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

Defective folding of mutant p16(INK4) proteins encoded by tumor-derived alleles.

The Journal of biological chemistry - 15 Nov 1996

Zhang B, Peng Z

Abstract excerpt

p16(INK4) is a specific cyclin D-dependent kinase inhibitor and a multiple tumor suppressor. Inactivation of p16 is frequent in both primary tumors and tumor-derived cell lines. We describe here the conformational properties and oligomerization state of seven mutant p16 proteins; all of them are deficient in function. Four of the seven proteins show significantly disrupted secondary structure and backbone...

Read the complete abstract on PubMed

Topics

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

Share to Alleles
Share to Carrier Proteins
Share to Circular Dichroism

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cyclin-Dependent Kinase Inhibitor p16

Share to Melanoma

Share to Mutagenesis, Site-Directed

Share to Protein Folding

Share to Tumor Cells, Cultured

Source

Identifiers

PMID: 8910511

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.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Defective folding of mutant p16(INK4) proteins encoded by tumor-derived alleles.PMID 8910511Read ↗

Stability and folding of the tumour suppressor protein p16.Semantic proximity Read ↗

Structural consequences of tumor-derived mutations in p16INK4a probed by limited proteolysis.Semantic proximity Read ↗

Sequential unfolding of ankyrin repeats in tumor suppressor p16.Semantic proximity Read ↗

Amyloid formation and depolymerization of tumor suppressor p16INK4a are regulated by a thiol-dependent redox mechanism.Semantic proximity Read ↗

Aberrant protein folding as the molecular basis of cancer.Semantic proximity Read ↗

A rare germline CDKN2A variant (47T>G; p16-L16R) predisposes carriers to pancreatic cancer by reducing cell cycle inhibition.Semantic proximity Read ↗

Regulatory mechanisms of tumor suppressor P16(INK4A) and their relevance to cancer.Semantic proximity Read ↗

Functional impairment of melanoma-associated p16(INK4a) mutants in melanoma cells despite retention of cyclin-dependent kinase 4 binding.Semantic proximity Read ↗

Regulation of Tumor Suppressor Gene CDKN2A and Encoded p16-INK4a Protein by Covalent ModificationsSemantic proximity Read ↗

Functional evaluation of tumour-specific variants of p16INK4a/CDKN2A: correlation with protein structure information.Semantic proximity Read ↗

Temperature-sensitive mutants of p16CDKN2 associated with familial melanoma.Semantic proximity Read ↗

Dissection of protein-protein interaction and CDK4 inhibition in the oncogenic versus tumor suppressing functions of gankyrin and P16.Semantic proximity Read ↗

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