ArticleJournal of protein chemistry1999
Structure-function analysis of the ADAM family of disintegrin-like and metalloproteinase-containing proteins (review).
Article in Journal of protein chemistry, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 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
40 citing papers in PubMed, 153 citations in OpenAlex.
- The ADAM Family of Proteases: Structure, Substrates, and Roles in Liver Diseases.International journal of molecular sciences · 2026Review
- A Valuable Target for Therapy: The Metalloproteinase ADAM10.Current protein & peptide science · 2025Review
- Snake venom disintegrins update: insights about new findings.The journal of venomous animals and toxins including tropical diseases · 2023Review
- The versatile roles of ADAM8 in cancer cell migration, mechanics, and extracellular matrix remodeling.Frontiers in cell and developmental biology · 2023Review
- ADAM and ADAMTS disintegrin and metalloproteinases as major factors and molecular targets in vascular malfunction and disease.Advances in pharmacology (San Diego, Calif.) · 2022Article
- Structure, regulatory factors and cancer-related physiological effects of ADAM9.Cell adhesion & migration · 2020Review
- Joint Entropy-Assisted Graphene Oxide-Based Multiplexing Biosensing Platform for Simultaneous Detection of Multiple Proteases.Analytical chemistry · 2020Article
- Developments in Carbohydrate-Based Metzincin Inhibitors.Pharmaceuticals (Basel, Switzerland) · 2020Review
- Genes and Pathways Regulating Decline in Lung Function and Airway Remodeling in Asthma.Allergy, asthma & immunology research · 2019Review
- Functions of 'A disintegrin and metalloproteases (ADAMs)' in the mammalian nervous system.Cellular and molecular life sciences : CMLS · 2019Review
- A Disintegrin and Metalloproteinase (ADAM) and ADAM with thrombospondin motifs (ADAMTS) family in vascular biology and disease.Biochemical pharmacology · 2019Review
- Article
- Review
- miR-720 is a downstream target of an ADAM8-induced ERK signaling cascade that promotes the migratory and invasive phenotype of triple-negative breast cancer cells.Breast cancer research : BCR · 2016Article
- The evolutionary conservation of the A Disintegrin-like and Metalloproteinase domain with Thrombospondin-1 motif metzincins across vertebrate species and their expression in teleost zebrafish.BMC evolutionary biology · 2015Article
- Recombinant disintegrin domain of human ADAM9 inhibits migration and invasion of DU145 prostate tumor cells.Cell adhesion & migration · 2015Article
- ADAM metallopeptidase domain 33 (ADAM33): a promising target for asthma.Mediators of inflammation · 2014Review
- Association of ADAM33 gene polymorphisms with asthma in the Uygur population of China.Biomedical reports · 2013Article
- Role of ADAM33 gene and associated single nucleotide polymorphisms in asthma.Allergy & rhinology (Providence, R.I.) · 2011Article
- Expression profile of microRNAs and mRNAs in human placentas from pregnancies complicated by preeclampsia and preterm labor.Reproductive sciences (Thousand Oaks, Calif.) · 2011Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
The ADAMs belong to a disintegrin-like and metalloproteinase-containing protein family that are zinc-dependent metalloproteinases. These proteins share all or some of the following domain structure: a signal peptide, a propeptide, a metalloproteinase, a disintegrin, a cysteine-rich, and an epidermal growth factor (EGF)-like domains, a transmembrane region, and a cytoplasmic tail. ADAMs are widely distributed in many organs, tissues, and cells, such as brain, testis, epididymis, ovary, breast, placenta, liver, heart, lung, bone, and muscle. These proteins are capable of four potential functions: proteolysis, adhesion, fusion, and intracellular signaling. Because the number of ADAM genes has grown rapidly and the biological functions of most members are unclear, this review analyzes the protein structures and functions, their activation and processing, their known and potential activities, and their evolutionary relationships. A sequence alignment of human ADAMs is compiled and their homology and physical data are calculated. The conceivable functions of ADAMs in reproduction, development, and diseases are also discussed.
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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.