WordNet
- territory over which rule or control is exercised; "his domain extended into Europe"; "he made it the law of the land" (同)demesne, land
- (mathematics) the set of values of the independent variable for which a function is defined (同)domain of a function
- of or relating to cytoplasm (同)cytoplasmatic
- the protoplasm of a cell excluding the nucleus; is full of proteins that control cell metabolism (同)cytol
PrepTutorEJDIC
- (国の)領地,領土;(個人の)所有地 / (関心・活動などの)範囲,分野 / (個人・一族の)所有地 / (数学で)変域(関数の独立変数がとる値の集合)
- 細胞質の
- 細胞質
UpToDate Contents
全文を閲覧するには購読必要です。 To read the full text you will need to subscribe.
- 1. インスリン受容体の構造および機能 structure and function of the insulin receptor
- 2. T細胞受容体シグナル伝達 t cell receptor signaling
- 3. 赤血球細胞膜の動態および機構 red blood cell membrane dynamics and organization
- 4. アポトーシスと自己免疫疾患 apoptosis and autoimmune disease
- 5. ペプチドホルモンのシグナル伝達および調節 peptide hormone signal transduction and regulation
English Journal
- Potential Role of Voltage-Sensing Phosphatases in Regulation of Cell Structure Through the Production of PI(3,4)P2.
- Yamaguchi S, Kurokawa T, Taira I, Aoki N, Sakata S, Okamura Y, Homma KJ.Author information Faculty of Pharmaceutical Sciences, Department of Life and Health Sciences, Teikyo University, Tokyo, Japan.AbstractVoltage-sensing phosphatase, VSP, consists of the transmembrane domain, operating as the voltage sensor, and the cytoplasmic domain with phosphoinositide-phosphatase activities. The voltage sensor tightly couples with the cytoplasmic phosphatase and membrane depolarization induces dephosphorylation of several species of phosphoinositides. VSP gene is conserved from urochordate to human. There are some diversities among VSP ortholog proteins; range of voltage of voltage sensor motions as well as substrate selectivity. In contrast with recent understandings of biophysical mechanisms of VSPs, little is known about its physiological roles. Here we report that chick ortholog of VSP (designated as Gg-VSP) induces morphological feature of cell process outgrowths with round cell body in DF-1 fibroblasts upon its forced expression. Expression of the voltage sensor mutant, Gg-VSPR153Q with shifted voltage dependence to a lower voltage led to more frequent changes of cell morphology than the wild-type protein. Coexpression of PTEN that dephosphorylates PI(3,4)P2 suppressed this effect by Gg-VSP, indicating that the increase of PI(3,4)P2 leads to changes of cell shape. In addition, visualization of PI(3,4)P2 with the fluorescent protein fused with the TAPP1-derived pleckstrin homology (PH) domain suggested that Gg-VSP influenced the distribution of PI(3,4)P2 . These findings raise a possibility that one of the VSP's functions could be to regulate cell morphology through voltage-sensitive tuning of phosphoinositide profile. J. Cell. Physiol. 229: 422-433, 2014. © 2013 Wiley Periodicals, Inc.
- Journal of cellular physiology.J Cell Physiol.2014 Apr;229(4):422-33. doi: 10.1002/jcp.24463.
- Voltage-sensing phosphatase, VSP, consists of the transmembrane domain, operating as the voltage sensor, and the cytoplasmic domain with phosphoinositide-phosphatase activities. The voltage sensor tightly couples with the cytoplasmic phosphatase and membrane depolarization induces dephosphorylation
- PMID 24038012
- Molecular cloning and expression analysis of mannose receptor C type 1 in grass carp (Ctenopharyngodon idella).
- Wang L1, Liu L1, Zhou Y1, Zhao X1, Xi M1, Wei S1, Fang R1, Ji W1, Chen N1, Gu Z1, Liu X1, Wang W2, Asim M1, Liu X3, Lin L4.Author information 1Department of Aquatic Animal Medicine, College of Fisheries, Huazhong Agricultural University, Wuhan 430070, People's Republic of China.2Hubei Collaborative Innovation Center for Freshwater Aquaculture, Wuhan 430070, People's Republic of China; Key Lab of Freshwater Animal Breeding, Ministry of Agriculture, Wuhan 430070, People's Republic of China.3Department of Aquatic Animal Medicine, College of Fisheries, Huazhong Agricultural University, Wuhan 430070, People's Republic of China. Electronic address: liuxl@mail.hzau.edu.cn.4Department of Aquatic Animal Medicine, College of Fisheries, Huazhong Agricultural University, Wuhan 430070, People's Republic of China; Hubei Collaborative Innovation Center for Freshwater Aquaculture, Wuhan 430070, People's Republic of China; Key Lab of Freshwater Animal Breeding, Ministry of Agriculture, Wuhan 430070, People's Republic of China; State Key Laboratory of Agricultural Microbiology, Wuhan 430070, People's Republic of China. Electronic address: linli@mail.hzau.edu.cn.AbstractMannose receptor C type 1 (MRC1) is a pattern-recognition receptor (PRR) which plays a significant role in immune responses. Much work on MRC1 has been done in mammals and birds while little in fish. In this study, we cloned and characterized MRC1 in grass carp (gcMR). The full-length gcMR contained 5291bp encoding a putative protein of 1432 amino acids. The predicted amino acid sequences showed that gcMR contained a signal peptide, a cysteine-rich (CR) domain, a fibronectin type II (FN II) domain, eight C-type lectin-like domains (CTLDs), a transmembrane domain and a short cytoplasmic domain. gcMR were constitutively expressed in different organs with the higher expression in spleen and head kidney. During embryonic development, gcMR transcript levels were highest at cleavage stage. The up-regulation expression of gcMR, IL-1β and TNF-α in liver, spleen, head kidney and intestine after Aeromonas hydrophila infection indicating it involved in innate immune regulation during bacterial infections.
