- 関
- mutein
WordNet
- tending to undergo or resulting from mutation; "a mutant gene"
- an animal that has undergone mutation
- (biology) an organism that has characteristics resulting from chromosomal alteration (同)mutation, variation, sport
- 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"
PrepTutorEJDIC
- 突然変異種(堤)
- 蛋白(たんばく)質
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2015/12/01 11:08:16」(JST)
[Wiki en表示]
A mutant protein is the protein product encoded by a gene with mutation.[1] Mutated protein can have single amino acid change (minor, but still in many cases significant change leading to disease) or wide-range amino acid changes by e.g. truncation of C-terminus after introducing premature stop codon.
See also
- missense mutation
- nonsense mutation
- point mutation
- single-nucleotide polymorphism
References
- ^ Wang, Qing; Chaerkady, Raghothama; Wu, Jian; Hwang, Hee Jung; Papadopoulos, Nick; Kopelovich, Levy; Maitra, Anirban; Matthaei, Hanno; et al. (2011). "Mutant proteins as cancer-specific biomarkers". Proceedings of the National Academy of Sciences 108 (6): 2444–9. doi:10.1073/pnas.1019203108. PMC 3038743. PMID 21248225.
UpToDate Contents
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English Journal
- Effect of VEGF, P53 and telomerase on angiogenesis of gastric carcinoma tissue.
- Yu YF1, Zhang Y2, Shen N2, Zhang RY2, Lu XQ2.Author information 1Affiliated Hospital of Hebei University of Engineering, Handan 056002, Hebei, China. Electronic address: yyfangtg@163.com.2Affiliated Hospital of Hebei University of Engineering, Handan 056002, Hebei, China.AbstractOBJECTIVE: To investigate the effect of vascular endothelial growth factor (VEGF), P53 and telomerase on angiogenesis in gastric carcinoma tissue.
- Asian Pacific journal of tropical medicine.Asian Pac J Trop Med.2014 Apr;7(4):293-6. doi: 10.1016/S1995-7645(14)60041-9.
- OBJECTIVE: To investigate the effect of vascular endothelial growth factor (VEGF), P53 and telomerase on angiogenesis in gastric carcinoma tissue.METHODS: A total of 95 surgical resection samples of gastric cancer tissue after pathological diagnosis are collected to observe the VEGF, P53 and telomer
- PMID 24507679
- PLEKHG2/FLJ00018, a Rho family-specific guanine nucleotide exchange factor, is tyrosine phosphorylated via the EphB2/cSrc signaling pathway.
- Sato K1, Suzuki T2, Yamaguchi Y3, Kitade Y4, Nagase T3, Ueda H5.Author information 1United Graduate School of Drug Discovery and Medical Information Sciences, Gifu University, Yanagido, Gifu 501-1193, Japan.2Department of Chemistry and Biomolecular Science, Faculty of Engineering, Gifu University, Yanagido, Gifu 501-1193, Japan.3Kazusa DNA Research Institute, Kisarazu, Chiba 292-0818, Japan.4United Graduate School of Drug Discovery and Medical Information Sciences, Gifu University, Yanagido, Gifu 501-1193, Japan; Department of Chemistry and Biomolecular Science, Faculty of Engineering, Gifu University, Yanagido, Gifu 501-1193, Japan.5United Graduate School of Drug Discovery and Medical Information Sciences, Gifu University, Yanagido, Gifu 501-1193, Japan; Department of Chemistry and Biomolecular Science, Faculty of Engineering, Gifu University, Yanagido, Gifu 501-1193, Japan. Electronic address: hueda@gifu-u.ac.jp.AbstractPLEKHG2/FLJ00018, a Rho family-specific guanine nucleotide exchange factor (RhoGEF), is activated by heterotrimeric GTP-binding protein (G protein) Gβγ subunits, and in turn activates the small G protein Rac and Cdc42, which have been shown to mediate signaling pathways leading to actin cytoskeletal reorganization. In the present study, we show that co-expression of the constitutively active mutant of cSrc, a non-receptor tyrosine kinase, and PLEKHG2 induced the tyrosine phosphorylation of PLEKHG2 in HEK293 cells. Through deletion and base substitution mutagenesis we have identified Tyr489 of PLEKHG2 as the site phosphorylated by cSrc. Furthermore, using a high-throughput src homology 2 (SH2) domain binding assay, the SH2 domain of ABL1 and the PI 3-kinse regulator subunit (PIK3R3) were identified as candidates for the binding partner of tyrosine-phosphorylated PLEKHG2. The interaction between PLEKHG2 and the full-length of PIK3R3, but not ABL1, occurs in a tyrosine-phosphorylation-dependent manner. Furthermore, PLEKHG2 is tyrosine phosphorylated at Tyr489 by ephrinB2 receptor signaling via cSrc. Investigation of the physiological function of tyrosine phosphorylation at Tyr489 in PLEKHG2 remains a subject for future studies.
