ArticleBiophysical journal2006
Locking CNGA1 channels in the open and closed state.
Article in Biophysical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
8 citing papers in PubMed, 18 citations in OpenAlex.
- Conformational rearrangements in the transmembrane domain of CNGA1 channels revealed by single-molecule force spectroscopy.Nature communications · 2015Article
- Activation of Slo2.1 channels by niflumic acid.The Journal of general physiology · 2010Article
- Gating in CNGA1 channels.Pflugers Archiv : European journal of physiology · 2010Review
- Conformational rearrangements in the S6 domain and C-linker during gating in CNGA1 channels.European biophysics journal : EBJ · 2009Article
- Computational molecular biology approaches to ligand-target interactions.HFSP journal · 2009Article
- Movements of native C505 during channel gating in CNGA1 channels.European biophysics journal : EBJ · 2009Article
- The analysis of desensitizing CNGA1 channels reveals molecular interactions essential for normal gating.The Journal of general physiology · 2009Article
- A comparison of electrophysiological properties of the CNGA1, CNGA1tandem and CNGA1cys-free channels.European biophysics journal : EBJ · 2008Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
With the aim of understanding the relation between structure and gating of CNGA1 channels from bovine rod, an extensive cysteine scanning mutagenesis was performed. Each residue from Phe-375 to Val-424 was mutated into a cysteine one at a time and the modification caused by various sulfhydryl reagents was analyzed. The addition of the mild oxidizing agent copper phenanthroline (CuP) in the open (presence of 1 mM cGMP) or closed state locked the channel in the respective states. A subsequent treatment with the reducing agent DTT restored normal gating fully in the open state and partially in the closed state. This action of CuP was not observed when F380 was mutated into a cysteine in the cysteine-free CNGA1 channel and in the double mutant C314S&F380C. These observations suggest that these effects are mediated by the formation of a disulfide bond (S-S) between F380C and the endogenous Cys-314 in the S5 segment. It can be rationalized by supposing that during gating the S6 segment rotates anticlockwise-when viewed from the extracellular side-by approximately 30 degrees .
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Registered trials
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.