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måndag 28 juli 2025

Olennainen uusi tieto ADAM-perheenjäsenistä terapioiden kannalta . (A Disintegrin And Metalloproteinase = ADAM)

 https://pubmed.ncbi.nlm.nih.gov/?term=ADAM-members&sort=date

10 results

ADAMs contribute to triple negative breast cancer via mTORC1 pathway: targeting ADAM-mTOR axis improves efficacy.
Liu S, Chen H, Gagea M, Federico L, Zhang F, Gomez J, Do KA, Symmans WF, Hortobagyi GN, Mills GB, Gonzalez-Angulo AM, Tripathy D. Cancer Lett. 2025 Aug 28;626:217775. doi: 10.1016/j.canlet.2025.217775. Epub 2025 May 6. PMID: 40339955 Free article.
The A Disintegrin and Metalloproteinase (ADAM) family plays a vital role in cancer pathophysiology. Previous studies focused on single ADAM members. However, none of these have entered into the clinical arena as diagnostics or therapeutics for breast cancer. In this …
Prior authorizations in dermatology and impact on patient care: An updated survey of US dermatology providers and staff by the American Academy of Dermatology.
Petitt CE, Kiracofe E, Adamson A, Barbieri JS. Dermatol Online J. 2021 Jan 15;27(1):13030/qt990631n9. PMID: 33560787 Free article.
-based dermatologists (N=3,000) and the Association of Dermatology Administrators/Managers (ADAM) members (N=718). RESULTS: Respondents reported 24% of patients require PAs. Dermatologists and staff spend a mean of 3.3 hours/day on PAs. ...
Molecular design and structural optimization of potent peptide hydroxamate inhibitors to selectively target human ADAM metallopeptidase domain 17.
Wang Z, Wang L, Fan R, Zhou J, Zhong J. Comput Biol Chem. 2016 Apr;61:15-22. doi: 10.1016/j.compbiolchem.2015.12.003. Epub 2015 Dec 8. PMID: 26709988
The ADAM metallopeptidase domain 17 (ADAM17 or TACE) and its close relative ADAM10 are two of the most important ADAM members that share high conservation in sequence, structure and function, but exhibit subtle difference in regulation of downstream cell signaling e …
Retinoids induce integrin-independent lymphocyte adhesion through RAR-α nuclear receptor activity.
Whelan JT, Wang L, Chen J, Metts ME, Nasser TA, McGoldrick LJ, Bridges LC. Biochem Biophys Res Commun. 2014 Nov 28;454(4):537-42. doi: 10.1016/j.bbrc.2014.10.120. Epub 2014 Oct 31. PMID: 25450689
Interestingly, adhesion occurs independent of integrin function, and mutant studies demonstrate that atRA-induced adhesion to ADAM members required a distinct binding interface(s) as compared to integrin recognition. ...
Structure of human ADAM-8 catalytic domain complexed with batimastat.
Hall T, Shieh HS, Day JE, Caspers N, Chrencik JE, Williams JM, Pegg LE, Pauley AM, Moon AF, Krahn JM, Fischer DH, Kiefer JR, Tomasselli AG, Zack MD. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Jun 1;68(Pt 6):616-21. doi: 10.1107/S1744309112015618. Epub 2012 May 22. PMID: 22684055 Free PMC article.
ADAM-8 has an overall fold similar to those of other ADAM members, including a central five-stranded beta-sheet and a catalytic Zn(2+) ion. ...
TGFβ induces proHB-EGF shedding and EGFR transactivation through ADAM activation in gastric cancer cells.
Ebi M, Kataoka H, Shimura T, Kubota E, Hirata Y, Mizushima T, Mizoshita T, Tanaka M, Mabuchi M, Tsukamoto H, Tanida S, Kamiya T, Higashiyama S, Joh T. Biochem Biophys Res Commun. 2010 Nov 19;402(3):449-54. doi: 10.1016/j.bbrc.2010.09.130. Epub 2010 Oct 8. PMID: 20934403
Membrane-anchored heparin-binding EGF-like growth factor (proHB-EGF) ectodomain is cleaved by a disintegrin and metalloproteinase (ADAM) members and is implicated in epidermal growth factor receptor (EGFR) transactivation. ...
ADAM gene expression and regulation during human osteoclast formation.
Verrier S, Hogan A, McKie N, Horton M. Bone. 2004 Jul;35(1):34-46. doi: 10.1016/j.bone.2003.12.029. PMID: 15207739
In this study, we identified the expression and the regulation of ADAM members (a disintegrin and metalloprotease) at both gene and protein levels during human osteoclast differentiation and activity. ...
ADAMs, a disintegrin and metalloproteinases, mediate shedding of oxytocinase.
Ito N, Nomura S, Iwase A, Ito T, Kikkawa F, Tsujimoto M, Ishiura S, Mizutani S. Biochem Biophys Res Commun. 2004 Feb 20;314(4):1008-13. doi: 10.1016/j.bbrc.2003.12.183. PMID: 14751233
Immunohistochemical analysis in human placenta demonstrated strong expression of ADAM12 in syncytiotrophoblasts, while little expression of ADAM9 was detected throughout the placenta. Our results suggest ADAM members, at least including ADAM12, are involved in P-LAP …

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