ADAM22

ADAM metallopeptidase domain 22, also known as ADAM22, is a human gene.cite web | title = Entrez Gene: ADAM22 ADAM metallopeptidase domain 22| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=53616| accessdate = ]

PBB_Summary
section_title =
summary_text = This gene encodes a member of the ADAM (a disintegrin and metalloprotease domain) family. Members of this family are membrane-anchored proteins structurally related to snake venom disintegrins, and have been implicated in a variety of biological processes involving cell-cell and cell-matrix interactions, including fertilization, muscle development, and neurogenesis. This gene is highly expressed in the brain and may function as an integrin ligand in the brain. Alternative splicing results in several transcript variants.cite web | title = Entrez Gene: ADAM22 ADAM metallopeptidase domain 22| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=53616| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Sagane K, Ohya Y, Hasegawa Y, Tanaka I |title=Metalloproteinase-like, disintegrin-like, cysteine-rich proteins MDC2 and MDC3: novel human cellular disintegrins highly expressed in the brain. |journal=Biochem. J. |volume=334 ( Pt 1) |issue= |pages= 93–8 |year= 1998 |pmid= 9693107 |doi=
*cite journal | author=Poindexter K, Nelson N, DuBose RF, "et al." |title=The identification of seven metalloproteinase-disintegrin (ADAM) genes from genomic libraries. |journal=Gene |volume=237 |issue= 1 |pages= 61–70 |year= 1999 |pmid= 10524237 |doi=
*cite journal | author=Harada T, Nishie A, Torigoe K, "et al." |title=The specific expression of three novel splice variant forms of human metalloprotease-like disintegrin-like cysteine-rich protein 2 gene inBrain tissues and gliomas. |journal=Jpn. J. Cancer Res. |volume=91 |issue= 10 |pages= 1001–6 |year= 2001 |pmid= 11050470 |doi=
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Zhu P, Sun Y, Xu R, "et al." |title=The interaction between ADAM 22 and 14-3-3zeta: regulation of cell adhesion and spreading. |journal=Biochem. Biophys. Res. Commun. |volume=301 |issue= 4 |pages= 991–9 |year= 2003 |pmid= 12589811 |doi=
*cite journal | author=Hillier LW, Fulton RS, Fulton LA, "et al." |title=The DNA sequence of human chromosome 7. |journal=Nature |volume=424 |issue= 6945 |pages= 157–64 |year= 2003 |pmid= 12853948 |doi= 10.1038/nature01782
*cite journal | author=Hillman RT, Green RE, Brenner SE |title=An unappreciated role for RNA surveillance. |journal=Genome Biol. |volume=5 |issue= 2 |pages= R8 |year= 2005 |pmid= 14759258 |doi= 10.1186/gb-2004-5-2-r8
*cite journal | author=Sagane K, Hayakawa K, Kai J, "et al." |title=Ataxia and peripheral nerve hypomyelination in ADAM22-deficient mice. |journal=BMC neuroscience |volume=6 |issue= 1 |pages= 33 |year= 2006 |pmid= 15876356 |doi= 10.1186/1471-2202-6-33
*cite journal | author=Zhu P, Sang Y, Xu H, "et al." |title=ADAM22 plays an important role in cell adhesion and spreading with the assistance of 14-3-3. |journal=Biochem. Biophys. Res. Commun. |volume=331 |issue= 4 |pages= 938–46 |year= 2005 |pmid= 15882968 |doi= 10.1016/j.bbrc.2005.03.229
*cite journal | author=Rual JF, Venkatesan K, Hao T, "et al." |title=Towards a proteome-scale map of the human protein-protein interaction network. |journal=Nature |volume=437 |issue= 7062 |pages= 1173–8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209
*cite journal | author=D'Abaco GM, Ng K, Paradiso L, "et al." |title=ADAM22, expressed in normal brain but not in high-grade gliomas, inhibits cellular proliferation via the disintegrin domain. |journal=Neurosurgery |volume=58 |issue= 1 |pages= 179–86; discussion 179–86 |year= 2006 |pmid= 16385342 |doi=
*cite journal | author=Gödde NJ, D'Abaco GM, Paradiso L, Novak U |title=Efficient ADAM22 surface expression is mediated by phosphorylation-dependent interaction with 14-3-3 protein family members. |journal=J. Cell. Sci. |volume=119 |issue= Pt 16 |pages= 3296–305 |year= 2006 |pmid= 16868027 |doi= 10.1242/jcs.03065
*cite journal | author=Fukata Y, Adesnik H, Iwanaga T, "et al." |title=Epilepsy-related ligand/receptor complex LGI1 and ADAM22 regulate synaptic transmission. |journal=Science |volume=313 |issue= 5794 |pages= 1792–5 |year= 2006 |pmid= 16990550 |doi= 10.1126/science.1129947
*cite journal | author=Chabrol E, Gourfinkel-An I, Scheffer IE, "et al." |title=Absence of mutations in the LGI1 receptor ADAM22 gene in autosomal dominant lateral temporal epilepsy. |journal=Epilepsy Res. |volume=76 |issue= 1 |pages= 41–8 |year= 2007 |pmid= 17681454 |doi= 10.1016/j.eplepsyres.2007.06.014
*cite journal | author=Gödde NJ, D'Abaco GM, Paradiso L, Novak U |title=Differential coding potential of ADAM22 mRNAs. |journal=Gene |volume=403 |issue= 1-2 |pages= 80–8 |year= 2007 |pmid= 17884303 |doi= 10.1016/j.gene.2007.07.033

PBB_Controls
update_page = yes
require_manual_inspection = no
update_protein_box = yes
update_summary = yes
update_citations = yes