ReviewSub-cellular biochemistry2026
GARP Complex in Golgi Physiology.
Review in Sub-cellular biochemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
1 citing paper in PubMed.
- Golgi CATCHR complexes function as organizing hubs for vesicle tethering and fusion.bioRxiv : the preprint server for biology · 2026Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
Abstract
The Golgi Associated Retrograde Protein (GARP) complex, a member of the Complexes Associated with Tethering Containing Helical Rods (CATCHR) family, is proposed to tether vesicles arriving from endosomes to the trans-Golgi network (TGN). Discovered nearly 25 years ago, this protein complex is important for sorting vacuolar hydrolases and recycling membrane proteins from the endosomal/prevacuolar compartment to the TGN; however, its exact function, molecular partners, and the nature of GARP-dependent trafficking intermediates remain understudied. GARP-dependent transport route is utilized by various plasma membrane recycling proteins, lysosomal hydrolase receptors, and pathogens, including toxins. Mutations in GARP subunits have been associated with multiple neurological disorders, although the precise mechanisms by which these mutations lead to these conditions remain unclear. This chapter reviews the current understanding of GARP's structure, function, interacting partners, mutations, and associated pathologies in both humans and model organisms.
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Registered trials
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.