出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2012/12/10 03:21:10」(JST)[Wiki en表示]
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- 1. プロテインＳ欠乏症 protein s deficiency
- 2. 止血の概要 overview of hemostasis
- 3. 先天性血栓性素因のマネージメント management of inherited thrombophilia
- 4. 成人における門脈血栓症の疫学および病因 epidemiology and pathogenesis of portal vein thrombosis in adults
- 5. Factor V Leiden and activated protein C resistance: Clinical manifestations and diagnosis
- NMR mapping of protein conformational landscapes using coordinated behavior of chemical shifts upon ligand binding.
- Cembran A1, Kim J, Gao J, Veglia G.Author information 1Department of Biochemistry, Biophysics & Molecular Biology, University of Minnesota, 6-155 Jackson Hall, MN 55455, USA. email@example.com.AbstractProteins exist as an ensemble of conformers that are distributed on free energy landscapes resembling folding funnels. While the most stable conformers populate low energy basins, protein function is often carried out through low-populated conformational states that occupy high energy basins. Ligand binding shifts the populations of these states, changing the distribution of these conformers. Understanding how the equilibrium among the states is altered upon ligand binding, interaction with other binding partners, and/or mutations and post-translational modifications is of critical importance for explaining allosteric signaling in proteins. Here, we propose a statistical analysis of the linear trajectories of NMR chemical shifts (CONCISE, COordiNated ChemIcal Shifts bEhavior) for the interpretation of protein conformational equilibria. CONCISE enables one to quantitatively measure the population shifts associated with ligand titrations and estimate the degree of collectiveness of the protein residues' response to ligand binding, giving a concise view of the structural transitions. The combination of CONCISE with thermocalorimetric and kinetic data allows one to depict a protein's approximate conformational energy landscape. We tested this method with the catalytic subunit of cAMP-dependent protein kinase A, a ubiquitous enzyme that undergoes conformational transitions upon both nucleotide and pseudo-substrate binding. When complemented with chemical shift covariance analysis (CHESCA), this new method offers both collective response and residue-specific correlations for ligand binding to proteins.
- Physical chemistry chemical physics : PCCP.Phys Chem Chem Phys.2014 Apr 14;16(14):6508-18. doi: 10.1039/c4cp00110a. Epub 2014 Mar 7.
- Proteins exist as an ensemble of conformers that are distributed on free energy landscapes resembling folding funnels. While the most stable conformers populate low energy basins, protein function is often carried out through low-populated conformational states that occupy high energy basins. Ligand
- PMID 24604024
- Fibrin-based biomaterials: Modulation of macroscopic properties through rational design at the molecular level.
- Brown AC1, Barker TH2.Author information 1The School of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta, GA 30332, USA; The Wallace H. Coulter Department of Biomedical Engineering, Georgia Institute of Technology and Emory University, Atlanta, GA 30332, USA.2The Wallace H. Coulter Department of Biomedical Engineering, Georgia Institute of Technology and Emory University, Atlanta, GA 30332, USA; The Parker H. Petit Institute for Bioengineering and Biosciences, Georgia Institute of Technology, Atlanta, GA 30332, USA. Electronic address: firstname.lastname@example.org.AbstractFibrinogen is one of the primary components of the coagulation cascade and rapidly forms an insoluble matrix following tissue injury. In addition to its important role in hemostasis, fibrin acts as a scaffold for tissue repair and provides important cues for directing cell phenotype following injury. Because of these properties and the ease of polymerization of the material, fibrin has been widely utilized as a biomaterial for over a century. Modifying the macroscopic properties of fibrin, such as elasticity and porosity, has been somewhat elusive until recently, yet with a molecular-level rational design approach it can now be somewhat easily modified through alterations of molecular interactions key to the protein's polymerization process. This review outlines the biochemistry of fibrin and discusses methods for modification of molecular interactions and their application to fibrin based biomaterials.
- Acta biomaterialia.Acta Biomater.2014 Apr;10(4):1502-1514. doi: 10.1016/j.actbio.2013.09.008. Epub 2013 Sep 19.
- Fibrinogen is one of the primary components of the coagulation cascade and rapidly forms an insoluble matrix following tissue injury. In addition to its important role in hemostasis, fibrin acts as a scaffold for tissue repair and provides important cues for directing cell phenotype following injury
- PMID 24056097
- Non-pungency in a Japanese Chili Pepper Landrace (Capsicum annuum) is Caused by a Novel Loss-of-function Pun1 Allele
- The Horticulture Journal advpub(0), 2018
- NAID 130005153886
- Identification and Characterization of Plasma Membrane Intrinsic Protein (PIP) Aquaporin Genes in Petals of Opening Carnation Flowers
- The Horticulture Journal advpub(0), 2017
- NAID 130005152905
- プロテインS, protein S 測定方法 ： 抗原量：EIA法(SRL）, 遊離型抗原量：ラテックス凝集比濁法（LSIM)、活性（BML) 外注会社 ： SRL，LSIM（旧MCM）、BML 基準範囲 ： SRL 63～135%（抗原量）
- Consumer-friendly information about human genetics from the U.S. National Library of Medicine. ... Protein S deficiency is a disorder of blood clotting. People with this condition have an increased risk of developing abnormal blood ...
|拡張検索||「70-kDa ribosomal protein S6 kinase」「acyl-carrier protein S-malonyltransferase」「ribosomal protein S6」|
- 肺動脈弁狭窄症 pulmonary stenosis
- 肺動脈狭窄 pulmonic stenosis
- 活動指標 活動指数 performance status
- プロテインS protein S