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

Interaction of apoptosis signal-regulating kinase 1 with isoforms of 14-3-3 proteins.

Experimental cell research - 1 Apr 2004

Subramanian Romesh R, Zhang Hongying, Wang Haining, Ichijo Hidenori, Miyashita Toshiyuki, Fu Haian

Abstract excerpt

Apoptosis signal-regulating kinase 1 (ASK1) is a critical mediator of apoptotic signaling pathways initiated by a variety of death stimuli. Its activity is tightly controlled by various mechanisms such as covalent modification and protein-protein interaction. One of the proteins that control ASK1...

Read the complete abstract on PubMed

Topics

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

Share to 14-3-3 Proteins
Share to Cell Compartmentation
Share to COS Cells

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Endoplasmic Reticulum

Share to HeLa Cells

Share to MAP Kinase Kinase Kinases

Share to Protein Isoforms

Share to Tyrosine 3-Monooxygenase

Source

Identifiers

PMID: 15023544
DOI: 10.1016/j.yexcr.2003.12.009

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-15023544-2026-09-04.2. 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 · 12 closest

Interaction of apoptosis signal-regulating kinase 1 with isoforms of 14-3-3 proteins.PMID 15023544Read ↗

Suppression of apoptosis signal-regulating kinase 1-induced cell death by 14-3-3 proteins.Semantic proximity Read ↗

The proapoptotic protein Bad binds the amphipathic groove of 14-3-3zeta.Semantic proximity Read ↗

Role of the 14-3-3 C-terminal loop in ligand interaction.Semantic proximity Read ↗

Structural basis of autoregulatory scaffolding by apoptosis signal-regulating kinase 1.Semantic proximity Read ↗

Functional specificity in 14-3-3 isoform interactions through dimer formation and phosphorylation. Chromosome location of mammalian isoforms and variants.Semantic proximity Read ↗

Structural basis of 14-3-3 protein functions.Semantic proximity Read ↗

Serine 58 of 14-3-3zeta is a molecular switch regulating ASK1 and oxidant stress-induced cell death.Semantic proximity Read ↗

Negative control of apoptosis signal-regulating kinase 1 through phosphorylation of Ser-1034.Semantic proximity Read ↗

Activation of apoptosis signal-regulating kinase 1 (ASK1) by the adapter protein Daxx.Semantic proximity Read ↗

Amyotrophic lateral sclerosis-related mutant superoxide dismutase 1 aggregates inhibit 14-3-3-mediated cell survival by sequestration into the JUNQ compartment.Semantic proximity Read ↗

Isolation of high-affinity peptide antagonists of 14-3-3 proteins by phage display.Semantic proximity Read ↗

Phosphorylation-independent interaction between 14-3-3 and exoenzyme S: from structure to pathogenesis.Semantic proximity Read ↗

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