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Items: 1 to 20 of 34

1.
Loss of ADAM9 Leads to Modifications of the Extracellular Matrix Modulating Tumor Growth
Anna N. Abety, Elke Pach, Nives Giebeler, Julia E. Fromme, Lavakumar Reddy Aramadhaka, Cornelia Mauch, Jay W. Fox, Paola Zigrino
Biomolecules. 2020 Sep; 10(9): 1290. Published online 2020 Sep 7. doi: 10.3390/biom10091290
PMCID:
PMC7564588
ArticlePDF–1.7M
2.
Mice Lacking the Metalloprotease-Disintegrin MDC9 (ADAM9) Have No Evident Major Abnormalities during Development or Adult Life
Gisela Weskamp, Hui Cai, Thomas A. Brodie, Shigeki Higashyama, Katia Manova, Thomas Ludwig, Carl P. Blobel
Mol Cell Biol. 2002 Mar; 22(5): 1537–1544. doi: 10.1128/mcb.22.5.1537-1544.2002
PMCID:
PMC134708
ArticlePDF–759K
3.
ADAM9 is present at endothelial cell - cell junctions and regulates monocyte – endothelial transmigration
William R. English, Richard J. Siviter, Martin Hansen, Gillian Murphy
Biochem Biophys Res Commun. 2017 Nov 18; 493(2): 1057–1062. doi: 10.1016/j.bbrc.2017.09.089
PMCID:
PMC5643258
ArticlePDF–1.2M
4.
ADAM9 is a Novel Product of Polymorphonuclear Neutrophils: Regulation of Expression and Contributions to Extracellular Matrix Protein Degradation During Acute Lung Injury
Robin Roychaudhuri, Anja H. Hergrueter, Francesca Polverino, Maria E. Laucho-Contreras, Kushagra Gupta, Niels Borregaard, Caroline A. Owen
J Immunol. Author manuscript; available in PMC 2015 Sep 1.
Published in final edited form as: J Immunol. 2014 Sep 1; 193(5): 2469–2482. Published online 2014 Jul 25. doi: 10.4049/jimmunol.1303370
PMCID:
PMC4134955
ArticlePDF–1.7M
5.
A Murine Model for Retinopathy of Prematurity Identifies Endothelial Cell Proliferation as a Potential Mechanism for Plus Disease
Victor H. Guaiquil, Nina J. Hewing, Michael F. Chiang, Mark I. Rosenblatt, R. V. Paul Chan, Carl P. Blobel
Invest Ophthalmol Vis Sci. 2013 Aug; 54(8): 5294–5302. Published online 2013 Aug 7. doi: 10.1167/iovs.12-11492
PMCID:
PMC3738219
ArticlePDF–1.5M
6.
The Disintegrin-like and Cysteine-rich domains of ADAM-9 Mediate Interactions between Melanoma Cells and Fibroblasts
Paola Zigrino, Roswitha Nischt, Cornelia Mauch
J Biol Chem. 2011 Feb 25; 286(8): 6801–6807. Published online 2010 Dec 6. doi: 10.1074/jbc.M110.168617
PMCID:
PMC3057808
ArticlePDF–813K
7.
ADAM9 Is Involved in Pathological Retinal Neovascularization
Victor Guaiquil, Steven Swendeman, Tsunehiko Yoshida, Sai Chavala, Peter A. Campochiaro, Carl P. Blobel
Mol Cell Biol. 2009 May; 29(10): 2694–2703. Published online 2009 Mar 9. doi: 10.1128/MCB.01460-08
PMCID:
PMC2682031
ArticlePDF–1.2M
8.
Loss of the Metalloprotease ADAM9 Leads to Cone-Rod Dystrophy in Humans and Retinal Degeneration in Mice
David A. Parry, Carmel Toomes, Lina Bida, Michael Danciger, Katherine V. Towns, Martin McKibbin, Samuel G. Jacobson, Clare V. Logan, Manir Ali, Jacquelyn Bond, Rebecca Chance, Steven Swendeman, Lauren L. Daniele, Kelly Springell, Matthew Adams, Colin A. Johnson, Adam P. Booth, Hussain Jafri, Yasmin Rashid, Eyal Banin, Tim M. Strom, Debora B. Farber, Dror Sharon, Carl P. Blobel, Edward N. Pugh, Jr., Eric A. Pierce, Chris F. Inglehearn
Am J Hum Genet. 2009 May 15; 84(5): 683–691. doi: 10.1016/j.ajhg.2009.04.005
PMCID:
PMC2681008
ArticlePDF–1.2M
9.
FMRP Regulates the Nuclear Export of Adam9 and Psen1 mRNAs: Secondary Analysis of an N6-Methyladenosine Dataset
Cara J. Westmark, Bryan Maloney, Reid S. Alisch, Deborah K. Sokol, Debomoy K. Lahiri
Sci Rep. 2020; 10: 10781. Published online 2020 Jul 1. doi: 10.1038/s41598-020-66394-y
PMCID:
PMC7329887
ArticlePDF–3.7M
10.
The Functional Maturation of A Disintegrin and Metalloproteinase (ADAM) 9, 10, and 17 Requires Processing at a Newly Identified Proprotein Convertase (PC) Cleavage Site
Eitan Wong, Thorsten Maretzky, Yoav Peleg, Carl P. Blobel, Irit Sagi
J Biol Chem. 2015 May 8; 290(19): 12135–12146. Published online 2015 Mar 20. doi: 10.1074/jbc.M114.624072
PMCID:
PMC4424348
ArticlePDF–1.5M
11.
