- 関
- collagen type XIII、collagen XIII
WordNet
- write by means of a keyboard with types; "type the acceptance letter, please" (同)typewrite
- a small metal block bearing a raised character on one end; produces a printed character when inked and pressed on paper; "he dropped a case of type, so they made him pick them up"
- (biology) the taxonomic group whose characteristics are used to define the next higher taxon
- a subdivision of a particular kind of thing; "what type of sculpture do you prefer?"
- all of the tokens of the same symbol; "the word `element contains five different types of character"
- printed characters; "small type is hard to read"
- identify as belonging to a certain type; "Such people can practically be typed" (同)typecast
- a paste-up made by sticking together pieces of paper or photographs to form an artistic image; "he used his computer to make a collage of pictures superimposed on a map" (同)montage
- any collection of diverse things; "a collage of memories"
- a fibrous scleroprotein in bone and cartilage and tendon and other connective tissue; yields gelatin on boiling
- writing done with a typewriter (同)typewriting
PrepTutorEJDIC
- 〈C〉(…の)『型』,タイプ,類型,種類(kind)《+of+名》 / 〈C〉(その種類の特質を最もよく表している)『典型』,手本,模範《+of+名》 / 〈U〉《集合的に》活字;〈C〉(1個の)活字 / 〈U〉(印刷された)字体,活字 / 〈C〉(貨幣・メダルなどの)模様,図柄 / 〈C〉血液型(blood group) / …‘を'タイプに打つ / (…として)…‘を'分類する《+名+as+名(doing)》 / …‘の'型を決める / タイプライターを打つ
- コラージュ / 〈C〉画面に絵具以外のいろいろな素材を貼り付けて耕成した絵 / 〈U〉1の絵画技法
UpToDate Contents
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- 1. 止血の概要 overview of hemostasis
- 2. von Willebrand病の臨床症状および診断 clinical presentation and diagnosis of von willebrand disease
- 3. 手術室で使用される局所止血剤および組織接着剤の概要 overview of topical hemostatic agents and tissues adhesives used in the operating room
- 4. 遺伝性腎炎（アルポート症候群）の遺伝学、病因、および病理 genetics pathogenesis and pathology of hereditary nephritis alport syndrome
- 5. 遺伝性腎炎（アルポート症候群）の臨床症状、診断および治療 clinical manifestations diagnosis and treatment of hereditary nephritis alport syndrome
English Journal
- Strain history dependence of the nonlinear stress response of fibrin and collagen networks.
- Münster S, Jawerth LM, Leslie BA, Weitz JI, Fabry B, Weitz DA.Author information School of Engineering and Applied Sciences and Department of Physics, Harvard University, Cambridge, MA 02138, USA.AbstractWe show that the nonlinear mechanical response of networks formed from un-cross-linked fibrin or collagen type I continually changes in response to repeated large-strain loading. We demonstrate that this dynamic evolution of the mechanical response arises from a shift of a characteristic nonlinear stress-strain relationship to higher strains. Therefore, the imposed loading does not weaken the underlying matrices but instead delays the occurrence of the strain stiffening. Using confocal microscopy, we present direct evidence that this behavior results from persistent lengthening of individual fibers caused by an interplay between fiber stretching and fiber buckling when the networks are repeatedly strained. Moreover, we show that covalent cross-linking of fibrin or collagen inhibits the shift of the nonlinear material response, suggesting that the molecular origin of individual fiber lengthening may be slip of monomers within the fibers. Thus, a fibrous architecture in combination with constituents that exhibit internal plasticity creates a material whose mechanical response adapts to external loading conditions. This design principle may be useful to engineer novel materials with this capability.
- Proceedings of the National Academy of Sciences of the United States of America.Proc Natl Acad Sci U S A.2013 Jul 23;110(30):12197-202. doi: 10.1073/pnas.1222787110. Epub 2013 Jun 10.
- We show that the nonlinear mechanical response of networks formed from un-cross-linked fibrin or collagen type I continually changes in response to repeated large-strain loading. We demonstrate that this dynamic evolution of the mechanical response arises from a shift of a characteristic nonlinear s
- PMID 23754380
- Substrates of Factor XIII-A: roles in thrombosis and wound healing.
- Richardson VR, Cordell P, Standeven KF, Carter AM.Author information Division of Cardiovascular & Diabetes Research, Leeds Institute for Genetics Health & Therapeutics, Faculty of Medicine & Health, and Multidisciplinary Cardiovascular Research Centre, University of Leeds, Leeds, UK.AbstractFXIII (Factor XIII) is a Ca²+-dependent enzyme which forms covalent ϵ-(γ-glutamyl)lysine cross-links between the γ-carboxy-amine group of a glutamine residue and the ϵ-amino group of a lysine residue. FXIII was originally identified as a protein involved in fibrin clot stabilization; however, additional extracellular and intracellular roles for FXIII have been identified which influence thrombus resolution and tissue repair. The present review discusses the substrates of FXIIIa (activated FXIII) involved in thrombosis and wound healing with a particular focus on: (i) the influence of plasma FXIIIa on the formation of stable fibrin clots able to withstand mechanical and enzymatic breakdown through fibrin-fibrin cross-linking and cross-linking of fibrinolysis inhibitors, in particular α2-antiplasmin; (ii) the role of intracellular FXIIIa in clot retraction through cross-linking of platelet cytoskeleton proteins, including actin, myosin, filamin and vinculin; (iii) the role of intracellular FXIIIa in cross-linking the cytoplasmic tails of monocyte AT1Rs (angiotensin type 1 receptors) and potential effects on the development of atherosclerosis; and (iv) the role of FXIIIa on matrix deposition and tissue repair, including cross-linking of extracellular matrix proteins, such as fibronectin, collagen and von Willebrand factor, and the effects on matrix deposition and cell-matrix interactions. The review highlights the central role of FXIIIa in the regulation of thrombus stability, thrombus regulation, cell-matrix interactions and wound healing, which is supported by observations in FXIII-deficient humans and animals.
