The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Tubules, rods and spirals: diverse modes of SepF-FtsZ assembling
Preprint — published as 10.1002/cm.21975 · Paper page
Abstract
Z-ring formation by FtsZ, the master assembler of divisome, is a key step in bacterial cell division. Both formation and membrane anchoring of the Z-ring requires assistance of a number of Z-ring binding proteins, such as FtsA, EzrA, SepF, SepH and ZipA. SepF participates in bundling and membrane anchoring of FtsZ in gram-positive bacteria. We report in vitro biophysical studies of the interactions between FtsZ and cytoplasmic component of cognate SepF from three different bacteria: Mycobacterium tuberculosis , Staphylococcus aureus and Enterococcus gallinarum. While the cytosolic domain of SepF from M. tuberculosis is a dimer, those from S. aureus and E. gallinarum polymerize to form ring-like structures. Mycobacterial SepF helps in bundling of FtsZ filaments to form thick filaments and large spirals. On the other hand, ring-forming SepF from the Firmicutes bundle FtsZ into tubules.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Highly accurate protein structure prediction with AlphaFold
Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764
Research works printed but not linked: 73
- 10.1016/j.ceb.2020.10.013 · DOI
- 10.1002/pro.3779 · DOI
- 10.1016/j.ijbiomac.2015.08.030 · DOI
- 10.1126/science.aak9973 · DOI · Paper page
- 10.1074/jbc.M111.330324 · DOI
- 10.1038/s41579-023-00942-x · DOI
- 10.1371/journal.pone.0043293 · DOI
- 10.1074/jbc.M703788200 · DOI
- 10.14348/molcells.2016.0202 · DOI
- 10.1016/S0065-2911(09)05502-7 · DOI
- 10.1111/j.1365-2958.2010.07352.x · DOI
- 10.1016/j.jmb.2022.167817 · DOI · Paper page
- 10.1073/pnas.1313978110 · DOI · Paper page
- 10.1128/JB.01258-10 · DOI
- 10.1128/JB.00176-12 · DOI
- 10.1073/pnas.93.1.519 · DOI · Paper page
- 10.1107/S1600576717007786 · DOI
- 10.1128/JB.01758-08 · DOI
- 10.1111/mmi.13050 · DOI
- 10.1101/gad.1014102 · DOI
- 10.1101/2024.01.12.575403 · DOI
- 10.1038/emboj.2010.345 · DOI
- 10.1038/nrmicro.2016.26 · DOI
- 10.1038/s41598-018-25355-2 · DOI
- 10.1016/S0092-8674(00)81838-3 · DOI
- 10.1128/JB.01245-10 · DOI
- 10.1111/j.1365-2958.2005.04987.x · DOI · Paper page
- 10.1074/jbc.M009810200 · DOI
- 10.1128/JB.02157-12 · DOI
- 10.1016/j.bpj.2017.08.046 · DOI
- 10.1111/febs.15235 · DOI
- 10.1111/j.1365-2958.2006.05184.x · DOI
- 10.1155/2012/905832 · DOI
- 10.1038/34472 · DOI
- 10.1247/csf.24.285 · DOI
- 10.1002/cm.21054 · DOI · Paper page
- 10.1107/S1600576720013412 · DOI · Paper page
- 10.1107/S0907444912022640 · DOI
- 10.1146/annurev-biophys-121219-081703 · DOI
- 10.7554/eLife.95557.1 · DOI
- 10.1038/s41592-022-01488-1 · DOI · Paper page
- 10.1093/emboj/19.13.3179 · DOI
- 10.1128/JB.181.3.823-832.1999 · DOI
- 10.1111/mmi.15067 · DOI
- 10.1093/femsre/fuv040 · DOI
- 10.1073/pnas.1222254110 · DOI
- 10.1093/bioinformatics/btm076 · DOI
- 10.1038/s41467-021-23099-8 · DOI
- 10.1107/S0909049513010431 · DOI
- 10.1093/emboj/21.4.685 · DOI
- 10.1111/j.1365-2958.2005.04522.x · DOI
- 10.1002/bip.21136 · DOI
- 10.1074/jbc.M109.084079 · DOI
- 10.1016/j.ejcb.2023.151380 · DOI
- 10.1038/s41598-020-78431-x · DOI
- 10.7554/eLife.63387 · DOI
- 10.1098/rstb.2015.0028 · DOI
- 10.1371/journal.pbio.3001497 · DOI
- 10.1038/nmeth.2019 · DOI · Paper page
- 10.1016/S0006-3495(00)76713-0 · DOI
- 10.1021/bi700710j · DOI · Paper page
- 10.1038/s41467-020-15490-8 · DOI
- 10.1038/s41564-021-00878-z · DOI
- 10.1038/emboj.2012.76 · DOI · Paper page
- 10.1093/molbev/msab120 · DOI · Paper page
- 10.1007/s00239-003-2523-5 · DOI
- 10.1128/mBio.00254-17 · DOI
- 10.1093/bioinformatics/btp033 · DOI
- 10.1073/pnas.2002635118 · DOI
- 10.1016/j.mib.2016.08.008 · DOI
- 10.1126/science.aak9995 · DOI · Paper page
- 10.1006/bbrc.2000.2439 · DOI
- 10.1021/acs.jpcb.2c02810 · DOI
Metadata
- Authors
- Choudhury, J., & Chaudhuri, B. N.
- Affiliations
- Institute of Microbial Technology (IN)
- Corresponding author
- Choudhury, Jagrity
- Venue
- Cytoskeleton
- Publisher
- openRxiv
- Published
- 2024-07-21
- Volume
- 82
- Issue
- 7
- Pages
- 432-443
- ISSN
- 1949-3584 (ISSN-L)
- OpenAlex
- W4405653034
- Cited by
- 3
- References
- 1
- Citations by year
- 2025: 3
- FWCI
- 0.80
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Cytoskeleton (publishedVersion)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
- PubMed (publishedVersion)
- Funders
- Council of Scientific and Industrial Research, India
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Structural Characterization
- Keywords
- SepF, FtsZ, Z-ring assembly, bacterial cell division, divisome, FtsZ polymerization, oligomeric state, Mycobacterium tuberculosis, Staphylococcus aureus, Enterococcus gallinarum
- MeSH terms
- Bacterial Proteins, Cytoskeletal Proteins, Mycobacterium tuberculosis, Staphylococcus aureus
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Tubules, rods and spirals: diverse modes of SepF-FtsZ assembling. https://app.cochat.ai/papers/10.1101/2024.07.18.604210
- The paper
- Choudhury, J., & Chaudhuri, B. N. (2024). Tubules, rods and spirals: diverse modes of SepF-FtsZ assembling. Cytoskeleton. https://doi.org/10.1101/2024.07.18.604210
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.