WordNet

fasten or secure with chains; "Chain the chairs together"
a unit of length
a necklace made by a stringing objects together; "a string of beads"; "a strand of pearls"; (同)string, strand
a linked or connected series of objects; "a chain of daisies"
a series of (usually metal) rings or links fitted into one another to make a flexible ligament
anything that acts as a restraint
(chemistry) a series of linked atoms (generally in an organic molecule) (同)chemical chain
a series of things depending on each other as if linked together; "the chain of command"; "a complicated concatenation of circumstances" (同)concatenation
(business) a number of similar establishments (stores or restaurants or banks or hotels or theaters) under one ownership
connect or arrange into a chain by linking
first in order of importance; "the alpha male in the group of chimpanzees"; "the alpha star in a constellation is the brightest or main star"
the 1st letter of the Greek alphabet
the beginning of a series or sequence; "the Alpha and Omega, the first and the last, the beginning and the end"--Revelations
early testing stage of a software or hardware product; "alpha version"
British biochemist (born in Germany) who isolated and purified penicillin, which had been discovered in 1928 by Sir Alexander Fleming (1906-1979) (同)Ernst Boris Chain, Sir Ernst Boris Chain
bound with chains; "enchained demons strained in anger to gnaw on his bones"; "prisoners in chains" (同)enchained
any high mountain

PrepTutorEJDIC

『鎖』;(装飾用の)鎖 / 《複数形で》『束縛』,拘束;囚人をつなぐ鎖 / (物事の)『連続』,つながり《+『of』+『名』》 / (商店・銀行・ホテルなどの)チェーン(一連の店が同一資本のもとで連携して経営される方式;その店) / チェーン(測量で用いられる単位;約21.7m) / …'を'『鎖でつなぐ』《+『up』(『together』)+『名,』+『名』+『up』(『together』)》
アルファ(ギリシア語アルファベットの第1字A,α;英語のA,aに相当) / アルファ星(星座の主星)
高山,高峰

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1. 白血球粘着不全症 leukocyte adhesion deficiency
2. 心筋炎の病因および発症機序 etiology and pathogenesis of myocarditis
3. 拡張型心筋症の遺伝学 genetics of dilated cardiomyopathy
4. 成人におけるステロイド抵抗性およびステロイド依存性の潰瘍性大腸炎に対するアプローチ approach to adults with steroid refractory and steroid dependent ulcerative colitis
5. 成人における重症または難治性クローン病の内科的マネージメントの概要 overview of the medical management of severe or refractory crohn disease in adults

English Journal

STRIPAK complexes: Structure, biological function, and involvement in human diseases.

Hwang J1, Pallas DC2.Author information 1Department of Biochemistry and Winship Cancer Institute, and Biochemistry, Cell, Developmental Biology Graduate Program, Emory University School of Medicine, 1510 Clifton Road, Atlanta, GA 30322, USA. Electronic address: jhwang8231@gmail.com.2Department of Biochemistry and Winship Cancer Institute, and Biochemistry, Cell, Developmental Biology Graduate Program, Emory University School of Medicine, 1510 Clifton Road, Atlanta, GA 30322, USA. Electronic address: dpallas@emory.edu.AbstractThe mammalian striatin family consists of three proteins, striatin, S/G2 nuclear autoantigen, and zinedin. Striatin family members have no intrinsic catalytic activity, but rather function as scaffolding proteins. Remarkably, they organize multiple diverse, large signaling complexes that participate in a variety of cellular processes. Moreover, they appear to be regulatory/targeting subunits for the major eukaryotic serine/threonine protein phosphatase 2A. In addition, striatin family members associate with germinal center kinase III kinases as well as other novel components, earning these assemblies the name striatin-interacting phosphatase and kinase (STRIPAK) complexes. Recently, there has been a great increase in functional and mechanistic studies aimed at identifying and understanding the roles of STRIPAK and STRIPAK-like complexes in cellular processes of multiple organisms. These studies have identified novel STRIPAK and STRIPAK-like complexes and have explored their roles in specific signaling pathways. Together, the results of these studies have sparked increased interest in striatin family complexes because they have revealed roles in signaling, cell cycle control, apoptosis, vesicular trafficking, Golgi assembly, cell polarity, cell migration, neural and vascular development, and cardiac function. Moreover, STRIPAK complexes have been connected to clinical conditions, including cardiac disease, diabetes, autism, and cerebral cavernous malformation. In this review, we discuss the expression, localization, and protein domain structure of striatin family members. Then we consider the diverse complexes these proteins and their homologs form in various organisms, emphasizing what is known regarding function and regulation. Finally, we explore possible roles of striatin family complexes in disease, especially cerebral cavernous malformation.
The international journal of biochemistry & cell biology.Int J Biochem Cell Biol.2014 Feb;47:118-48. doi: 10.1016/j.biocel.2013.11.021. Epub 2013 Dec 11.
The mammalian striatin family consists of three proteins, striatin, S/G2 nuclear autoantigen, and zinedin. Striatin family members have no intrinsic catalytic activity, but rather function as scaffolding proteins. Remarkably, they organize multiple diverse, large signaling complexes that participate
PMID 24333164

Synovial membrane protein expression differs between juvenile idiopathic arthritis subtypes in early disease.

