ADAM10 (English Wikipedia)

Analysis of information sources in references of the Wikipedia article "ADAM10" in English language version.

refsWebsite

Global rank English rank

25nih.gov

4^th place

15doi.org

2^nd place

6semanticscholar.org

11^th place

8^th place

2ensembl.org

1,626^th place

1,007^th place

1brenda-enzymes.info

low place

1web.archive.org

1^st place

1wellcome.ac.uk

low place

brenda-enzymes.info (Global: low place; English: low place)

"Entry of ADAM10 endopeptidase (EC-Number 3.4.24.81 )".

doi.org (Global: 2^nd place; English: 2^nd place)

Moss ML, Bartsch JW (June 2004). "Therapeutic benefits from targeting of ADAM family members". Biochemistry. 43 (23): 7227–7235. doi:10.1021/bi049677f. PMID 15182168.
Nagano O, Saya H (December 2004). "Mechanism and biological significance of CD44 cleavage". Cancer Science. 95 (12): 930–935. doi:10.1111/j.1349-7006.2004.tb03179.x. PMC 11159127. PMID 15596040. S2CID 9009213.
Blobel CP (January 2005). "ADAMs: key components in EGFR signalling and development". Nature Reviews. Molecular Cell Biology. 6 (1): 32–43. doi:10.1038/nrm1548. PMID 15688065. S2CID 7011302.
Janes PW, Saha N, Barton WA, Kolev MV, Wimmer-Kleikamp SH, Nievergall E, et al. (October 2005). "Adam meets Eph: an ADAM substrate recognition module acts as a molecular switch for ephrin cleavage in trans". Cell. 123 (2): 291–304. doi:10.1016/j.cell.2005.08.014. PMID 16239146. S2CID 7962666.
Haass C, Kaether C, Thinakaran G, Sisodia S (May 2012). "Trafficking and proteolytic processing of APP". Cold Spring Harbor Perspectives in Medicine. 2 (5) a006270. doi:10.1101/cshperspect.a006270. PMC 3331683. PMID 22553493.
Yang J, Fu Z, Zhang X, Xiong M, Meng L, Zhang Z (July 2020). "TREM2 ectodomain and its soluble form in Alzheimer's disease". Journal of Neuroinflammation. 17 (1) 204. doi:10.1186/s12974-020-01878-2. PMC 7341574. PMID 32635934.
Souza JS, Lisboa AB, Santos TM, Andrade MV, Neves VB, Teles-Souza J, et al. (September 2020). "The evolution of ADAM gene family in eukaryotes". Genomics. 112 (5): 3108–3116. doi:10.1016/j.ygeno.2020.05.010. PMID 32437852. S2CID 218832838.
Smith KM, Gaultier A, Cousin H, Alfandari D, White JM, DeSimone DW (December 2002). "The cysteine-rich domain regulates ADAM protease function in vivo". The Journal of Cell Biology. 159 (5): 893–902. doi:10.1083/jcb.200206023. PMC 2173380. PMID 12460986.
Wolfsberg TG, Primakoff P, Myles DG, White JM (October 1995). "ADAM, a novel family of membrane proteins containing A Disintegrin And Metalloprotease domain: multipotential functions in cell-cell and cell-matrix interactions". The Journal of Cell Biology. 131 (2): 275–278. doi:10.1083/jcb.131.2.275. PMC 2199973. PMID 7593158.
Lolis E, Petsko GA (1990). "Transition-state analogues in protein crystallography: probes of the structural source of enzyme catalysis". Annual Review of Biochemistry. 59: 597–630. doi:10.1146/annurev.bi.59.070190.003121. PMID 2197984.
Marcello E, Borroni B, Pelucchi S, Gardoni F, Di Luca M (November 2017). "ADAM10 as a therapeutic target for brain diseases: from developmental disorders to Alzheimer's disease". Expert Opinion on Therapeutic Targets. 21 (11): 1017–1026. doi:10.1080/14728222.2017.1386176. PMID 28960088. S2CID 46800368.
Yuan Q, Yu H, Chen J, Song X, Sun L (2020). "ADAM10 promotes cell growth, migration, and invasion in osteosarcoma via regulating E-cadherin/β-catenin signaling pathway and is regulated by miR-122-5p". Cancer Cell International. 20 99. doi:10.1186/s12935-020-01174-2. PMC 7106760. PMID 32256208.
Das S, Amin SA, Jha T (November 2021). "Inhibitors of gelatinases (MMP-2 and MMP-9) for the management of hematological malignancies". European Journal of Medicinal Chemistry. 223 113623. doi:10.1016/j.ejmech.2021.113623. PMID 34157437.
Liu PC, Liu X, Li Y, Covington M, Wynn R, Huber R, et al. (June 2006). "Identification of ADAM10 as a major source of HER2 ectodomain sheddase activity in HER2 overexpressing breast cancer cells". Cancer Biology & Therapy. 5 (6): 657–664. doi:10.4161/cbt.5.6.2708. PMID 16627989. S2CID 23463401.
Marcello E, Saraceno C, Musardo S, Vara H, de la Fuente AG, Pelucchi S, et al. (June 2013). "Endocytosis of synaptic ADAM10 in neuronal plasticity and Alzheimer's disease". The Journal of Clinical Investigation. 123 (6): 2523–2538. doi:10.1172/JCI65401. PMC 3668814. PMID 23676497.

