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any of a large group of nitrogenous organic compounds that are essential constituents of living cells; consist of polymers of amino acids; essential in the diet of animals for growth and for repair of tissues; can be obtained from meat and eggs and milk and legumes; "a diet high in protein"
in the Christian era; used before dates after the supposed year Christ was born; "in AD 200" (同)A.D., anno_Domini

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Americans for Democratic Action 米国人民主行動連盟

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2014/01/24 14:08:23」(JST)

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Diagram of an ectodomain shedding ADAM metalloprotease.

ADAM (A Disintegrin And Metalloproteinase)^[1]^[2] is a family of peptidase proteins.^[3] It is also known as the adamalysin family or MDC family(metalloproteinase-like, Disintegrin-like, cysteine rich). ADAMs are classified as sheddases because they cut off or shed extracellular portions of transmembrane proteins. For example, ADAM10 can cut off part of the HER2 receptor, activating it.^[4] Therapeutic ADAM inhibitors can potentiate anti-cancer therapy.^{[citation needed]}

It is categorized under EC 3.4.24.46.

Family members are:

ADAM2
ADAM7
ADAM8
ADAM9
ADAM10
ADAM11
ADAM12
ADAM15
ADAM17
ADAM18 (=ADAM27)
ADAM19
ADAM20
ADAM21 (=ADAM31)
ADAM22
ADAM23
ADAM28
ADAM29
ADAM30
ADAM33

References[edit]

^ Edwards DR, Handsley MM, Pennington CJ (October 2008). "The ADAM metalloproteinases". Mol. Aspects Med. 29 (5): 258–89. doi:10.1016/j.mam.2008.08.001. PMID 18762209.
^ Brocker, C; Vasiliou, V; Nebert, DW (Oct 2009). "Evolutionary divergence and functions of the ADAM and ADAMTS gene families.". Human Genomics 4 (1): 43–55. PMC 3500187. PMID 19951893. Cite uses deprecated parameters (help)
^ Wolfsberg TG, Straight PD, Gerena RL, et al. (1995). "ADAM, a widely distributed and developmentally regulated gene family encoding membrane proteins with a disintegrin and metalloprotease domain". Dev. Biol. 169 (1): 378–383. doi:10.1006/dbio.1995.1152. PMID 7750654.
^ Liu, P.C.; et al. (2006). "Identification of ADAM10 as a major source of HER2 ectodomain sheddase activity in HER2 overexpressing breast cancer cells.". Cancer Biology and Therapy 5 (6): 657–664. doi:10.4161/cbt.5.6.2708. PMID 16627989. Cite uses deprecated parameters (help)

External links[edit]

ADAM Proteins at the US National Library of Medicine Medical Subject Headings (MeSH)
http://www.healthvalue.net/sheddase.html

This hydrolase article is a stub. You can help Wikipedia by expanding it.

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English Journal

MBNL proteins and their target RNAs, interaction and splicing regulation.

Konieczny P1, Stepniak-Konieczna E1, Sobczak K2.
Nucleic acids research.Nucleic Acids Res.2015 Jan 1;42(17):10873-87. doi: 10.1093/nar/gku767. Epub 2014 Sep 2.
Muscleblind-like (MBNL) proteins are key regulators of precursor and mature mRNA metabolism in mammals. Based on published and novel data, we explore models of tissue-specific MBNL interaction with RNA. We portray MBNL domains critical for RNA binding and splicing regulation, and the structure of MB
PMID 25183524

Comparison of thylakoid structure and organization in sun and shade Haberlea rhodopensis populations under desiccation and rehydration.

Sárvári E1, Mihailova G2, Solti A3, Keresztes A4, Velitchkova M5, Georgieva K6.
Journal of plant physiology.J Plant Physiol.2014 Nov 1;171(17):1591-600. doi: 10.1016/j.jplph.2014.07.015. Epub 2014 Aug 12.
The resurrection plant, Haberlea rhodopensis can survive nearly total desiccation only in its usual low irradiation environment. However, populations with similar capacity to recover were discovered recently in several sunny habitats. To reveal what kind of morphological, structural and thylakoid-le
PMID 25151128

The DEAD-box helicase Ded1 from yeast is an mRNP cap-associated protein that shuttles between the cytoplasm and nucleus.

Senissar M1, Saux AL2, Belgareh-Touzé N3, Adam C2, Banroques J4, Tanner NK4.
Nucleic acids research.Nucleic Acids Res.2014 Nov 1;42(15):10005-22. doi: 10.1093/nar/gku584. Epub 2014 Jul 10.
The DEAD-box helicase Ded1 is an essential yeast protein that is closely related to mammalian DDX3 and to other DEAD-box proteins involved in developmental and cell cycle regulation. Ded1 is considered to be a translation-initiation factor that helps the 40S ribosome scan the mRNA from the 5' 7-meth
PMID 25013175

Japanese Journal

Crucial role of the Rap G protein signal in Notch activation and leukemogenicity of T-cell acute lymphoblastic leukemia.

Doi Keiko,Imai Takahiko,Kressler Christopher,Yagita Hideo,Agata Yasutoshi,Vooijs Marc,Hamazaki Yoko,Inoue Joe,Minato Nagahiro
Scientific reports 5, 2015-01-23
… The Rap G protein signal regulates Notch activation in early thymic progenitor cells, and deregulated Rap activation (Rap(high)) results in the development of Notch-dependent T-cell acute lymphoblastic leukemia (T-ALL). … Attenuation of the Rap signal by the expression of a dominant-negative Rap1A17 or Rap1GAP, Sipa1, in a T-ALL cell line resulted in the reduced Notch processing at site 2 due to impaired maturation of Adam10. …
NAID 120005555511

Central role of the exchange factor GEF-H1 in TNF-α–induced sequential activation of Rac, ADAM17/TACE, and RhoA in tubular epithelial cells

Waheed Faiza,Dan Qinghong,Amoozadeh Yasaman,Zhang Yuqian,Tanimura Susumu,Speight Pam,Kapus András,Szászi Katalin
Molecular Biology of the Cell 24(7), 1068-1082, 2013-04-01
… TACE activation requires the mitogen-activated protein kinase p38, which is activated through the small GTPase Rac. …
NAID 120005231330

The Release of EGF Domain from EGF-like Factors by a Specific Cleavage Enzyme Activates the EGFR-MAPK3/1 Pathway in Both Granulosa Cells and Cumulus Cells During the Ovulation Process

YAMASHITA Yasuhisa,SHIMADA Masayuki
The Journal of reproduction and development 58(5), 510-514, 2012-10-01
… Recent reports showed that granulosa cells and cumulus cells express EGF-like factors that activate the EGF receptor (EGFR)-mitogen-activated protein kinase3/1 (MAPK3/1) (also known as extracellular signal-regulated kinase1/2 (ERK1/2)) pathway in both cell types. … In our studies, TACE/ADAM17, which is known to be a proteolytic enzyme of EGF-like factors in many types of tissue, was found to be expressed in FSH/LH-stimulated granulosa cells and cumulus cells together with activation of the EGFR-MAPK3/1 pathway. …
NAID 10031123293