Finnegan S, Robson J, Scaife C, McAllister C, Pennington SR, Gibson DS, Rooney ME.AbstractINTRODUCTION: Juvenile idiopathic arthritis (JIA) is the most common rheumatological disease of childhood with a prevalence of around 1 in 1000. Without appropriate treatment it can have devastating consequences including permanent disability from joint destruction and growth deformities. Disease aetiology remains unknown. Investigation of disease pathology at the level of the synovial membrane is required if we want to begin to understand the disease at the molecular and biochemical level. The synovial membrane proteome from early disease-stage, treatment naive JIA patients was compared between polyarticular and oligoarticular subgroups.
Arthritis research & therapy.Arthritis Res Ther.2014 Jan 13;16(1):R8. [Epub ahead of print]
INTRODUCTION: Juvenile idiopathic arthritis (JIA) is the most common rheumatological disease of childhood with a prevalence of around 1 in 1000. Without appropriate treatment it can have devastating consequences including permanent disability from joint destruction and growth deformities. Disease ae
PMID 24410838

A site for direct integrin αvβ6•uPAR interaction from structural modelling and docking.

Sowmya G1, Khan JM1, Anand S2, Ahn SB2, Baker MS2, Ranganathan S3.Author information 1Department of Chemistry and Biomolecular Sciences, Macquarie University, Sydney, NSW, Australia; ARC Centre of Excellence in Bioinformatics, Macquarie University, Sydney, NSW, Australia.2Department of Chemistry and Biomolecular Sciences, Macquarie University, Sydney, NSW, Australia.3Department of Chemistry and Biomolecular Sciences, Macquarie University, Sydney, NSW, Australia; ARC Centre of Excellence in Bioinformatics, Macquarie University, Sydney, NSW, Australia; Department of Biochemistry, Yong Loo Lin School of Medicine, National University of Singapore, Singapore. Electronic address: shoba.ranganathan@mq.edu.au.AbstractIntegrin αvβ6 is an epithelially-restricted heterodimeric transmembrane glycoprotein, known to interact with the urokinase plasminogen activating receptor (uPAR), playing a critical role in cancer progression. While the X-ray crystallographic structures of segments of other integrin heterodimers are known, there is no structural information for the complete αvβ6 integrin to assess its direct interaction with uPAR. We have performed structural analysis of αvβ6•uPAR interactions using model data with docking simulations to pinpoint their interface, in accord with earlier reports of the β-propeller region of integrin α-chain interacting with uPAR. Interaction of αvβ6•uPAR was demonstrated by our previous study using immunoprecipitation coupled with proteomic analysis by mass spectrometry. Recently this interaction was validated with proximity ligation assays and peptide arrays. The data suggested that two potential peptide regions from domain II and one peptide region from domain III of uPAR, interact with αvβ6 integrin. Only the peptide region from domain III is consistent with the three-dimensional interaction site proposed in this study. The molecular basis of integrin αvβ6•uPAR binding using structural data is discussed for its implications as a potential therapeutic target in cancer management.
Journal of structural biology.J Struct Biol.2014 Jan 11. pii: S1047-8477(14)00002-1. doi: 10.1016/j.jsb.2014.01.001. [Epub ahead of print]
Integrin αvβ6 is an epithelially-restricted heterodimeric transmembrane glycoprotein, known to interact with the urokinase plasminogen activating receptor (uPAR), playing a critical role in cancer progression. While the X-ray crystallographic structures of segments of other integrin heterodimers a
PMID 24423664

Japanese Journal

Effects of RGDS sequence genetically interfused in the silk fibroin light chain protein on chondrocyte adhesion and cartilage synthesis.

Biomaterials 31(29), 7503-7511, 2010-10
NAID 80021273775

Peptide-Chitosan Membrane Mimicking the Dual-Function of Laminin Alpha 1 Chain LG4 Module

Peptide science : proceedings of the ... Japanese Peptide Symposium 2007, 111-114, 2008-03-01
NAID 10021906704

Aggretin, a heterodimeric C-type lectin from Calloselasma rhodostoma (malayan pit viper), stimulates platelets by binding to alpha 2beta 1 integrin and glycoprotein Ib, activating Syk and phospholipase Cgamma 2, but does not involve the glycoprotein VI/Fc receptor gamma chain collagen receptor