Evidence map›Paper›PMID 19034494›Full record

ArticlePflugers Archiv : European journal of physiology2009

Probing S4 and S5 segment proximity in mammalian hyperpolarization-activated HCN channels by disulfide bridging and Cd2+ coordination.

Damian C Bell, Harma K Turbendian, Matthew T Valley, Lei Zhou, John H Riley, Steven A Siegelbaum, Gareth R Tibbs

Abstract read
In one paragraph

Article in Pflugers Archiv : European journal of physiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

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Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

7 citing papers in PubMed.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors.

Damian C BellDepartment of Neuroscience, Columbia University, 722 West 168th Street, New York, NY 10032, USA.
Harma K Turbendian
Matthew T Valley
Lei Zhou
John H Riley
Steven A Siegelbaum
Gareth R Tibbs

Funding

Regulation of HCN channel trafficking and function in the brain by TRIP8bR01NS036658 · NINDS · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI SIEGELBAUM, STEVEN A · 1998 to 2016
$4.5M
Howard Hughes Medical InstituteNINDS NIH HHS R01 NS036658NINDS NIH HHS R01NS36658Wellcome Trust
6 · The paper itself

Abstract

We explored the structural basis of voltage sensing in the HCN1 hyperpolarization-activated cyclic nucleotide-gated cation channel by examining the relative orientation of the voltage sensor and pore domains. The opening of channels engineered to contain single cysteine residues at the extracellular ends of the voltage-sensing S4 (V246C) and pore-forming S5 (C303) domains is inhibited by formation of disulfide or cysteine:Cd(2+) bonds. As Cd(2+) coordination is promoted by depolarization, the S4-S5 interaction occurs preferentially in the closed state. The failure of oxidation to catalyze dimer formation, as assayed by Western blotting, indicates the V246C:C303 interaction occurs within a subunit. Intriguingly, a similar interaction has been observed in depolarization-activated Shaker voltage-dependent potassium (Kv) channels at depolarized potentials but such an intrasubunit interaction is inconsistent with the X-ray crystal structure of Kv1.2, wherein S4 approaches S5 of an adjacent subunit. These findings suggest channels of opposite voltage-sensing polarity adopt a conserved S4-S5 orientation in the depolarized state that is distinct from that trapped upon crystallization.

Indexed as

AnimalsCadmiumCyclic Nucleotide-Gated Cation ChannelsCysteineDisulfidesOocytesPatch-Clamp TechniquesPhenanthrolinesXenopus laevis1,10-phenanthrolineCadmiumCyclic Nucleotide-Gated Cation ChannelsCysteineDisulfidesPhenanthrolines

Identifiers

PMID19034494
PMCPMC2748781

What OpenQuestion holds

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.