ensembl.org (Global: 1,626^th place; English: 1,007^th place)

May2017.archive.ensembl.org

GRCh38: Ensembl release 89: ENSG00000137845 – Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000054693 – Ensembl, May 2017

nih.gov (Global: 4^th place; English: 4^th place)

pubmed.ncbi.nlm.nih.gov

Moss ML, Bartsch JW (June 2004). "Therapeutic benefits from targeting of ADAM family members". Biochemistry. 43 (23): 7227–7235. doi:10.1021/bi049677f. PMID 15182168.
Nagano O, Saya H (December 2004). "Mechanism and biological significance of CD44 cleavage". Cancer Science. 95 (12): 930–935. doi:10.1111/j.1349-7006.2004.tb03179.x. PMC 11159127. PMID 15596040. S2CID 9009213.
Blobel CP (January 2005). "ADAMs: key components in EGFR signalling and development". Nature Reviews. Molecular Cell Biology. 6 (1): 32–43. doi:10.1038/nrm1548. PMID 15688065. S2CID 7011302.
Janes PW, Saha N, Barton WA, Kolev MV, Wimmer-Kleikamp SH, Nievergall E, et al. (October 2005). "Adam meets Eph: an ADAM substrate recognition module acts as a molecular switch for ephrin cleavage in trans". Cell. 123 (2): 291–304. doi:10.1016/j.cell.2005.08.014. PMID 16239146. S2CID 7962666.
Haass C, Kaether C, Thinakaran G, Sisodia S (May 2012). "Trafficking and proteolytic processing of APP". Cold Spring Harbor Perspectives in Medicine. 2 (5) a006270. doi:10.1101/cshperspect.a006270. PMC 3331683. PMID 22553493.
Yang J, Fu Z, Zhang X, Xiong M, Meng L, Zhang Z (July 2020). "TREM2 ectodomain and its soluble form in Alzheimer's disease". Journal of Neuroinflammation. 17 (1) 204. doi:10.1186/s12974-020-01878-2. PMC 7341574. PMID 32635934.
Souza JS, Lisboa AB, Santos TM, Andrade MV, Neves VB, Teles-Souza J, et al. (September 2020). "The evolution of ADAM gene family in eukaryotes". Genomics. 112 (5): 3108–3116. doi:10.1016/j.ygeno.2020.05.010. PMID 32437852. S2CID 218832838.
Smith KM, Gaultier A, Cousin H, Alfandari D, White JM, DeSimone DW (December 2002). "The cysteine-rich domain regulates ADAM protease function in vivo". The Journal of Cell Biology. 159 (5): 893–902. doi:10.1083/jcb.200206023. PMC 2173380. PMID 12460986.
Wolfsberg TG, Primakoff P, Myles DG, White JM (October 1995). "ADAM, a novel family of membrane proteins containing A Disintegrin And Metalloprotease domain: multipotential functions in cell-cell and cell-matrix interactions". The Journal of Cell Biology. 131 (2): 275–278. doi:10.1083/jcb.131.2.275. PMC 2199973. PMID 7593158.
Lolis E, Petsko GA (1990). "Transition-state analogues in protein crystallography: probes of the structural source of enzyme catalysis". Annual Review of Biochemistry. 59: 597–630. doi:10.1146/annurev.bi.59.070190.003121. PMID 2197984.
Marcello E, Borroni B, Pelucchi S, Gardoni F, Di Luca M (November 2017). "ADAM10 as a therapeutic target for brain diseases: from developmental disorders to Alzheimer's disease". Expert Opinion on Therapeutic Targets. 21 (11): 1017–1026. doi:10.1080/14728222.2017.1386176. PMID 28960088. S2CID 46800368.
Yuan Q, Yu H, Chen J, Song X, Sun L (2020). "ADAM10 promotes cell growth, migration, and invasion in osteosarcoma via regulating E-cadherin/β-catenin signaling pathway and is regulated by miR-122-5p". Cancer Cell International. 20 99. doi:10.1186/s12935-020-01174-2. PMC 7106760. PMID 32256208.
Das S, Amin SA, Jha T (November 2021). "Inhibitors of gelatinases (MMP-2 and MMP-9) for the management of hematological malignancies". European Journal of Medicinal Chemistry. 223 113623. doi:10.1016/j.ejmech.2021.113623. PMID 34157437.
Liu PC, Liu X, Li Y, Covington M, Wynn R, Huber R, et al. (June 2006). "Identification of ADAM10 as a major source of HER2 ectodomain sheddase activity in HER2 overexpressing breast cancer cells". Cancer Biology & Therapy. 5 (6): 657–664. doi:10.4161/cbt.5.6.2708. PMID 16627989. S2CID 23463401.
Marcello E, Saraceno C, Musardo S, Vara H, de la Fuente AG, Pelucchi S, et al. (June 2013). "Endocytosis of synaptic ADAM10 in neuronal plasticity and Alzheimer's disease". The Journal of Clinical Investigation. 123 (6): 2523–2538. doi:10.1172/JCI65401. PMC 3668814. PMID 23676497.

