Literature for peptidase M12.208: ADAM8 peptidase
(Topics flags: A Assay, S Structure, T Target, P Specificity, K Knockout, E Expression, V Review, M Mutation, I Inhibitor. To select only the references relevant to a single topic, click the link above. See explanation.)
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Shen,K., Shan,Z., Li,Y., Ji,Z., Zhou,L. and Lv,Z.
TFAP2A Activates ADAM8 to Promote Lung Adenocarcinoma Angiogenesis Through the JAK/STAT Signaling Pathway
J Biochem Mol Toxicol39, e70097-e70097. PubMed Europe PubMed DOI K -
Chen,K., Tao,H., Zhu,P., Chu,M., Li,X., Shi,Y., Zhang,L., Xu,Y., Lv,S., Huang,L., Huang,W. and Geng,D.
ADAM8 silencing suppresses the migration and invasion of fibroblast-like synoviocytes via FSCN1/MAPK cascade in osteoarthritis
Arthritis Res Ther26, 20-20. PubMed Europe PubMed DOI -
Qian,Z., Zhang,Q., Li,P., Li,Y., Zhang,Y., Li,R., Zhao,T., Xia,M., Chen,Y. and Hong,X.
A Disintegrin and Metalloproteinase-8 Protects Against Erastin-Induced Neuronal Ferroptosis via Activating Nrf2/HO-1/FTH1 Signaling Pathway
Mol Neurobiol61, 3490-3502. PubMed Europe PubMed DOI K -
Alawak,M., Abu Dayyih,A., Mahmoud,G., Tariq,I., Duse,L., Goergen,N., Engelhardt,K., Reddy Pinnapireddy,S., Jedelska,J., Awak,M., Konig,A.M., Brussler,J., Bartsch,J.W. and Bakowsky,U.
ADAM 8 as a Novel Target for Doxorubicin Delivery to TNBC Cells using Magnetic Thermosensitive Liposomes
Eur J Pharm Biopharm158, 390-400. PubMed Europe PubMed DOI -
Awan,T., Babendreyer,A., Mahmood Alvi,A., Dusterhoft,S., Lambertz,D., Bartsch,J.W., Liedtke,C. and Ludwig,A.
Expression levels of the metalloproteinase ADAM8 critically regulate proliferation, migration and malignant signalling events in hepatoma cells
J Cell Mol Med25, 1982-1999. PubMed Europe PubMed DOI K -
Awan,T., Babendreyer,A., Wozniak,J., Alvi,A.M., Sterzer,V., Cook,L., Bartsch,J.W., Liedtke,C., Yildiz,D. and Ludwig,A.
Expression of the Metalloproteinase ADAM8 Is Upregulated in Liver Inflammation Models and Enhances Cytokine Release In Vitro
Mediators Inflamm2021, 6665028-6665028. PubMed Europe PubMed DOI K -
Jaworek,C., Verel-Yilmaz,Y., Driesch,S., Ostgathe,S., Cook,L., Wagner,S., Bartsch,D.K., Slater,E.P. and Bartsch,J.W.
Cohort Analysis of ADAM8 Expression in the PDAC Tumor Stroma
J Pers Med11, 113-113. PubMed Europe PubMed DOI -
Lu,H., Meng,Y., Han,X. and Zhang,W.
ADAM8 Activates NLRP3 Inflammasome to Promote Cerebral Ischemia-Reperfusion Injury
J Healthc Eng2021, 3097432-3097432. PubMed Europe PubMed DOI -
Li,Y., Guo,S., Zhao,K., Conrad,C., Driescher,C., Rothbart,V., Schlomann,U., Guerreiro,H., Bopp,M.H., Konig,A., Carl,B., Pagenstecher,A., Nimsky,C. and Bartsch,J.W.
ADAM8 affects glioblastoma progression by regulating osteopontin-mediated angiogenesis
Biol Chem402, 195-206. PubMed Europe PubMed DOI -
Schlomann,U., Dorzweiler,K., Nuti,E., Tuccinardi,T., Rossello,A. and Bartsch,J.W.
Metalloprotease inhibitor profiles of human ADAM8 in vitro and in cell-based assays
Biol Chem400, 801-810. PubMed Europe PubMed DOI I -
Polverino,F., Rojas-Quintero,J., Wang,X., Petersen,H., Zhang,L., Gai,X., Higham,A., Zhang,D., Gupta,K., Rout,A., Yambayev,I., Pinto-Plata,V., Sholl,L.M., Cunoosamy,D., Celli,B.R., Goldring,J., Singh,D., Tesfaigzi,Y., Wedzicha,J., Olsson,H. and Owen,C.A.
