ArticleScience advances2017
A nanosecond time-resolved XFEL analysis of structural changes associated with CO release from cytochrome c oxidase.
Open access · goldAbstract read
In one paragraph
Article in Science advances, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
4.6field-weighted citation impact, top 4% of its field
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
49 citing papers in PubMed, 79 citations in OpenAlex.
- A simple and practical approach for protein serial crystallography using grease matrix and large-area support film.Journal of synchrotron radiation · 2026Article
- Identification of CO-binding modes in the CuThe FEBS journal · 2025Article
- Structural and functional mechanisms of cytochrome c oxidase.Journal of inorganic biochemistry · 2025Review
- The three-dimensional structure of a proton-pumping pathway, the H-pathway, is evolutionarily conserved in all three families of cytochromeFrontiers in chemistry · 2025Article
- Mapping the Multiscale Proteomic Organization of Cellular and Disease Phenotypes.Annual review of biomedical data science · 2024Review
- Real-time observation of a metal complex-driven reaction intermediate using a porous protein crystal and serial femtosecond crystallography.Nature communications · 2024Article
- The time revolution in macromolecular crystallography.Structural dynamics (Melville, N.Y.) · 2024Article
- Time-resolved serial crystallography to track the dynamics of carbon monoxide in the active site of cytochromeScience advances · 2023Article
- Detection of a Geminate Photoproduct of Bovine CytochromeJournal of the American Chemical Society · 2023Article
- Combining on-line spectroscopy with synchrotron and X-ray free electron laser crystallography.Current opinion in structural biology · 2023Review
- Detection of a geminate photoproduct of bovine cytochrome c oxidase by time-resolved serial femtosecond crystallography.bioRxiv : the preprint server for biology · 2023Article
- Recent progress in experimental studies on the catalytic mechanism of cytochromeFrontiers in chemistry · 2023Review
- A unifying Bayesian framework for merging X-ray diffraction data.Nature communications · 2022Article
- Implications of the Essential Role of Small Molecule Ligand Binding Pockets in Protein-Protein Interactions.The journal of physical chemistry. B · 2022Article
- Time-resolved serial femtosecond crystallography on fatty-acid photodecarboxylase: lessons learned.Acta crystallographica. Section D, Structural biology · 2022Article
- Serial femtosecond crystallography.Nature reviews. Methods primers · 2022Article
- Mapping Enzyme Landscapes by Time-Resolved Crystallography with Synchrotron and X-Ray Free Electron Laser Light.Annual review of biophysics · 2022Review
- Review
- Crystallographic studies of cytochrome c and cytochrome c oxidase.Journal of biochemistry · 2022Article
- Crystal structure of CmABCB1 multi-drug exporter in lipidic mesophase revealed by LCP-SFX.IUCrJ · 2022Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
29 authors at 7 institutions in 1 country.
Atsuhiro ShimadaPicobiology Institute, Graduate School of Life Science, University of Hyogo, 3-2-1 Kouto, Kamigori-cho, Ako-gun, Hyogo 678-1297, Japan.
Minoru KuboRIKEN SPring-8 Center, 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo 679-5148, Japan.ORCID 0000-0002-1470-942X
Seiki BabaJapan Synchrotron Radiation Research Institute, 1-1-1, Kouto, Sayo-cho, Sayo-gun, Hyogo 679-5198, Japan.
Keitaro YamashitaRIKEN SPring-8 Center, 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo 679-5148, Japan.
Kunio HirataRIKEN SPring-8 Center, 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo 679-5148, Japan.
Go UenoRIKEN SPring-8 Center, 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo 679-5148, Japan.
Takashi NomuraRIKEN SPring-8 Center, 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo 679-5148, Japan.ORCID 0000-0002-4613-7403
Tetsunari KimuraGraduate School of Science, Kobe University, 1-1 Rokkodai, Nada, Kobe, Hyogo 657-8501, Japan.ORCID 0000-0003-1650-7298
Kyoko Shinzawa-ItohPicobiology Institute, Graduate School of Life Science, University of Hyogo, 3-2-1 Kouto, Kamigori-cho, Ako-gun, Hyogo 678-1297, Japan.