PROTEOLYTIC PROCESSING OF DELTA-LIKE 1 BY ADAM PROTEASES
Emilia Dyczynska, Danqiong Sun, Haiqing Yi, Atsuko Sehara-Fujisawa, Carl P. Blobel, Anna Zolkiewska
J Biol Chem. Author manuscript; available in PMC 2009 Jun 8.
Published in final edited form as: J Biol Chem. 2007 Jan 5; 282(1): 436–444. Published online 2006 Nov 15. doi: 10.1074/jbc.M605451200
PMCID:
PMC2692894
ArticlePDF–1.6M
12.
ADAM10, the Rate-limiting Protease of Regulated Intramembrane Proteolysis of Notch and Other Proteins, Is Processed by ADAMS-9, ADAMS-15, and the γ-Secretase
Thomas Tousseyn, Amantha Thathiah, Ellen Jorissen, Tim Raemaekers, Uwe Konietzko, Karina Reiss, Elke Maes, An Snellinx, Lutgarde Serneels, Omar Nyabi, Wim Annaert, Paul Saftig, Dieter Hartmann, Bart De Strooper
J Biol Chem. 2009 Apr 24; 284(17): 11738–11747. doi: 10.1074/jbc.M805894200
PMCID:
PMC2670177
ArticlePDF–683K
13.
MDC9, a widely expressed cellular disintegrin containing cytoplasmic SH3 ligand domains
J Cell Biol. 1996 Feb 2; 132(4): 717–726. doi: 10.1083/jcb.132.4.717
PMCID:
PMC2199860
SummaryPDF–1.9M
14.
Distinct roles for ADAM10 and ADAM17 in ectodomain shedding of six EGFR ligands
Umut Sahin, Gisela Weskamp, Kristine Kelly, Hong-Ming Zhou, Shigeki Higashiyama, Jacques Peschon, Dieter Hartmann, Paul Saftig, Carl P. Blobel
J Cell Biol. 2004 Mar 1; 164(5): 769–779. doi: 10.1083/jcb.200307137
PMCID:
PMC2172154
ArticlePDF–3.7M
15.
ADAM9 enhances Th17 cell differentiation and autoimmunity by activating TGF-β1
Masataka Umeda, Nobuya Yoshida, Ryo Hisada, Catalina Burbano, Seo Yeon K. Orite, Michihito Kono, Vasileios C. Kyttaris, Suzanne Krishfield, Caroline A. Owen, George C. Tsokos
Proc Natl Acad Sci U S A. 2021 May 4; 118(18): e2023230118. Published online 2021 Apr 28. doi: 10.1073/pnas.2023230118
PMCID:
PMC8106302
ArticlePDF–1.5M
16.
Shedding of Collagen XVII/BP180 in Skin Depends on Both ADAM10 and ADAM9
Claus-Werner Franzke, Leena Bruckner-Tuderman, Carl P. Blobel
J Biol Chem. 2009 Aug 28; 284(35): 23386–23396. Published online 2009 Jul 1. doi: 10.1074/jbc.M109.034090
PMCID:
PMC2749112
ArticlePDF–2.0M
17.
The disintegrin domain of ADAM9: a ligand for multiple β1 renal integrins
Rajeev M. Mahimkar, Orvin Visaya, Allan S. Pollock, David H. Lovett
Biochem J. 2005 Jan 15; 385(Pt 2): 461–468. Prepublished online 2004 Sep 10. Published online 2005 Jan 7. doi: 10.1042/BJ20041133
PMCID:
PMC1134717
ArticlePDF–461K
18.
A family of cellular proteins related to snake venom disintegrins.
G Weskamp, C P Blobel
Proc Natl Acad Sci U S A. 1994 Mar 29; 91(7): 2748–2751. doi: 10.1073/pnas.91.7.2748
PMCID:
PMC43447
SummaryPage BrowsePDF–1.0M
19.
A metalloprotease-disintegrin, MDC9/meltrin-gamma/ADAM9 and PKCdelta are involved in TPA-induced ectodomain shedding of membrane-anchored heparin-binding EGF-like growth factor.
Y Izumi, M Hirata, H Hasuwa, R Iwamoto, T Umata, K Miyado, Y Tamai, T Kurisaki, A Sehara-Fujisawa, S Ohno, E Mekada
EMBO J. 1998 Dec 15; 17(24): 7260–7272. doi: 10.1093/emboj/17.24.7260
PMCID:
PMC1171072
SummaryPDF–599K
20.
Regulation of insulin-like growth factor binding protein-5, four and a half lim-2, and a disintegrin and metalloprotease-9 expression in osteoblasts
K.E. Govoni, Y.G. Amaar, A. Kramer, E. Winter, D.J. Baylink, S. Mohan
Growth Horm IGF Res. Author manuscript; available in PMC 2010 Jul 15.
Published in final edited form as: Growth Horm IGF Res. 2006 Feb; 16(1): 49–56. Published online 2005 Nov 28. doi: 10.1016/j.ghir.2005.10.001
PMCID:
PMC2904509
ArticlePDF–513K

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