- Cellular signalling.Cell Signal.2014 Apr;26(4):691-6. doi: 10.1016/j.cellsig.2013.12.006. Epub 2013 Dec 27.
- PLEKHG2/FLJ00018, a Rho family-specific guanine nucleotide exchange factor (RhoGEF), is activated by heterotrimeric GTP-binding protein (G protein) Gβγ subunits, and in turn activates the small G protein Rac and Cdc42, which have been shown to mediate signaling pathways leading to actin cytoskelet
- PMID 24378532
- Identification of Genes Required by Bacillus thuringiensis for Survival in Soil by Transposon-Directed Insertion Site Sequencing.
- Bishop AH, Rachwal PA, Vaid A.Author information Detection Department, Defence Science and Technology Laboratory, Porton Down, Salisbury, Wiltshire, SP4 0JQ, UK, AHBishop@dstl.gov.uk.AbstractTransposon-directed insertion site sequencing was used to identify genes required by Bacillus thuringiensis to survive in non-axenic plant/soil microcosms. A total of 516 genetic loci fulfilled the criteria as conferring survival characteristics. Of these, 127 (24.6 %) were associated with uptake and transport systems; 227 loci (44.0 %) coded for enzymatic properties; 49 (9.5 %) were gene regulation or sensory loci; 40 (7.8 %) were structural proteins found in the cell envelope or had enzymatic activities related to it and 24 (4.7 %) were involved in the production of antibiotics or resistance to them. Eighty-three (16.1 %) encoded hypothetical proteins or those of unknown function. The ability to form spores was a key survival characteristic in the microcosms: bacteria, inoculated in either spore or vegetative form, were able to multiply and colonise the soil, whereas a sporulation-deficient mutant was not. The presence of grass seedlings was critical to colonisation. Bacteria labelled with green fluorescent protein were observed to adhere to plant roots. The sporulation-specific promoter of spo0A, the key regulator of sporulation, was strongly activated in the rhizosphere. In contrast, the vegetative-specific promoters of spo0A and PlcR, a pleiotropic regulator of genes with diverse activities, were only very weakly activated.
- Current microbiology.Curr Microbiol.2014 Apr;68(4):477-85. doi: 10.1007/s00284-013-0502-7. Epub 2013 Dec 6.
- Transposon-directed insertion site sequencing was used to identify genes required by Bacillus thuringiensis to survive in non-axenic plant/soil microcosms. A total of 516 genetic loci fulfilled the criteria as conferring survival characteristics. Of these, 127 (24.6 %) were associated with uptake a
- PMID 24310935
Japanese Journal
- 酵素変異体に基づくタンパク質ラベル化技術の開発と新たな生物学研究ツールへの展開 (特集 生化学に新たな視点を与える技術の開発とその応用)
- 新進気鋭シリーズ 第49回 日本生物物理学会年会 若手招待講演 Gタンパク質共役受容体オプシンとその構成的活性化変異体の構造ダイナミクス
- Molecular Simulation Analysis of the Structure Complex of C2 Domains of DKK Family Members and β-propeller Domains of LRP5/6:Explaining Why DKK3 Does Not Bind to LRP5/6
- Fujii Yasuyuki,Hoshino Tyuji,Kumon Hiromi
- Acta Medica Okayama 68(2), 63-78, 2014-04
- … Dickkopf (DKK) proteins interact with low-density lipoprotein receptor-related protein 5/6 (LRP5/6) to modulate WNT signaling. … The interaction is mediated by a cysteine-rich domain (C2) in the DKK protein and β-propeller domains (PD) of LRP5/6. … To determine why DKK3 does not bind to the receptor domains, we performed a molecular modeling simulation study including homology modeling, protein-protein docking and molecular dynamics (MD). …
- NAID 120005425629
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- 英
- mutant protein、mutein
- 関
- ムテイン、変異タンパク、変異蛋白質、変異蛋白
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- 英
- mutant protein
- 関
- 変異タンパク質、変異タンパク、変異蛋白質
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- 英
- mutant protein
- 関
- 変異タンパク質、変異タンパク、変異蛋白
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- 英
- mutant protein
- 関
- 変異タンパク質、変異蛋白質、変異蛋白
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- 関
- mutant protein
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