A disintegrin and metalloproteinase domain-8: a novel protective proteinase in chronic obstructive pulmonary disease
Am J Respir Crit Care Med198, 1254-1267. PubMed Europe PubMed DOI -
Kleino,I., Jarviluoma,A., Hepojoki,J., Huovila,A.P. and Saksela,K.
Preferred SH3 domain partners of ADAM metalloproteases include shared and ADAM-specific SH3 interactions
PLoS ONE10, e0121301-e0121301. PubMed Europe PubMed DOI -
Bartsch,J.W. and Schlomann,U.
ADAM8/MS2/CD156a
[ISSN:978-0-12-407744-7]3, 1094-1101. DOI -
Hall,T., Shieh,H.S., Day,J.E., Caspers,N., Chrencik,J.E., Williams,J.M., Pegg,L.E., Pauley,A.M., Moon,A.F., Krahn,J.M., Fischer,D.H., Kiefer,J.R., Tomasselli,A.G. and Zack,M.D.
Structure of human ADAM-8 catalytic domain complexed with batimastat
Acta Crystallogr Sect F Struct Biol Cryst Commun68, 616-621. PubMed Europe PubMed DOI S I -
Liang,J. and Kong,Q.
alpha-Cleavage of cellular prion protein
Prion6, 453-460. PubMed Europe PubMed DOI -
Dominguez-Luis,M., Lamana,A., Vazquez,J., Garcia-Navas,R., Mollinedo,F., Sanchez-Madrid,F., Diaz-Gonzalez,F. and Urzainqui,A.
The metalloprotease ADAM8 is associated with and regulates the function of the adhesion receptor PSGL-1 through ERM proteins
Eur J Immunol41, 3436-3442. PubMed Europe PubMed DOI -
Ishizuka,H., Garcia-Palacios,V., Lu,G., Subler,M.A., Zhang,H., Boykin,C.S., Choi,S.J., Zhao,L., Patrene,K., Galson,D.L., Blair,H.C., Hadi,T.M., Windle,J.J., Kurihara,N. and Roodman,G.D.
ADAM8 enhances osteoclast precursor fusion and osteoclast formation in vitro and in vivo
J Bone Miner Res26, 169-181. PubMed Europe PubMed DOI -
Paulissen,G., Rocks,N., Gueders,M.M., Bedoret,D., Crahay,C., Quesada-Calvo,F., Hacha,J., Bekaert,S., Desmet,C., Foidart,J.M., Bureau,F., Noel,A. and Cataldo,D.D.
ADAM-8, a metalloproteinase, drives acute allergen-induced airway inflammation
Eur J Immunol41, 380-391. PubMed Europe PubMed DOI -
Bartsch,J.W., Wildeboer,D., Koller,G., Naus,S., Rittger,A., Moss,M.L., Minai,Y. and Jockusch,H.
Tumor necrosis factor-alpha (TNF-alpha) regulates shedding of TNF-alpha receptor 1 by the metalloprotease-disintegrin ADAM8: evidence for a protease-regulated feedback loop in neuroprotection
J Neurosci30, 12210-12218. PubMed Europe PubMed DOI -
Gossens,K., Naus,S., Hollander,G.A. and Ziltener,H.J.
Deficiency of the metalloproteinase-disintegrin ADAM8 is associated with thymic hyper-cellularity
PLoS ONE5, e12766-e12766. PubMed Europe PubMed DOI -
Guaiquil,V.H., Swendeman,S., Zhou,W., Guaiquil,P., Weskamp,G., Bartsch,J.W. and Blobel,C.P.
ADAM8 is a negative regulator of retinal neovascularization and of the growth of heterotopically injected tumor cells in mice
J Mol Med (Berl)88, 497-505. PubMed Europe PubMed DOI -
Hernandez,I., Moreno,J.L., Zandueta,C., Montuenga,L. and Lecanda,F.
Novel alternatively spliced ADAM8 isoforms contribute to the aggressive bone metastatic phenotype of lung cancer
Oncogene29, 3758-3769. PubMed Europe PubMed DOI M -
Iida,A., Sakaguchi,K., Sato,K., Sakurai,H., Nishimura,D., Iwaki,A., Takeuchi,M., Kobayashi,M., Misaki,K., Yonemura,S., Kawahara,A. and Sehara-Fujisawa,A.
Metalloprotease-dependent onset of blood circulation in zebrafish
Curr Biol20, 1110-1116. PubMed Europe PubMed DOI -
Naus,S., Blanchet,M.R., Gossens,K., Zaph,C., Bartsch,J.W., McNagny,K.M. and Ziltener,H.J.
