WordNet

relying on or requiring a person or thing for support, supply, or what is needed; "dependent children"; "dependent on moisture"
addicted to a drug (同)dependant, drug-addicted, hooked, strung-out
contingent on something else (同)dependant, qualified
(of a clause) unable to stand alone syntactically as a complete sentence; "a subordinate (or dependent) clause functions as a noun or adjective or adverb within a sentence" (同)subordinate
the 3rd letter of the Roman alphabet (同)c
(music) the keynote of the scale of C major
a general-purpose programing language closely associated with the UNIX operating system

PrepTutorEJDIC

『頼っている』,依存している,従属している / 扶養される人(家族)
carbonの化学記号
Calciumの化学記号

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1. ビタミンKおよびその合成ならびにガンマカルボキシグルタミン酸の機能 vitamin k and the synthesis and function of gamma carboxyglutamic acid
2. 黒色腫（メラノーマ）に対する遺伝的感受性 inherited susceptibility to melanoma
3. 稀な遺伝性凝固異常 rare inherited coagulation disorders
4. 前立腺癌の分子生物学 molecular biology of prostate cancer
5. T細胞受容体シグナル伝達 t cell receptor signaling

English Journal

Defining the interaction of perforin with calcium and the phospholipid membrane.

Traore DA, Brennan AJ, Law RH, Dogovski C, Perugini MA, Lukoyanova N, Leung EW, Norton RS, Lopez JA, Browne KA, Yagita H, Lloyd GJ, Ciccone A, Verschoor S, Trapani JA, Whisstock JC, Voskoboinik I.Source††Crystallography, Institute of Structural and Molecular Biology, Birkbeck College, Malet Street, London WC1E 7HX, U.K.
The Biochemical journal.Biochem J.2013 Dec 15;456(3):323-35. doi: 10.1042/BJ20130999.
Following its secretion from cytotoxic lymphocytes into the immune synapse, perforin binds to target cell membranes through its Ca2+-dependent C2 domain. Membrane-bound perforin then forms pores that allow passage of pro-apoptopic granzymes into the target cell. In the present study, structural and
PMID 24070258

Autonomous changes in the swimming direction of sperm in the gastropod Strombus luhuanus.

Shiba K, Shibata D, Inaba K.SourceUniversity of Tsukuba, Japan.
The Journal of experimental biology.J Exp Biol.2013 Dec 5. [Epub ahead of print]
The sperm of the gastropod Strombus luhuanus show dimorphism. The eusperm have a nucleus and fertilize the egg, whereas the other type of sperm, parasperm, are anucleate and are thought to assist fertilization. Here we report the autonomous changes in the swimming pattern of S. luhuanus eusperm. In
PMID 24311809

Ca2+/S100 proteins inhibit the interactions of FKBP38 with Bcl-2 and Hsp90.

Shimamoto S, Tsuchiya M, Yamaguchi F, Kubota Y, Tokumitsu H, Kobayashi R.AbstractFKBP38 (FK506-binding protein 38), a membrane-anchored, tetratricopeptide repeat (TPR)-containing immunophilin, regulates signaling pathways such as cell survival, apoptosis, proliferation, and metastasis. However, the mechanisms that regulate the activity of FKBP38 are, at present, poorly understood. We previously reported that Ca2+/S100 proteins directly associate with the TPR-proteins, such as Hsp70/Hsp90-organizing protein (Hop), kinesin-light chain, Tom70, FKBP52, CyP40, C-terminus of Hsc70-interacting protein (CHIP) and protein phosphatase 5 (PP5), leading to the dissociation of the interactions of the TPR-proteins with their target proteins. Therefore, we have hypothesized that Ca2+/S100 proteins can interact with FKBP38 and regulate its function. In vitro binding studies demonstrated that S100A1, S100A2, S100A6, S100B, and S100P specifically interact with FKBP38 and inhibit the interaction of FKBP38 with Bcl-2 and Hsp90. Overexpression of permanently active S100P in Huh-7 cells inhibited the interaction of FKBP38 with Bcl-2, resulting in the suppression of Bcl-2 stability. The association of the S100 proteins with FKBP38 provides a Ca2+-dependent regulatory mechanism of the FKBP38 mediated signaling pathways.
The Biochemical journal.Biochem J.2013 Dec 3. [Epub ahead of print]
FKBP38 (FK506-binding protein 38), a membrane-anchored, tetratricopeptide repeat (TPR)-containing immunophilin, regulates signaling pathways such as cell survival, apoptosis, proliferation, and metastasis. However, the mechanisms that regulate the activity of FKBP38 are, at present, poorly understoo
PMID 24295050