WordNet
- an enzyme that catalyzes the conversion of a proenzyme to an active enzyme
- an amino acid found in most proteins; a precursor of several hormones
- the basic unit of money in Papua New Guinea
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- 1. 慢性骨髄性白血病の治療の概要 overview of the treatment of chronic myeloid leukemia
- 2. 進行消化管間質腫瘍に対するチロシンキナーゼ阻害剤療法 tyrosine kinase inhibitor therapy for advanced gastrointestinal stromal tumors
- 3. 慢性骨髄性白血病に対するチロシンキナーゼ阻害剤の臨床使用 clinical use of tyrosine kinase inhibitors for chronic myeloid leukemia
- 4. 成人におけるフィラデルフィア染色体陽性急性リンパ芽球性白血病に対する導入療法 induction therapy for philadelphia chromosome positive acute lymphoblastic leukemia in adults
- 5. 未分化リンパ腫キナーゼ（ALK）融合癌遺伝子陽性非小細胞肺癌 anaplastic lymphoma kinase alk fusion oncogene positive non small cell lung cancer
English Journal
- Structural basis of recognition of interferon-α receptor by tyrosine kinase 2.
- Wallweber HJ, Tam C, Franke Y, Starovasnik MA, Lupardus PJ.Author information Department of Structural Biology, Genentech, South San Francisco, California, USA.AbstractTyrosine kinase 2 (TYK2) is a member of the Janus kinase (JAK) family of nonreceptor tyrosine kinases, which are essential for proper signaling in immune responses and development. Here we present a 2.0-Å-resolution crystal structure of a receptor-binding fragment of human TYK2, encompassing the FERM and SH2 domains, in complex with a so-called 'box2'-containing intracellular peptide motif from the interferon-α receptor chain 1 (IFNAR1). The TYK2-IFNAR1 interface reveals an unexpected receptor-binding mode that mimics a SH2 domain-phosphopeptide interaction, with a glutamate replacing the canonical phosphotyrosine residue. This structure provides the first view, to our knowledge, of a JAK in complex with its cognate receptor and defines the molecular logic through which JAKs have evolved to interact with divergent receptor sequences.
- Nature structural & molecular biology.Nat Struct Mol Biol.2014 Apr 6. doi: 10.1038/nsmb.2807. [Epub ahead of print]
- Tyrosine kinase 2 (TYK2) is a member of the Janus kinase (JAK) family of nonreceptor tyrosine kinases, which are essential for proper signaling in immune responses and development. Here we present a 2.0-Å-resolution crystal structure of a receptor-binding fragment of human TYK2, encompassing the FE
- PMID 24704786
- Inhibitory effects of heat shock protein 90 blockade on proinflammatory human Th1 and Th17 cell subpopulations.
- Tukaj S, Zillikens D, Kasperkiewicz M1.Author information 1Department of Dermatology, University of Lübeck, Ratzeburger Allee 160, 23538 Lübeck, Germany. Michael.Kasperkiewicz@uk-sh.de.AbstractBACKGROUND: Heat shock protein 90 (Hsp90), a chaperone that regulates activity of many client proteins responsible for cellular growth, differentiation, and apoptosis, has been proposed as an important clinical and preclinical therapeutic target in a number of malignancies and autoimmune diseases, respectively. In this study, we evaluated the effects of pharmacological Hsp90 inhibition on human proinflammatory T cell responses.
- Journal of inflammation (London, England).J Inflamm (Lond).2014 Apr 2;11(1):10. doi: 10.1186/1476-9255-11-10.
- BACKGROUND: Heat shock protein 90 (Hsp90), a chaperone that regulates activity of many client proteins responsible for cellular growth, differentiation, and apoptosis, has been proposed as an important clinical and preclinical therapeutic target in a number of malignancies and autoimmune diseases, r
- PMID 24694060
- The Capable ABL: What Is Its Biological Function?