The metalloprotease-disintegrin ADAM8 is essential for the development of experimental asthma
Am J Respir Crit Care Med181, 1318-1328. PubMed Europe PubMed DOI K T -
Ainola,M., Li,T.F., Mandelin,J., Hukkanen,M., Choi,S.J., Salo,J. and Konttinen,Y.T.
Involvement of a disintegrin and a metalloproteinase 8 (ADAM8) in osteoclastogenesis and pathological bone destruction
Ann Rheum Dis68, 427-434. PubMed Europe PubMed DOI -
Hall,T., Leone,J.W., Wiese,J.F., Griggs,D.W., Pegg,L.E., Pauley,A.M., Tomasselli,A.G. and Zack,M.D.
Autoactivation of human ADAM8: a novel pre-processing step is required for catalytic activity
Biosci Rep29, 217-228. PubMed Europe PubMed DOI -
Hall,T., Pegg,L.E., Pauley,A.M., Fischer,H.D., Tomasselli,A.G. and Zack,M.D.
ADAM8 substrate specificity: influence of pH on pre-processing and proteoglycan degradation
Arch Biochem Biophys491, 106-111. PubMed Europe PubMed DOI -
Knolle,M.D. and Owen,C.A.
ADAM8: a new therapeutic target for asthma
Expert Opin Ther Targets13, 523-540. PubMed Europe PubMed DOI V T -
Koller,G., Schlomann,U., Golfi,P., Ferdous,T., Naus,S. and Bartsch,J.W.
ADAM8/MS2/CD156, an emerging drug target in the treatment of inflammatory and invasive pathologies
Curr Pharm Des15, 2272-2281. PubMed Europe PubMed DOI T -
Mahoney,E.T., Benton,R.L., Maddie,M.A., Whittemore,S.R. and Hagg,T.
ADAM8 is selectively up-regulated in endothelial cells and is associated with angiogenesis after spinal cord injury in adult mice
J Comp Neurol512, 243-255. PubMed Europe PubMed DOI -
Yeh,H.Y. and Klesius,P.H.
Channel catfish (Ictalurus punctatus Rafinesque, 1818) CD156a (ADAM metallopeptidase domain 8): cDNA clone, characterization and expression in tissues
Vet Immunol Immunopathol132, 307-313. PubMed Europe PubMed DOI E -
Zack,M.D., Melton,M.A., Stock,J.L., Storer,C.E., Barve,R.A., Minnerly,J.C., Weiss,D.J., Stejskal,J.A., Tortorella,M.D., Turk,J.R., Shevlin,K.M. and Malfait,A.M.
Reduced incidence and severity of experimental autoimmune arthritis in mice expressing catalytically inactive A disintegrin and metalloproteinase 8 (ADAM8)
Clin Exp Immunol158, 246-256. PubMed Europe PubMed DOI K -
Zack,M.D., Malfait,A.M., Skepner,A.P., Yates,M.P., Griggs,D.W., Hall,T., Hills,R.L., Alston,J.T., Nemirovskiy,O.V., Radabaugh,M.R., Leone,J.W., Arner,E.C. and Tortorella,M.D.
ADAM-8 isolated from human osteoarthritic chondrocytes cleaves fibronectin at Ala(271)
Arthritis Rheum60, 2704-2713. PubMed Europe PubMed DOI P -
Foley,S.C., Mogas,A.K., Olivenstein,R., Fiset,P.O., Chakir,J., Bourbeau,J., Ernst,P., Lemiere,C., Martin,J.G. and Hamid,Q.
Increased expression of ADAM33 and ADAM8 with disease progression in asthma
J Allergy Clin Immunol119, 863-871. PubMed Europe PubMed DOI -
Gomez-Gaviro,M., Dominguez-Luis,M., Canchado,J., Calafat,J., Janssen,H., Lara-Pezzi,E., Fourie,A., Tugores,A., Valenzuela-Fernandez,A., Mollinedo,F., Sanchez-Madrid,F. and Diaz-Gonzalez,F.
Expression and regulation of the metalloproteinase ADAM-8 during human neutrophil pathophysiological activation and its catalytic activity on L-selectin shedding
J Immunol178, 8053-8063. PubMed Europe PubMed -
Moss,M.L. and Rasmussen,F.H.
