ArticleProceedings of the National Academy of Sciences of the United States of America2004
Crystal structure of a central stalk subunit C and reversible association/dissociation of vacuole-type ATPase.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.
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.
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
65 citing papers in PubMed, 141 citations in OpenAlex.
- Membrane platform protein PulF of themBio · 2024Article
- Cryo-EM analysis of V/A-ATPase intermediates reveals the transition of the ground-state structure to steady-state structures by sequential ATP binding.The Journal of biological chemistry · 2023Article
- Structural and functional understanding of disease-associated mutations in V-ATPase subunit a1 and other isoforms.Frontiers in molecular neuroscience · 2023Review
- Structures of multisubunit membrane complexes with the CRYO ARM 200.Microscopy (Oxford, England) · 2022Article
- Structural asymmetry governs the assembly and GTPase activity of McrBC restriction complexes.Nature communications · 2020Article
- Mechanical inhibition of isolated VeLife · 2020Article
- Diversification of the type IV filament superfamily into machines for adhesion, protein secretion, DNA uptake, and motility.PLoS biology · 2019Article
- Mass spectrometry: From plasma proteins to mitochondrial membranes.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Structural Asymmetry and Kinetic Limping of Single Rotary F-ATP Synthases.Molecules (Basel, Switzerland) · 2019Review
- A Hybrid Secretion System Facilitates Bacterial Sporulation: A Structural Perspective.Microbiology spectrum · 2019Review
- Cryo-EM studies of the rotary HBiophysics and physicobiology · 2019Review
- Valproate inhibits glucose-stimulated insulin secretion in beta cells.Histochemistry and cell biology · 2018Article
- Structural characterization of SpoIIIAB sporulation-essential protein in Bacillus subtilis.Journal of structural biology · 2018Article
- Cryo EM structure of intact rotary HNature communications · 2018Article
- Reversible Association of the Hemagglutinin Subcomplex, HA-33/HA-17 Trimer, with the Botulinum Toxin Complex.The protein journal · 2017Article
- Breaking up and making up: The secret life of the vacuolar HProtein science : a publication of the Protein Society · 2017Review
- FOXO/DAF-16 Activation Slows Down Turnover of the Majority of Proteins in C. elegans.Cell reports · 2016Article
- Cryo-EM studies of the structure and dynamics of vacuolar-type ATPases.Science advances · 2016Review
- Computational modeling of TC0583 as a putative component of the Chlamydia muridarum V-type ATP synthase complex and assessment of its protective capabilities as a vaccine antigen.Microbes and infection · 2016Article
- Models for the a subunits of the Thermus thermophilus V/A-ATPase and Saccharomyces cerevisiae V-ATPase enzymes by cryo-EM and evolutionary covariance.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
5 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
12 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The vacuole-type ATPases (V-ATPases) exist in various intracellular compartments of eukaryotic cells to regulate physiological processes by controlling the acidic environment. The crystal structure of the subunit C of Thermus thermophilus V-ATPase, homologous to eukaryotic subunit d of V-ATPases, has been determined at 1.95-A resolution and located into the holoenzyme complex structure obtained by single particle analysis as suggested by the results of subunit cross-linking experiments. The result shows that V-ATPase is substantially longer than the related F-type ATPase, due to the insertion of subunit C between the V(1) (soluble) and the V(o) (membrane bound) domains. Subunit C, attached to the V(o) domain, seems to have a socket like function in attaching the central-stalk subunits of the V(1) domain. This architecture seems essential for the reversible association/dissociation of the V(1) and the V(o) domains, unique for V-ATPase activity regulation.
Indexed as
Identifiers
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.