(Q42370534)

English

The transmembrane tyrosines Y56, Y91 and Y167 play important roles in determining the affinity and transport rate of the rabbit proton-coupled peptide transporter PepT1

scientific article published on 21 April 2009

In more languages

Statements

scholarly article

1 reference

Europe PubMed Central

28 October 2017

The transmembrane tyrosines Y56, Y91 and Y167 play important roles in determining the affinity and transport rate of the rabbit proton-coupled peptide transporter PepT1 (English)

1 reference

Europe PubMed Central

28 October 2017

transmembrane transport

0 references

transmembrane protein

0 references

author name string

Myrtani Pieri

1

1 reference

Europe PubMed Central

28 October 2017

Christine Gan

2

1 reference

Europe PubMed Central

28 October 2017

Patrick Bailey

3

1 reference

Europe PubMed Central

28 October 2017

David Meredith

4

1 reference

Europe PubMed Central

28 October 2017

publication date

21 April 2009

1 reference

Europe PubMed Central

28 October 2017

International Journal of Biochemistry & Cell Biology

1 reference

Europe PubMed Central

28 October 2017

41

1 reference

Europe PubMed Central

28 October 2017

11

1 reference

Europe PubMed Central

28 October 2017

2204-2213

1 reference

Europe PubMed Central

28 October 2017

An intracellular interaction network regulates conformational transitions in the dopamine transporter.

1 reference

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29 May 2018

Site-directed mutagenesis of Arginine282 suggests how protons and peptides are co-transported by rabbit PepT1

1 reference

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Calcium block of single sodium channels: role of a pore-lining aromatic residue

1 reference

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Cysteine scanning of transmembrane domain three of the human dipeptide transporter: implications for substrate transport

1 reference

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29 May 2018

Molecular modeling of PepT1--towards a structure

1 reference

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A cation-pi interaction discriminates among sodium channels that are either sensitive or resistant to tetrodotoxin block.

1 reference

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A cation-pi interaction between extracellular TEA and an aromatic residue in potassium channels.

1 reference

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From bacteria to man: archaic proton-dependent peptide transporters at work

1 reference

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Three-dimensional quantitative structure-activity relationship analyses of beta-lactam antibiotics and tripeptides as substrates of the mammalian H+/peptide cotransporter PEPT1.

1 reference

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Proton-coupled electron transfer: a reaction chemist's view

1 reference

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Peptide transporters: structure, function, regulation and application for drug delivery

1 reference

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Analysis of Transmembrane Segment 7 of the Dipeptide Transporter hPepT1 by Cysteine-scanning Mutagenesis

1 reference

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Transmembrane segment 5 of the dipeptide transporter hPepT1 forms a part of the substrate translocation pathway

1 reference

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Electron, proton and hydrogen-atom transfers in photosynthetic water oxidation

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Structure and function of eukaryotic peptide transporters

1 reference

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1 reference

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Biopharmaceutics of transmucosal peptide and protein drug administration: role of transport mechanisms with a focus on the involvement of PepT1.

1 reference

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Molecular identification of a role for tyrosine 167 in the function of the human intestinal proton- coupled dipeptide transporter (hPepT1).

1 reference

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Identification of a potential substrate binding domain in the mammalian peptide transporters PEPT1 and PEPT2 using PEPT1-PEPT2 and PEPT2-PEPT1 chimeras.

1 reference

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Cation-pi interactions in chemistry and biology: a new view of benzene, Phe, Tyr, and Trp

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A mechanism for ion selectivity in potassium channels: computational studies of cation-pi interactions

1 reference

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A simple method for displaying the hydropathic character of a protein

1 reference

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Potency Difference between the Zwitterion Form and the Cation Forms of Tetrodotoxin

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Influence of amino acid side-chain modification on the uptake system for beta-lactam antibiotics and dipeptides from rabbit small intestine

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1 reference

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Evidence that the rabbit proton-peptide co-transporter PepT1 is a multimer when expressed in Xenopus laevis oocytes.

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Site-directed mutation of arginine 282 to glutamate uncouples the movement of peptides and protons by the rabbit proton-peptide cotransporter PepT1.

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1 reference

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Structure, function, and molecular modeling approaches to the study of the intestinal dipeptide transporter PepT1.

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Expression cloning of a mammalian proton-coupled oligopeptide transporter.

1 reference

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How to Make Drugs Orally Active: A Substrate Template for Peptide Transporter PepT1

1 reference

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Membrane topology of the human dipeptide transporter, hPEPT1, determined by epitope insertions

1 reference

https://pubmed.ncbi.nlm.nih.gov/19389486

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Affinity prediction for substrates of the peptide transporter PepT1

1 reference

https://pubmed.ncbi.nlm.nih.gov/19389486

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1016/J.BIOCEL.2009.04.014

1 reference

Europe PubMed Central

28 October 2017

1 reference

Europe PubMed Central

28 October 2017

1 reference

Europe PubMed Central

28 October 2017

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0 references

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