ReviewJMA journal2026
Integrated Studies on the Biological Functions and Regulatory Mechanisms of Dedicator of Cytokinesis Family Proteins-Secondary Publication.
Review in JMA journal, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
0 citing papers in PubMed.
No citing paper in PubMed yet.
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Authors and funding
1 author.
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Abstract
Small guanosine triphosphatases act as molecular switches in signaling pathways by alternating between an inactive guanosine diphosphate (GDP)-bound state and an active guanosine triphosphate (GTP)-bound state. Upon activation, they interact with various effector molecules to regulate a wide range of cellular processes. This activation is triggered by external stimuli and is mediated by guanine nucleotide exchange factors (GEFs). GEFs are classified into two major types: Dbl homology (DH)-domain-containing proteins (DH-type GEFs) and dedicator of cytokinesis (DOCK) proteins (DOCK-type GEFs). Traditionally, DH-type GEFs were thought to represent the universal GEFs in eukaryotic systems. However, since we first demonstrated the crucial role of DOCK2 in lymphocyte migration, accumulating evidence has highlighted the importance of DOCK family proteins in diverse biological responses. These proteins share two evolutionarily conserved domains: DOCK homology region-1 (DHR-1) and DHR-2. The DHR-1 domain mediates phospholipid binding, which governs the intracellular localization of DOCK proteins, whereas the DHR-2 domain functions as the catalytic site for GDP-GTP exchange reaction on Rac or Cdc42. In mammals, the DOCK family comprises 11 members. In this review, I summarize the biological functions and regulatory mechanisms of DOCK proteins, with a particular emphasis on DOCK2 and DOCK8.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.