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

Dissecting protein function: an efficient protocol for identifying separation-of-function mutations that encode structurally stable proteins.

Genetics - 1 Mar 2013

Lubin Johnathan W, Rao Timsi, Mandell Edward K, Wuttke Deborah S, Lundblad Victoria

Abstract excerpt

Mutations that confer the loss of a single biochemical property (separation-of-function mutations) can often uncover a previously unknown role for a protein in a particular biological process. However, most mutations are identified based on loss-of-function phenotypes, which cannot differentiate...

Read the complete abstract on PubMed

Topics

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

Share to Circular Dichroism
Share to Conserved Sequence
Share to Protein Stability

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Protein Structure, Secondary

Share to Protein Subunits

Share to Saccharomyces cerevisiae Proteins

Share to Static Electricity

Share to Telomerase

Source

Open in PubMed Open full text

Identifiers

PMID: 23307900
DOI: 10.1534/genetics.112.147801
PMCID: PMC3583993

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-23307900-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 10 closest

Dissecting protein function: an efficient protocol for identifying separation-of-function mutations that encode structurally stable proteins.PMID 23307900Read ↗

Using Separation-of-Function Mutagenesis To Define the Full Spectrum of Activities Performed by the Est1 Telomerase Subunit in Vivo.Semantic proximity Read ↗

Using two-hybrid interactions to identify separation-of-function mutations.Semantic proximity Read ↗

Reverse two-hybrid and one-hybrid systems to detect dissociation of protein-protein and DNA-protein interactions.Semantic proximity Read ↗

Essential functions of amino-terminal domains in the yeast telomerase catalytic subunit revealed by selection for viable mutants.Semantic proximity Read ↗

The canonical RPA complex interacts with Est3 to regulate yeast telomerase activitySemantic proximity Read ↗

Stimulation of yeast telomerase activity by the ever shorter telomere 3 (Est3) subunit is dependent on direct interaction with the catalytic protein Est2.Semantic proximity Read ↗

Alleviation of deleterious effects of protein mutation through inactivation of molecular chaperones.Semantic proximity Read ↗

A proposed OB-fold with a protein-interaction surface in Candida albicans telomerase protein Est3.Semantic proximity Read ↗

Senescence mutants of Saccharomyces cerevisiae with a defect in telomere replication identify three additional EST genes.Semantic proximity Read ↗

Saccharomyces cerevisiae Est3p dimerizes in vitro and dimerization contributes to efficient telomere replication in vivo.Semantic proximity Read ↗

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