ArticleProceedings of the National Academy of Sciences of the United States of America2002
Translocation of a functional protein by a voltage-dependent ion channel.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
10 citing papers in PubMed, 28 citations in OpenAlex.
- Exploring Uniform, Dual, and Dynamic Topologies of Membrane Proteins by Substituted Cysteine Accessibility Method (SCAM™).Methods in molecular biology (Clifton, N.J.) · 2024Article
- Channel domain of colicin A modifies the dimeric organization of its immunity protein.The Journal of biological chemistry · 2010Article
- Thermodynamic characterization of two homologous protein complexes: associations of the semaphorin receptor plexin-B1 RhoGTPase binding domain with Rnd1 and active Rac1.Protein science : a publication of the Protein Society · 2009Article
- Lipid-dependent membrane protein topogenesis.Annual review of biochemistry · 2009Review
- Colicin N binds to the periphery of its receptor and translocator, outer membrane protein F.Structure (London, England : 1993) · 2008Article
- Colicin E2 is still in contact with its receptor and import machinery when its nuclease domain enters the cytoplasm.Journal of bacteriology · 2007Article
- Colicin biology.Microbiology and molecular biology reviews : MMBR · 2007Review
- Release of immunity protein requires functional endonuclease colicin import machinery.Journal of bacteriology · 2006Article
- Global structural rearrangement of the cell penetrating ribonuclease colicin E3 on interaction with phospholipid membranes.Protein science : a publication of the Protein Society · 2006Article
- Gating movements of colicin A and colicin Ia are different.The Journal of membrane biology · 2004Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The voltage-dependent gating of the colicin channel involves a substantial structural rearrangement that results in the transfer of about 35% of the 200 residues in its pore-forming domain across the membrane. This transfer appears to represent an unusual type of protein translocation that does not depend on a large, multimeric, protein pore. To investigate the ability of this system to transport arbitrary proteins, we made use of a pair of strongly interacting proteins, either of which could serve as a translocated cargo or as a probe to detect the other. Here we show that both an 86-residue and a 134-residue hydrophilic protein inserted into the translocated segment of colicin A are themselves translocated and are functional on the trans side of the bilayer. The disparate features of these proteins suggest that the colicin channel has a general protein translocation mechanism.
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What OpenQuestion holds
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.