Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Amino acid substitutions at proline 220 of beta-tubulin confer resistance to paclitaxel and colcemid.

Molecular cancer therapeutics - 1 Oct 2007

Yin Shanghua, Cabral Fernando, Veeraraghavan Sudha

Abstract excerpt

Chinese hamster ovary cells selected for resistance to paclitaxel have a high incidence of mutations affecting L215, L217, and L228 in the H6/H7 loop region of beta1-tubulin. To determine whether other mutations in this loop are also capable of conferring resistance to drugs that affect microtubule assembly, saturation mutagenesis of the highly conserved P220 codon in beta1-tubulin cDNA was carried out....

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Proline
Share to Cricetulus
Share to Fluorescent Antibody Technique

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Microtubules

Share to Paclitaxel

Share to Tubulin

Share to Tubulin Modulators

Share to Vinblastine

Source

Identifiers

PMID: 17938271
DOI: 10.1158/1535-7163.MCT-06-0791

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Amino acid substitutions at proline 220 of beta-tubulin confer resistance to paclitaxel and colcemid.PMID 17938271Read ↗

Mutations at leucine 215 of beta-tubulin affect paclitaxel sensitivity by two distinct mechanisms.Semantic proximity Read ↗

Mutations in alpha- and beta-tubulin that stabilize microtubules and confer resistance to colcemid and vinblastine.Semantic proximity Read ↗

Human mutations that confer paclitaxel resistance.Semantic proximity Read ↗

Paclitaxel resistance in cells with reduced beta-tubulin.Semantic proximity Read ↗

Cancer cells acquire mitotic drug resistance properties through beta I-tubulin mutations and alterations in the expression of beta-tubulin isotypes.Semantic proximity Read ↗

Paclitaxel-resistant human ovarian cancer cells have mutant beta-tubulins that exhibit impaired paclitaxel-driven polymerization.Semantic proximity Read ↗

Resistance to peloruside A and laulimalide: functional significance of acquired βI-tubulin mutations at sites important for drug-tubulin binding.Semantic proximity Read ↗

Molecular basis for class V beta-tubulin effects on microtubule assembly and paclitaxel resistance.Semantic proximity Read ↗

Enhanced stability of microtubules contributes in the development of colchicine resistance in MCF-7 cells.Semantic proximity Read ↗

Intra-allelic suppression of a mutation that stabilizes microtubules and confers resistance to colcemid.Semantic proximity Read ↗

βII-tubulin and βIII-tubulin mediate sensitivity to peloruside A and laulimalide, but not paclitaxel or vinblastine, in human ovarian carcinoma cells.Semantic proximity Read ↗

Peloruside- and laulimalide-resistant human ovarian carcinoma cells have βI-tubulin mutations and altered expression of βII- and βIII-tubulin isotypes.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.