Fluorescent substrates for the proteinases ADAM17, ADAM10, ADAM8, and ADAM12 useful for high-throughput inhibitor screening
Anal Biochem366, 144-148. PubMed Europe PubMed DOI A I -
Naus,S., Reipschlager,S., Wildeboer,D., Lichtenthaler,S.F., Mitterreiter,S., Guan,Z., Moss,M.L. and Bartsch,J.W.
Identification of candidate substrates for ectodomain shedding by the metalloprotease-disintegrin ADAM8
Biol Chem387, 337-346. PubMed Europe PubMed DOI E -
Wildeboer,D., Naus,S., Amy Sang,Q.X., Bartsch,J.W. and Pagenstecher,A.
Metalloproteinase disintegrins ADAM8 and ADAM19 are highly regulated in human primary brain tumors and their expression levels and activities are associated with invasiveness
J Neuropathol Exp Neurol65, 516-527. PubMed Europe PubMed DOI -
Kelly,K., Hutchinson,G., Nebenius-Oosthuizen,D., Smith,A.J., Bartsch,J.W., Horiuchi,K., Rittger,A., Manova,K., Docherty,A.J. and Blobel,C.P.
Metalloprotease-disintegrin ADAM8: expression analysis and targeted deletion in mice
Dev Dyn232, 221-231. PubMed Europe PubMed DOI K -
Ishikawa,N., Daigo,Y., Yasui,W., Inai,K., Nishimura,H., Tsuchiya,E., Kohno,N. and Nakamura,Y.
ADAM8 as a novel serological and histochemical marker for lung cancer
Clin Cancer Res10, 8363-8370. PubMed Europe PubMed DOI -
[YEAR:15-4-2004]King,N.E., Zimmermann,N., Pope,S.M., Fulkerson,P.C., Nikolaidis,N.M., Mishra,A., Witte,D.P. and Rothenberg,M.E.
Expression and regulation of a disintegrin and metalloproteinase (ADAM)8 in experimental asthma
Am J Respir Cell Mol Biol31, 257-265. PubMed Europe PubMed DOI -
[YEAR:16-4-2004]Naus,S., Richter,M., Wildeboer,D., Moss,M., Schachner,M. and Bartsch,J.W.
Ectodomain shedding of the neural recognition molecule CHL1 by the metalloprotease-disintegrin ADAM8 promotes neurite outgrowth and suppresses neuronal cell death
J Biol Chem279, 16083-16090. PubMed Europe PubMed DOI I -
Wolfsberg,T.G. and White,J.M.
ADAM metalloproteinases
[ISSN:0-12-079610-4]2, 709-714. V -
[YEAR:15-8-2003]Fourie,A.M., Coles,F., Moreno,V. and Karlsson,L.
Catalytic activity of ADAM8, ADAM15, and MDC-L (ADAM28) on synthetic peptide substrates and in ectodomain cleavage of CD23
J Biol Chem278, 30469-30477. PubMed Europe PubMed DOI -
[YEAR:31-7-2002]Amour,A., Knight,C.G., English,W.R., Webster,A., Slocombe,P.M., Knauper,V., Docherty,A.J., Becherer,J.D., Blobel,C.P. and Murphy,G.
The enzymatic activity of ADAM8 and ADAM9 is not regulated by TIMPs
FEBS Lett524, 154-158. PubMed Europe PubMed DOI -
[YEAR:13-12-2002]Schlomann,U., Wildeboer,D., Webster,A., Antropova,O., Zeuschner,D., Knight,C.G., Docherty,A.J., Lambert,M., Skelton,L., Jockusch,H. and Bartsch,J.W.
The metalloprotease disintegrin ADAM8. Processing by autocatalysis is required for proteolytic activity and cell adhesion
J Biol Chem277, 48210-48219. PubMed Europe PubMed DOI I -
[YEAR:1-11-2000]Schlomann,U., Rathke-Hartlieb,S., Yamamoto,S., Jockusch,H. and Bartsch,J.W.
Tumor necrosis factor alpha induces a metalloprotease-disintegrin, ADAM8 (CD 156): Implications for neuron-glia interactions during neurodegeneration
J Neurosci20, 7964-7971. PubMed Europe PubMed -
Kataoka,M., Yoshiyama,K., Matsuura,K., Hijiya,N., Higuchi,Y. and Yamamoto,S.
Structure of the murine CD156 gene, characterization of its promoter, and chromosomal location
J Biol Chem272, 18209-18215. PubMed Europe PubMed DOI -
Yoshiyama,K., Higuchi,Y., Kataoka,M., Matsuura,K. and Yamamoto,S.
CD156 (human ADAM8): expression, primary amino acid sequence, and gene location
Genomics41, 56-62. PubMed Europe PubMed DOI
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