The DOI matches its Crossref record.
Tubulysins, New Cytostatic Peptides from Myxobacteria Acting on Microtubuli. Production, Isolation, Physico-chemical and Biological Properties.
Open accessAbstract
New cytostatic compounds, tubulysins, were isolated from the culture broth of strains of the myxobacteria Archangium gephyra and Angiococcus disciformis. The compounds are peptides partly consisting of unusual amino acids and are distantly related to the dolastatins. The tubulysins were not active against bacteria and only little against fungi, but showed high cytostatic activity against mammalian cell lines with IC50 values in the picomolar range. An incubation with 50 ng/ml tubulysin A led to a complete disappearance of the microtubuli network of the cells within 24 hours. The more active tubulysin D induced multipolar spindles: At 0.5 ng/ml all mitotic cells showed more than four spindle poles.
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
Cited by
Recent applications of multicomponent reactions in medicinal chemistry
Slobbe, P., Ruijter, E., & Orru, R. V. A. (2012) · MedChemComm · doi:10.1039/c2md20089a · Cited by 484
Tan, M. L., Choong, P. F. M., & Dass, C. R. (2010) · Peptides · doi:10.1016/j.peptides.2009.10.002 · Cited by 350
Myxobacterial secondary metabolites: bioactivities and modes-of-action
Weissman, K. J., & Müller, R. (2010) · Natural Product Reports · doi:10.1039/c001260m · Cited by 310
Metadata
- Authors
- SASSE, F., SIEINMETZ, H., HEIL, J., HÖFLE, G., & REICHENBACH, H.
- Venue
- The Journal of Antibiotics
- Published
- 2000
- Volume
- 53
- Issue
- 9
- Pages
- 879-885
- ISSN
- 0021-8820 (ISSN-L)
- 1881-1469
- OpenAlex
- W1985072203
- Cited by
- 257
- References
- 0
- FWCI
- 2.27
- Type
- journal article
- Language
- en
- Open access
- bronze
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: Tubulysins, New Cytostatic Peptides from Myxobacteria Acting on Microtubuli. Production, Isolation, Physico-chemical and Biological Properties. https://app.cochat.ai/papers/10.7164/antibiotics.53.879
- The paper
- SASSE, F., SIEINMETZ, H., HEIL, J., HÖFLE, G., & REICHENBACH, H. (2000). Tubulysins, New Cytostatic Peptides from Myxobacteria Acting on Microtubuli. Production, Isolation, Physico-chemical and Biological Properties. The Journal of Antibiotics. https://doi.org/10.7164/antibiotics.53.879
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.