Identification of Loop D Domain Amino Acids in the Human Aquaporin-1 Channel Involved in Activation of the Ionic Conductance and Inhibition by AqB011. (Q55277058)

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scientific article published on 27 April 2018

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English	Identification of Loop D Domain Amino Acids in the Human Aquaporin-1 Channel Involved in Activation of the Ionic Conductance and Inhibition by AqB011.	scientific article published on 27 April 2018

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scholarly article

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Europe PubMed Central

PMC publication ID

30 June 2018

http://europepmc.org/abstract/PMC/5934433

Identification of Loop D Domain Amino Acids in the Human Aquaporin-1 Channel Involved in Activation of the Ionic Conductance and Inhibition by AqB011. (English)

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Europe PubMed Central

PMC publication ID

30 June 2018

http://europepmc.org/abstract/PMC/5934433

Saeed Nourmohammadi

3

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:29755973%20AND%20SRC:MED&resulttype=core&format=json

13 June 2020

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Mohamad Kourghi

1

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:29755973%20AND%20SRC:MED&resulttype=core&format=json

13 June 2020

Michael L De Ieso

2

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13 June 2020

Jinxin V Pei

4

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13 June 2020

Andrea J Yool

5

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13 June 2020

publication date

27 April 2018

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Europe PubMed Central

PMC publication ID

30 June 2018

http://europepmc.org/abstract/PMC/5934433

Frontiers in Chemistry

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13 June 2020

6

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13 June 2020

142

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13 June 2020

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Creative Commons Attribution 4.0 International

27 April 2018

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April 2022 Public Data File from Crossref

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A multilevel theoretical study to disclose the binding mechanisms of gold(III) bipyridyl compounds as selective aquaglyceroporin inhibitors.

1 reference

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Activating mutations of the TRPML1 channel revealed by proline-scanning mutagenesis

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Aquaporins: multiple roles in the central nervous system

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Ion channel function of aquaporin-1 natively expressed in choroid plexus.

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Physiological roles of aquaporins in the choroid plexus

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Aquaporin-1, nothing but a water channel.

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Single amino acids in the carboxyl terminal domain of aquaporin-1 contribute to cGMP-dependent ion channel activation

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The (beta)gamma subunits of G proteins gate a K(+) channel by pivoted bending of a transmembrane segment

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Tetraethylammonium block of water flux in Aquaporin-1 channels expressed in kidney thin limbs of Henle's loop and a kidney-derived cell line

1 reference

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New roles for old holes: ion channel function in aquaporin-1

1 reference

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Structural basis of water-specific transport through the AQP1 water channel

1 reference

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Water and ion permeation of aquaporin-1 in planar lipid bilayers. Major differences in structural determinants and stoichiometry.

1 reference

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Coupling Gbetagamma-dependent activation to channel opening via pore elements in inwardly rectifying potassium channels

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Visualization of a water-selective pore by electron crystallography in vitreous ice

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30 June 2018

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Distribution of the aquaporin CHIP in secretory and resorptive epithelia and capillary endothelia

1 reference

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30 June 2018

The MIP family of integral membrane channel proteins: sequence comparisons, evolutionary relationships, reconstructed pathway of evolution, and proposed functional differentiation of the two repeated halves of the proteins

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Side-chain accessibilities in the pore of a K+ channel probed by sulfhydryl-specific reagents after cysteine-scanning mutagenesis

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Aquaporin CHIP: the archetypal molecular water channel

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Proline motifs in peptides and their biological processing

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Helix geometry in proteins

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p-(Chloromercuri)benzenesulfonate binding by membrane proteins and the inhibition of water transport in human erythrocytes

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High-resolution epitope mapping of hGH-receptor interactions by alanine-scanning mutagenesis

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Purified lens junctional protein forms channels in planar lipid films

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Proline residues in transmembrane helices: structural or dynamic role?

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Properties of channels reconstituted from the major intrinsic protein of lens fiber membranes

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Divalent Cations Regulate the Ion Conductance Properties of Diverse Classes of Aquaporins.

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Non-selective cation channel activity of aquaporin AtPIP2;1 regulated by Ca2+ and pH.

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Bumetanide Derivatives AqB007 and AqB011 Selectively Block the Aquaporin-1 Ion Channel Conductance and Slow Cancer Cell Migration

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Discovery of novel human aquaporin-1 blockers

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1 reference

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

The influence of proline residues on alpha-helical structure

1 reference

https://pubmed.ncbi.nlm.nih.gov/29755973

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.3389/FCHEM.2018.00142

1 reference

Europe PubMed Central

PMC publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:29755973%20AND%20SRC:MED&resulttype=core&format=json

13 June 2020

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:29755973%20AND%20SRC:MED&resulttype=core&format=json

13 June 2020

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:29755973%20AND%20SRC:MED&resulttype=core&format=json

13 June 2020

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