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

Positive and negative control of multidrug resistance by the Sit4 protein phosphatase in Kluyveromyces lactis.

The Journal of biological chemistry - 19 May 2000

Chen X J, Bauer B E, Kuchler K, Clark-Walker G D

Abstract excerpt

The nuclear gene encoding the Sit4 protein phosphatase was identified in the budding yeast Kluyveromyces lactis. K. lactis cells carrying a disrupted sit4 allele are resistant to oligomycin, antimycin, ketoconazole, and econazole but hypersensitive to paromomycin, sorbic acid, and 4-nitroquinoline-N-oxide (4-NQO). Overexpression of SIT4 leads to an elevation in resistance to paromomycin and to lesser extent...

Read the complete abstract on PubMed

Topics

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

Share to 4-Nitroquinoline-1-oxide
Share to Antifungal Agents

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

Share to Antimycin A

Share to Drug Resistance, Multiple

Share to Kluyveromyces

Share to Phosphoprotein Phosphatases

Share to Protein Phosphatase 2

Share to Tacrolimus

Source

Identifiers

PMID: 10809730
DOI: 10.1074/jbc.275.20.14865

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

Positive and negative control of multidrug resistance by the Sit4 protein phosphatase in Kluyveromyces lactis.PMID 10809730Read ↗

Activity of the Kluyveromyces lactis Pdr5 multidrug transporter is modulated by the Sit4 protein phosphatase.Semantic proximity Read ↗

KNQ1, a Kluyveromyces lactis gene encoding a drug efflux permease.Semantic proximity Read ↗

KTI11 and KTI13, Saccharomyces cerevisiae genes controlling sensitivity to G1 arrest induced by Kluyveromyces lactis zymocin.Semantic proximity Read ↗

Sit4p protein phosphatase is required for sensitivity of Saccharomyces cerevisiae to Kluyveromyces lactis zymocin.Semantic proximity Read ↗

Active efflux by multidrug transporters as one of the strategies to evade chemotherapy and novel practical implications of yeast pleiotropic drug resistance.Semantic proximity Read ↗

Transcriptional control of multidrug resistance in the yeast Saccharomyces.Semantic proximity Read ↗

Sit4 phosphatase is functionally linked to the ubiquitin-proteasome system.Semantic proximity Read ↗

Retrograde regulation of multidrug resistance in Saccharomyces cerevisiae.Semantic proximity Read ↗

The yeast SR protein kinase Sky1p modulates salt tolerance, membrane potential and the Trk1,2 potassium transporter.Semantic proximity Read ↗

Unique SNPs in the promoter of the peptide transporter gene PTR2 increase its expression in the Saccharomyces cerevisiae sake strain.Semantic proximity Read ↗

Glutathione S-transferase ϴ-subunit as a phenotypic suppressor of pmr1Δ strain, the Kluyveromyces lactis model for Hailey-Hailey disease.Semantic proximity Read ↗

TOR-induced resistance to toxic adenosine analogs in Leishmania brought about by the internalization and degradation of the adenosine permease.Semantic proximity Read ↗

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