ReviewOpen biology2018
Sequence analysis and structure prediction of ABHD16A and the roles of the ABHD family members in human disease.
Review in Open biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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
28 citing papers in PubMed.
- Emerging roles of α/β hydrolase domain (ABHD) proteins in S-palmitoylation modification: molecular mechanisms, structural features, and pathological implications.Cellular & molecular biology letters · 2026Review
- The Phospholipase AJournal of lipid and atherosclerosis · 2026Review
- Proteomic signatures in cerebrospinal fluid and their clinical associations in patients with ME/CFS.Scientific reports · 2026Article
- Effect ofJournal of thoracic disease · 2026Article
- Case Report: Post-mortem analysis of long-term inflammation after mild COVID-19.Frontiers in immunology · 2026Article
- Recent advances in S-palmitoylation and its emerging roles in human diseases.Journal of hematology & oncology · 2025Review
- The Unconventional Role of ABHD17A in Increasing the S-Palmitoylation and Antiviral Activity of IFITM1 by Downregulating ABHD16A.Biomolecules · 2025Article
- Depalmitoylase ABHD16A negatively regulates the anti-hepatitis B virus activity of IFITM1.Microbiology spectrum · 2025Article
- An S-acylated N-terminus and a conserved loop regulate the activity of the ABHD17 deacylase.The Journal of cell biology · 2025Article
- Swine RNF5 positively regulates the antiviral activity of IFITM1 by mediating the degradation of ABHD16A.Journal of virology · 2025Article
- Expansion of the genetic and phenotypic spectrum of hereditary spastic paraplegia caused byFrontiers in pediatrics · 2025Article
- Pooled PPIseq: Screening the SARS-CoV-2 and human interface with a scalable multiplexed protein-protein interaction assay platform.PloS one · 2025Article
- Mechanisms and functions of protein S-acylation.Nature reviews. Molecular cell biology · 2024Review
- ABHD5 as a friend or an enemy in cancer biology?Frontiers in oncology · 2024Review
- ABHD12 contributes to tumorigenesis and sorafenib resistance by preventing ferroptosis in hepatocellular carcinoma.iScience · 2023Article
- Integrating eQTL and GWAS data characterises established and identifies novel migraine risk loci.Human genetics · 2023Article
- A genome-wide cross-cancer meta-analysis highlights the shared genetic links of five solid cancers.Frontiers in microbiology · 2023Article
- Lost in traffic: consequences of altered palmitoylation in neurodegeneration.Frontiers in physiology · 2023Review
- ABHD16A Negatively Regulates the Palmitoylation and Antiviral Function of IFITM Proteins.mBio · 2022Article
- An ER phospholipid hydrolase drives ER-associated mitochondrial constriction for fission and fusion.eLife · 2022Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Abhydrolase domain containing 16A (ABHD16A) is a member of the α/β hydrolase domain-containing (ABHD) protein family and is expressed in a variety of animal cells. Studies have shown that ABHD16A has acylglycerol lipase and phosphatidylserine lipase activities. Its gene location in the main histocompatibility complex (MHC) III gene cluster suggests that this protein may participate in the immunomodulation of the body. The results of studies investigating nearly 20 species of ABHDs reveal that the ABHD proteins are key factors in metabolic regulation and disease occurrence and development. In this paper, we summarize the related progress regarding the function of ABHD16A and other ABHD proteins. A prediction of the active sites and structural domains of ABHD16A and an analysis of the amino acid sites are included. Moreover, we analysed the amino acid sequences of the ABHD16A molecules in different species and provide an overview of the related functions and diseases associated with these proteins. The functions and diseases related to ABHD are systematically summarized and highlighted. Future research directions for studies investigating the functions and mechanisms of these proteins are also suggested. Further studies investigating the function of ABHD proteins may further confirm their positions as important determinants of lipid metabolism and related diseases.
Indexed as
Identifiers
What OpenQuestion holds
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.