ADAM, a novel family of membrane proteins containing A Disintegrin And Metalloprotease domain: multipotential functions in cell-cell and cell-matrix interactions.
Open accessAbstract
ELL--cell and cell-matrix adhesion, as well as proteolysis of the extracellular matrix, are vital for normal processes such as tissue morphogenesis and wound healing, as well as for pathologies such as tumor cell invasion and metastasis. A variety of cell surface adhesion proteins and proteases are important players in these events. Families of membrane-anchored cell surface adhesion molecules include cadherins, immunoglobulin superfamily members, selectins, integrins, and syndecans (7). Membrane-anchored cell surface proteases include membrane-type matrix metalloprotease (4) and meprin (9). In this review we describe the ADAMs, a recently discovered gene family encoding membrane proteins with A Disintegrin And Metalloprotease domain. ADAMs 1 are unique among cell surface proteins in possessing both a
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Benchmark tests on GPCR sequences with determined structures showed that RoseTTAFold models for both active and inactive states can be quite accurate even in the absence of close homologs with known structures, and better than those in current GPCR model databases.
“Benchmark tests on GPCR sequences with determined structures showed that RoseTTAFold models for both active and inactive states can be quite accurate even in the absence of close homologs with known structures (and better than those in current GPCR model databases (14, 15); fig. S7)”
From Accurate prediction of protein structures and interactions using a 3-track network (2021) · cites this paper as [15]
The cited paper’s Conclusions (p. 277) discuss the ADAM protein family and its possible functions. Searches of our copy for RoseTTAFold, GPCR structural models, and model databases found no passage addressing the benchmark or comparison claimed here. (LLM, conf=0.78)
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- Authors
- Wolfsberg, T. G., Primakoff, P., Myles, D. G., & White, J. M.
- Affiliations
- University of California, San Francisco (US)
- Venue
- The Journal of cell biology
- Publisher
- Rockefeller University Press
- Published
- 1995-10-15
- Volume
- 131
- Issue
- 2
- Pages
- 275-278
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- PMC
- PMC2199973
- OpenAlex
- W1989228411
- Cited by
- 502
- References
- 21
- Citations by year
- 2026: 1 · 2025: 6 · 2024: 6 · 2023: 5 · 2022: 5 · 2021: 4 · 2020: 9 · 2019: 6 · 2018: 9 · 2017: 12 · 2016: 4 · 2015: 11 · 2014: 15 · 2013: 9 · 2012: 17
- FWCI
- 9.76
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- cc-by-nc-sa
- Locations
- The Journal of Cell Biology (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion, cc-by-nc-sa)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
- Health Sciences › Medicine › Hematology › Blood Coagulation and Thrombosis Mechanisms
- Keywords
- ADAM family, membrane proteins, cell-cell interactions, cell-matrix interactions, ADAMTS, ADAM12, ADAM17, ADAM19, ADAM22, ADAM23, ADAM28, ADAM33, Adam
- MeSH terms
- Fertilins, Amino Acid Sequence, Animals, Antigens, Surface, Binding Sites, Cell Communication, Extracellular Matrix, Humans, Membrane Glycoproteins, Membrane Proteins, Metalloendopeptidases, Molecular Sequence Data, Peptides, Antigens, CD, Sequence Alignment, Disintegrins, ADAM Proteins
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