- Developmental and comparative immunology.Dev Comp Immunol.2014 Mar;43(1):54-8. doi: 10.1016/j.dci.2013.10.006. Epub 2013 Oct 31.
- Mannose receptor C type 1 (MRC1) is a pattern-recognition receptor (PRR) which plays a significant role in immune responses. Much work on MRC1 has been done in mammals and birds while little in fish. In this study, we cloned and characterized MRC1 in grass carp (gcMR). The full-length gcMR contained
- PMID 24184700
- Thermostable single domain antibody-maltose binding protein fusion for Bacillus anthracis spore protein BclA detection.
- Walper SA1, Battle SR2, Audrey Brozozog Lee P3, Zabetakis D1, Turner KB1, Buckley PE4, Calm AM4, Welsh HS4, Warner CR5, Zacharko MA5, Goldman ER1, Anderson GP6.Author information 1Center for Bio/Molecular Science and Engineering, Naval Research Laboratory, Washington, DC 20375, USA.2Clark Atlanta University, Atlanta, GA 30314, USA.3NOVA Research, Alexandria, VA 22308, USA.4Biosciences Division, U.S. Army Edgewood Chemical Biological Center, Aberdeen Proving Grounds, Edgewood, MD 21010, USA.5Excet, Springfield, VA 22151, USA.6Center for Bio/Molecular Science and Engineering, Naval Research Laboratory, Washington, DC 20375, USA. Electronic address: george.anderson@nrl.navy.mil.AbstractWe constructed a genetic fusion of a single domain antibody (sdAb) with the thermal stable maltose binding protein from the thermophile Pyrococcus furiosus (PfuMBP). Produced in the Escherichia coli cytoplasm with high yield, it proved to be a rugged and effective immunoreagent. The sdAb-A5 binds BclA, a Bacillus anthracis spore protein, with high affinity (KD∼50pM). MBPs, including the thermostable PfuMBP, have been demonstrated to be excellent folding chaperones, improving production of many recombinant proteins. A three-step purification of E. coli shake flask cultures of PfuMBP-sdAb gave a yield of approximately 100mg/L highly purified product. The PfuMBP remained stable up to 120°C, whereas the sdAb-A5 portion unfolded at approximately 68 to 70°C but could refold to regain activity. This fusion construct was stable to heating at 1mg/ml for 1h at 70°C, retaining nearly 100% of its binding activity; nearly one-quarter (24%) activity remained after 1h at 90°C. The PfuMBP-sdAb construct also provides a stable and effective method to coat gold nanoparticles. Most important, the construct was found to provide enhanced detection of B. anthracis Sterne strain (34F2) spores relative to the sdAb-A5 both as a capture reagent and as a detection reagent.
- Analytical biochemistry.Anal Biochem.2014 Feb 15;447:64-73. doi: 10.1016/j.ab.2013.10.031. Epub 2013 Oct 30.
- We constructed a genetic fusion of a single domain antibody (sdAb) with the thermal stable maltose binding protein from the thermophile Pyrococcus furiosus (PfuMBP). Produced in the Escherichia coli cytoplasm with high yield, it proved to be a rugged and effective immunoreagent. The sdAb-A5 binds Bc
- PMID 24184358
Japanese Journal
- Ultrastructure of Cytoplasmic Matrix
- Journal of Integrated Creative Studies 1(1), 1-19, 2015-03-10
- NAID 120005650266
- Proteomic profiling of antigens in circulating immune complexes associated with each of seven autoimmune diseases
- Clinical Biochemistry 48(3), 181-185, 2015-02
- NAID 120005553907
- Cytoplasmic Fragment of Alcadein alpha Generated by Regulated Intramembrane Proteolysis Enhances Amyloid beta-Protein Precursor (APP) Transport into the Late Secretory Pathway and Facilitates APP Cleavage
- Journal of biological chemistry 290(2), 987-995, 2015-01-09
- NAID 120005567733
Related Links
- INTRODUCTION. Integrin adhesion receptors are heterodimers of α and β subunits that contain a large extracellular domain responsible for ligand binding, a single transmembrane domain and a cytoplasmic domain that in most cases ...
- The intracellular (or cytoplasmic) domain of the receptor interacts with the interior of the cell or organelle, relaying the signal. ... The intracellular domain communicates via specific protein-protein-interactions with effector proteins, which in turn ...
Related Pictures
★リンクテーブル★
| リンク元 | 「細胞質領域」 |
| 関連記事 | 「cytoplasmic」「domain」「domains」 |
「細胞質領域」
「cytoplasmic」
- 細胞質の、細胞質内の、細胞質側の、原形質の
「domain」
- n.
「domains」
- 関
- See also specific type