- Wang JY.Author information Department of Medicine, Division of Hematology-Oncology, Moores Cancer Center, University of California, San Diego, La Jolla, California, USA.AbstractThe mammalian ABL1 gene encodes the ubiquitously expressed nonreceptor tyrosine kinase ABL. In response to growth factors, cytokines, cell adhesion, DNA damage, oxidative stress, and other signals, ABL is activated to stimulate cell proliferation or differentiation, survival or death, retraction, or migration. ABL also regulates specialized functions such as antigen receptor signaling in lymphocytes, synapse formation in neurons, and bacterial adhesion to intestinal epithelial cells. Although discovered as the proto-oncogene from which the Abelson leukemia virus derived its Gag-v-Abl oncogene, recent results have linked ABL kinase activation to neuronal degeneration. This body of knowledge on ABL seems confusing because it does not fit the one-gene-one-function paradigm. Without question, ABL capabilities are encoded by its gene sequence and that molecular blueprint designs this kinase to be regulated by subcellular location-dependent interactions with inhibitors and substrate activators. Furthermore, ABL shuttles between the nucleus and the cytoplasm where it binds DNA and actin-two biopolymers with fundamental roles in almost all biological processes. Taken together, the cumulated results from analyses of ABL structure-function, ABL mutant mouse phenotypes, and ABL substrates suggest that this tyrosine kinase does not have its own agenda but that, instead, it has evolved to serve a variety of tissue-specific and context-dependent biological functions.
- Molecular and cellular biology.Mol Cell Biol.2014 Apr;34(7):1188-97. doi: 10.1128/MCB.01454-13. Epub 2014 Jan 13.
- The mammalian ABL1 gene encodes the ubiquitously expressed nonreceptor tyrosine kinase ABL. In response to growth factors, cytokines, cell adhesion, DNA damage, oxidative stress, and other signals, ABL is activated to stimulate cell proliferation or differentiation, survival or death, retraction, or
- PMID 24421390
Japanese Journal
- Identification of a Novel SHP-2 Protein Tyrosine Phosphatase Inhibitor
- Bulletin of the Chemical Society of Japan 87(3), 420-424, 2014
- NAID 130004153283
- Effects of Halogenation on Tyrosine Phosphorylation and Peptide Binding to the Src Homology 2 Domain of Lymphocyte-Specific Protein Tyrosine Kinase
- Biological and Pharmaceutical Bulletin 35(3), 433-437, 2012
- NAID 130001872328
- Non-receptor Protein Tyrosine Kinase Fes as a Candidate for Anticancer Molecular Targeting Therapy
- Oncogene Proteins: Structure, Functions and Analyses, 209-221, 2008
- NAID 120002709178
Related Links
- Phosphorylation of proteins by nonreceptor tyrosine kinases is reversible, and often used to control intracellular signals to the nucleus by inducing conformational changes in the active binding site of the phosphorylated proteins ...
- The Oncologist is a journal devoted to medical and practice issues for surgical, radiation, and medical oncologists. ... I ntroduction The clinical development of targeted tyrosine kinase (TK) inhibitors for cancer treatment represents a ...
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★リンクテーブル★
| リンク元 | 「非受容体チロシンキナーゼ」「非受容体型チロシンキナーゼ」「非レセプター型チロシンキナーゼ」「非レセプター型チロシンリン酸化酵素」「non-receptor tyrosine kinase」 |
| 関連記事 | 「kinase」 |
「非受容体チロシンキナーゼ」
- 英
- nonreceptor tyrosine kinase、non-receptor tyrosine kinase
- 関
- 非レセプター型チロシンキナーゼ、非レセプター型チロシンリン酸化酵素、非受容体型チロシンキナーゼ
「非受容体型チロシンキナーゼ」
- 英
- nonreceptor tyrosine kinase、non-receptor tyrosine kinase
- 関
- 非レセプター型チロシンキナーゼ、非レセプター型チロシンリン酸化酵素、非受容体チロシンキナーゼ
「非レセプター型チロシンキナーゼ」
- 英
- nonreceptor tyrosine kinase、non-receptor tyrosine kinase
- 関
- 非レセプター型チロシンリン酸化酵素、非受容体チロシンキナーゼ、非受容体型チロシンキナーゼ