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

Abolishing the prelamin A ZMPSTE24 cleavage site leads to progeroid phenotypes with near-normal longevity in mice.

Proceedings of the National Academy of Sciences of the United States of America - 1 Mar 2022

Wang Yuexia, Shilagardi Khurts, Hsu Trunee, Odinammadu Kamsi O, Maruyama Takamitsu, Wu Wei, Lin Chyuan-Sheng, Damoci Christopher B, Spear Eric D, Shin Ji-Yeon, Hsu Wei, Michaelis Susan, Worman Howard J

Abstract excerpt

Prelamin A is a farnesylated precursor of lamin A, a nuclear lamina protein. Accumulation of the farnesylated prelamin A variant progerin, with an internal deletion including its processing site, causes Hutchinson-Gilford progeria syndrome. Loss-of-function mutations in ZMPSTE24, which encodes the prelamin A processing enzyme, lead to accumulation of full-length farnesylated prelamin A and cause related progeroid...

Read the complete abstract on PubMed

Topics

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

Share to Binding Sites
Share to Lamin Type A

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Longevity

Share to Membrane Proteins

Share to Metalloendopeptidases

Share to Phenotype

Share to Progeria

Source

Open in PubMed Open full text

Identifiers

PMID: 35197292
DOI: 10.1073/pnas.2118695119
PMCID: PMC8892526

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

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

Abolishing the prelamin A ZMPSTE24 cleavage site leads to progeroid phenotypes with near-normal longevity in mice.PMID 35197292Read ↗

Abolishing the prelamin A ZMPSTE24 cleavage site leads to progeroid phenotypes with near-normal longevity in miceSemantic proximity Read ↗

Heterozygosity for Lmna deficiency eliminates the progeria-like phenotypes in Zmpste24-deficient mice.Semantic proximity Read ↗

A mutation abolishing the ZMPSTE24 cleavage site in prelamin A causes a progeroid disorder.Semantic proximity Read ↗

Hutchinson-Gilford progeria syndrome.Semantic proximity Read ↗

The Accumulation of Progerin Underlies the Loss of Aortic Smooth Muscle Cells in Hutchinson-Gilford Progeria SyndromeSemantic proximity Read ↗

Targeting RAS-converting enzyme 1 overcomes senescence and improves progeria-like phenotypes of ZMPSTE24 deficiency.Semantic proximity Read ↗

Requirements for efficient proteolytic cleavage of prelamin A by ZMPSTE24.Semantic proximity Read ↗

Premature aging syndromes: From patients to mechanism.Semantic proximity Read ↗

Compound heterozygous ZMPSTE24 mutations reduce prelamin A processing and result in a severe progeroid phenotype.Semantic proximity Read ↗

Hutchinson-Gilford Progeria Syndrome: A premature aging disease caused by LMNA gene mutations.Semantic proximity Read ↗

A homozygous ZMPSTE24 null mutation in combination with a heterozygous mutation in the LMNA gene causes Hutchinson-Gilford progeria syndrome (HGPS): insights into the pathophysiology of HGPS.Semantic proximity Read ↗

Prelamin A causes progeria through cell-extrinsic mechanisms and prevents cancer invasion.Semantic proximity Read ↗

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