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

Disruption of Myc-tubulin interaction by hyperphosphorylation of c-Myc during mitosis or by constitutive hyperphosphorylation of mutant c-Myc in Burkitt's lymphoma.

Molecular and cellular biology - 1 Jul 2000

Niklinski J, Claassen G, Meyers C, Gregory M A, Allegra C J, Kaye F J, Hann S R, Zajac-Kaye M

Abstract excerpt

Somatic mutations at Thr-58 of c-Myc have been detected in Burkitt's lymphoma (BL) tumors and have been shown to affect the transforming potential of the Myc oncoprotein. In addition, the N-terminal domain of c-Myc has been shown to interact with microtubules in vivo, and the binding of c-Myc to alpha-tubulin was localized to amino acids 48 to 135 within the c-Myc protein. We demonstrate that c-Myc proteins...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Substitution
Share to Burkitt Lymphoma

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

Share to Microtubules

Share to Mitosis

Share to Peptide Mapping

Share to Phosphoproteins

Share to Proto-Oncogene Proteins c-myc

Share to Tubulin

Source

Open in PubMed Open full text

Identifiers

PMID: 10866684
DOI: 10.1128/MCB.20.14.5276-5284.2000
PMCID: PMC85977

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

Disruption of Myc-tubulin interaction by hyperphosphorylation of c-Myc during mitosis or by constitutive hyperphosphorylation of mutant c-Myc in Burkitt's lymphoma.PMID 10866684Read ↗

c-Myc hot spot mutations in lymphomas result in inefficient ubiquitination and decreased proteasome-mediated turnover.Semantic proximity Read ↗

Mitogen-activated protein/extracellular signal-regulated kinase kinase 1act/tubulin interaction is an important determinant of mitotic stability in cultured HT1080 human fibrosarcoma cells.Semantic proximity Read ↗

c-Myc proteolysis by the ubiquitin-proteasome pathway: stabilization of c-Myc in Burkitt's lymphoma cells.Semantic proximity Read ↗

c-Myc is glycosylated at threonine 58, a known phosphorylation site and a mutational hot spot in lymphomas.Semantic proximity Read ↗

p21-activated kinase 1 regulates microtubule dynamics by phosphorylating tubulin cofactor B.Semantic proximity Read ↗

A link between increased transforming activity of lymphoma-derived MYC mutant alleles, their defective regulation by p107, and altered phosphorylation of the c-Myc transactivation domain.Semantic proximity Read ↗

Characterization of mitosis-specific phosphorylation of tumor-associated microtubule-associated protein.Semantic proximity Read ↗

Ongoing mutations in the N-terminal domain of c-Myc affect transactivation in Burkitt's lymphoma cell lines.Semantic proximity Read ↗

Phosphorylation-dependent binding of a 138-kDa myc intron factor to a regulatory element in the first intron of the c-myc gene.Semantic proximity Read ↗

Cell cycle activation by c-myc in a Burkitt lymphoma model cell lineSemantic proximity Read ↗

Evidence for involvement of calpain in c-Myc proteolysis in vivo.Semantic proximity Read ↗

Wild-type p53 induces apoptosis in a Burkitt lymphoma (BL) line that carries mutant p53.Semantic proximity Read ↗

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