- Clinical science (London, England : 1979).Clin Sci (Lond).2013 Feb;124(3):123-37. doi: 10.1042/CS20120233.
- FXIII (Factor XIII) is a Ca²+-dependent enzyme which forms covalent ϵ-(γ-glutamyl)lysine cross-links between the γ-carboxy-amine group of a glutamine residue and the ϵ-amino group of a lysine residue. FXIII was originally identified as a protein involved in fibrin clot stabilization; however, a
- PMID 23075332
- Collagen XIII: a type II transmembrane protein with relevance to musculoskeletal tissues, microvessels and inflammation.
- Heikkinen A, Tu H, Pihlajaniemi T.Author information Center for Cell-Matrix Research and Biocenter Oulu, Department of Medical Biochemistry and Molecular Biology, PO Box 5000, 90014 University of Oulu, Finland. anne.heikkinen@oulu.fiAbstractCollagen XIII and the homologous collagens XXIII and XXV form a subgroup of type II transmembrane proteins within the collagen superfamily. Collagen XIII consists of a short cytosolic domain, a transmembrane domain and a large extracellular ectodomain, which may be shed into the pericellular matrix. It has been proposed that collagen XIII may function as an adhesion molecule, due to its cellular localization at focal contacts, numerous interactions with basement membrane (BM) and other extracellular matrix (ECM) proteins and expression at various cell-cell and cell-matrix junctions. Recent in vivo studies highlight its involvement in the development, differentiation and maturation of musculoskeletal tissues and vessels and in maintaining tissue integrity.
- The international journal of biochemistry & cell biology.Int J Biochem Cell Biol.2012 May;44(5):714-7. doi: 10.1016/j.biocel.2012.01.024. Epub 2012 Feb 8.
- Collagen XIII and the homologous collagens XXIII and XXV form a subgroup of type II transmembrane proteins within the collagen superfamily. Collagen XIII consists of a short cytosolic domain, a transmembrane domain and a large extracellular ectodomain, which may be shed into the pericellular matrix.
- PMID 22342189
Japanese Journal
- Studies on Pharmacological Activation of Human Immunoglobulin G by Chemical Modification and Active Subfragments. XIII. Effect of Carboxamidemethylated Fc Fragment (CM-Fc) on Type II Collagen-Induced Arthritis in DBA/1J Mice
- 三村 務,伊藤 正明,郷木 寛子,鈴木 信孝,竹内 勝義,辻川 和丈,小濱 靖弘
- Ｂｉｏｌｏｇｉｃａｌ ＆ Ｐｈａｒｍａｃｅｕｔｉｃａｌ Ｂｕｌｌｅｔｉｎ 17(5), 623-626, 1994-05-15
- … The effect of carboxamidemethylated Fc fragment (CM-Fc) from human immunoglobulin G (IgG) on type II collagen (C II)-induced arthritis (CIA) in DBA/1J mice was studied. … CM-Fc suppressed C II-induced delayed type hypersensitivity (DTH) in DBA/1J mice. …
- NAID 110003640604
- 初期胚着床部における接着性物質の局在に関する免疫組織学的研究
- 朝比奈 俊彦,小林 隆夫,寺尾 俊彦
- 1990-09-01
- … 方法:(1)ICR系雌マウスをPMS-hCGを用い過排卵処理し交配させ, 妊娠5日目に子宮を摘出しfibronectin (FN), laminin (LM), type IV collagen (C_<IV>), XIII因子subunit S (XIII_S)の染色を行った. …
- NAID 120005312533
- 初期胚着床部における接着性物質の局在に関する免疫組織学的研究
- 朝比奈 俊彦,小林 隆夫,寺尾 俊彦
- 日本産科婦人科學會雜誌 42(9), 1168-1174, 1990-09-01
- … 方法:(1)ICR系雌マウスをPMS-hCGを用い過排卵処理し交配させ, 妊娠5日目に子宮を摘出しfibronectin (FN), laminin (LM), type IV collagen (C_<IV>), XIII因子subunit S (XIII_S)の染色を行った. …
- NAID 110002105758
Related Links
- Type XIII collagen : characterization of ectodomain shedding and its biological implications in mammalian cells, characterization of type XIII collagen ... Tekijä: Väisänen, Marja-Riitta Organisaatiot: University of Oulu, Faculty of ...
- I wish to thank all the collageagues in our department, especially the members of the type XIII collagen group, but also others outside this group with whom I have worked during these years, for instance when teaching. Ph.D. Anne ...
Related Pictures
★リンクテーブル★
| リンク元 | 「XIII型コラーゲン」「collagen type XIII」 |
| 関連記事 | 「type」「typed」「typing」 |
「XIII型コラーゲン」
- 英
- type XIII collagen、collagen XIII、collagen type XIII
- 関
- コラーゲンXIII
「collagen type XIII」
- 関
- collagen XIII、type XIII collagen
「type」
- n.
- (windows)ファイル内容表示(linux -> cat])
- ex. type report_20111118.jp.htm | php a.php > report_20111118.jp.jp.jp.html
「typed」
- adj.
- 型の
「typing」
- n.
- タイプで打つこと、タイピング。分類