ncbi.nlm.nih.gov

"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
"Entrez Gene: ADAM10 ADAM metallopeptidase domain 10".
Nagano O, Saya H (December 2004). "Mechanism and biological significance of CD44 cleavage". Cancer Science. 95 (12): 930–935. doi:10.1111/j.1349-7006.2004.tb03179.x. PMC 11159127. PMID 15596040. S2CID 9009213.
Haass C, Kaether C, Thinakaran G, Sisodia S (May 2012). "Trafficking and proteolytic processing of APP". Cold Spring Harbor Perspectives in Medicine. 2 (5) a006270. doi:10.1101/cshperspect.a006270. PMC 3331683. PMID 22553493.
Yang J, Fu Z, Zhang X, Xiong M, Meng L, Zhang Z (July 2020). "TREM2 ectodomain and its soluble form in Alzheimer's disease". Journal of Neuroinflammation. 17 (1) 204. doi:10.1186/s12974-020-01878-2. PMC 7341574. PMID 32635934.
Smith KM, Gaultier A, Cousin H, Alfandari D, White JM, DeSimone DW (December 2002). "The cysteine-rich domain regulates ADAM protease function in vivo". The Journal of Cell Biology. 159 (5): 893–902. doi:10.1083/jcb.200206023. PMC 2173380. PMID 12460986.
Wolfsberg TG, Primakoff P, Myles DG, White JM (October 1995). "ADAM, a novel family of membrane proteins containing A Disintegrin And Metalloprotease domain: multipotential functions in cell-cell and cell-matrix interactions". The Journal of Cell Biology. 131 (2): 275–278. doi:10.1083/jcb.131.2.275. PMC 2199973. PMID 7593158.
Yuan Q, Yu H, Chen J, Song X, Sun L (2020). "ADAM10 promotes cell growth, migration, and invasion in osteosarcoma via regulating E-cadherin/β-catenin signaling pathway and is regulated by miR-122-5p". Cancer Cell International. 20 99. doi:10.1186/s12935-020-01174-2. PMC 7106760. PMID 32256208.
Marcello E, Saraceno C, Musardo S, Vara H, de la Fuente AG, Pelucchi S, et al. (June 2013). "Endocytosis of synaptic ADAM10 in neuronal plasticity and Alzheimer's disease". The Journal of Clinical Investigation. 123 (6): 2523–2538. doi:10.1172/JCI65401. PMC 3668814. PMID 23676497.

semanticscholar.org (Global: 11^th place; English: 8^th place)

api.semanticscholar.org

Nagano O, Saya H (December 2004). "Mechanism and biological significance of CD44 cleavage". Cancer Science. 95 (12): 930–935. doi:10.1111/j.1349-7006.2004.tb03179.x. PMC 11159127. PMID 15596040. S2CID 9009213.
Blobel CP (January 2005). "ADAMs: key components in EGFR signalling and development". Nature Reviews. Molecular Cell Biology. 6 (1): 32–43. doi:10.1038/nrm1548. PMID 15688065. S2CID 7011302.
Janes PW, Saha N, Barton WA, Kolev MV, Wimmer-Kleikamp SH, Nievergall E, et al. (October 2005). "Adam meets Eph: an ADAM substrate recognition module acts as a molecular switch for ephrin cleavage in trans". Cell. 123 (2): 291–304. doi:10.1016/j.cell.2005.08.014. PMID 16239146. S2CID 7962666.
Souza JS, Lisboa AB, Santos TM, Andrade MV, Neves VB, Teles-Souza J, et al. (September 2020). "The evolution of ADAM gene family in eukaryotes". Genomics. 112 (5): 3108–3116. doi:10.1016/j.ygeno.2020.05.010. PMID 32437852. S2CID 218832838.
Marcello E, Borroni B, Pelucchi S, Gardoni F, Di Luca M (November 2017). "ADAM10 as a therapeutic target for brain diseases: from developmental disorders to Alzheimer's disease". Expert Opinion on Therapeutic Targets. 21 (11): 1017–1026. doi:10.1080/14728222.2017.1386176. PMID 28960088. S2CID 46800368.
Liu PC, Liu X, Li Y, Covington M, Wynn R, Huber R, et al. (June 2006). "Identification of ADAM10 as a major source of HER2 ectodomain sheddase activity in HER2 overexpressing breast cancer cells". Cancer Biology & Therapy. 5 (6): 657–664. doi:10.4161/cbt.5.6.2708. PMID 16627989. S2CID 23463401.

web.archive.org (Global: 1^st place; English: 1^st place)

"'Sheddase' helps the malaria parasite invade red blood cells". Archived from the original on 2008-04-12.

wellcome.ac.uk (Global: low place; English: low place)

malaria.wellcome.ac.uk

"'Sheddase' helps the malaria parasite invade red blood cells". Archived from the original on 2008-04-12.