018

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Hinges, swivels and switches: the role of prolines in signalling via transmembrane alpha-helices

29 October 2018

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Critical amino acid residues in transmembrane span 7 of the serotonin transporter identified by random mutagenesis

29 October 2018

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Identification of a Mutation in the Ileal Sodium-dependent Bile Acid Transporter Gene That Abolishes Transport Activity

29 October 2018

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The influence of proline residues on alpha-helical structure

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12 December 2020

Proline residues in transmembrane helices of channel and transport proteins: a molecular modelling study

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Determination of external loop topology in the serotonin transporter by site-directed chemical labeling

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Substituted-cysteine accessibility method

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Bile acid uptake via the human apical sodium-bile acid cotransporter is electrogenic

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Transmembrane Domain VII of the Human Apical Sodium-Dependent Bile Acid Transporter ASBT (SLC10A2) Lines the Substrate Translocation Pathway

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A model for the topology of excitatory amino acid transporters determined by the extracellular accessibility of substituted cysteines

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Identifiers

DOI

10.1021/BI900616W

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:19653651%20AND%20SRC:MED&resulttype=core&format=json

4 February 2020

1 reference

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4 February 2020

PubMed publication ID

19653651

1 reference