Junpei BabaPicobiology Institute, Graduate School of Life Science, University of Hyogo, 3-2-1 Kouto, Kamigori-cho, Ako-gun, Hyogo 678-1297, Japan.
Keita HatanoPicobiology Institute, Graduate School of Life Science, University of Hyogo, 3-2-1 Kouto, Kamigori-cho, Ako-gun, Hyogo 678-1297, Japan.
Yuki EtoPicobiology Institute, Graduate School of Life Science, University of Hyogo, 3-2-1 Kouto, Kamigori-cho, Ako-gun, Hyogo 678-1297, Japan.
Akari MiyamotoPicobiology Institute, Graduate School of Life Science, University of Hyogo, 3-2-1 Kouto, Kamigori-cho, Ako-gun, Hyogo 678-1297, Japan.
Hironori MurakamiJapan Synchrotron Radiation Research Institute, 1-1-1, Kouto, Sayo-cho, Sayo-gun, Hyogo 679-5198, Japan.
Takashi KumasakaJapan Synchrotron Radiation Research Institute, 1-1-1, Kouto, Sayo-cho, Sayo-gun, Hyogo 679-5198, Japan.
Shigeki OwadaRIKEN SPring-8 Center, 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo 679-5148, Japan.ORCID 0000-0002-1451-7612
Kensuke TonoJapan Synchrotron Radiation Research Institute, 1-1-1, Kouto, Sayo-cho, Sayo-gun, Hyogo 679-5198, Japan.ORCID 0000-0003-1218-3759
Makina YabashiJapan Synchrotron Radiation Research Institute, 1-1-1, Kouto, Sayo-cho, Sayo-gun, Hyogo 679-5198, Japan.ORCID 0000-0002-2472-1684
Yoshihiro YamaguchiPicobiology Institute, Graduate School of Life Science, University of Hyogo, 1-1-1 Kouto, Sayo, Hyogo 679-5148, Japan.
Sachiko YanagisawaPicobiology Institute, Graduate School of Life Science, University of Hyogo, 1-1-1 Kouto, Sayo, Hyogo 679-5148, Japan.
Miyuki SakaguchiPicobiology Institute, Graduate School of Life Science, University of Hyogo, 1-1-1 Kouto, Sayo, Hyogo 679-5148, Japan.
Takashi OguraPicobiology Institute, Graduate School of Life Science, University of Hyogo, 1-1-1 Kouto, Sayo, Hyogo 679-5148, Japan.
Ryo KomiyaDepartment of Mechanical Engineering, Keio University, 3-14-1 Hiyoshi, Kohoku-ku, Yokohama 223-8522, Japan.
Jiwang YanDepartment of Mechanical Engineering, Keio University, 3-14-1 Hiyoshi, Kohoku-ku, Yokohama 223-8522, Japan.
Eiki YamashitaInstitute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka 565-0871, Japan.
Masaki YamamotoRIKEN SPring-8 Center, 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo 679-5148, Japan.
Hideo AgoRIKEN SPring-8 Center, 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo 679-5148, Japan.
Shinya YoshikawaPicobiology Institute, Graduate School of Life Science, University of Hyogo, 3-2-1 Kouto, Kamigori-cho, Ako-gun, Hyogo 678-1297, Japan.ORCID 0000-0002-6020-0974
Tomitake TsukiharaPicobiology Institute, Graduate School of Life Science, University of Hyogo, 3-2-1 Kouto, Kamigori-cho, Ako-gun, Hyogo 678-1297, Japan.
University of Hyogo · JPSPring-8 · JPJapan Synchrotron Radiation Research Institute · JPJapan Science and Technology Agency · JPKeio University · JPKobe University · JPThe University of Osaka · JP
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bovine cytochrome c oxidase (CcO), a 420-kDa membrane protein, pumps protons using electrostatic repulsion between protons transferred through a water channel and net positive charges created by oxidation of heme
Indexed as
Carbon MonoxideElectron Transport Complex IVHemeHydrogen BondingModels, MolecularMolecular ConformationMolecular StructureOxidation-ReductionPhotolysisStructure-Activity RelationshipCarbon MonoxideElectron Transport Complex IVHeme
Identifiers
What OpenQuestion holds
Textmetadata
LicenceCC BY-NC
Read underepoch 390
Registered trials
None linked
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.