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Wyszukujesz frazę ""Protein-Tyrosine Kinases metabolism"" wg kryterium: Temat


Tytuł :
Janus kinase (Jak) subcellular localization revisited: the exclusive membrane localization of endogenous Janus kinase 1 by cytokine receptor interaction uncovers the Jak.receptor complex to be equivalent to a receptor tyrosine kinase
Index Terms :
Cell Line
Receptors, Cytokine/metabolism
Receptor Protein-Tyrosine Kinases/metabolism
Proto-Oncogene Proteins/metabolism
Protein-Tyrosine Kinases/metabolism
Protein Binding
Janus Kinase 2
Janus Kinase 1
Humans
Enzyme Activation
Cell Membrane/metabolism
Signal Transduction
info:eu-repo/semantics/article
URL :
http://orbilu.uni.lu/handle/10993/788">http://orbilu.uni.lu/handle/10993/788
Zasób elektroniczny
Tytuł :
Janus kinase (Jak) subcellular localization revisited: the exclusive membrane localization of endogenous Janus kinase 1 by cytokine receptor interaction uncovers the Jak.receptor complex to be equivalent to a receptor tyrosine kinase
Index Terms :
Cell Line
Receptors, Cytokine/metabolism
Receptor Protein-Tyrosine Kinases/metabolism
Proto-Oncogene Proteins/metabolism
Protein-Tyrosine Kinases/metabolism
Protein Binding
Janus Kinase 2
Janus Kinase 1
Humans
Enzyme Activation
Cell Membrane/metabolism
Signal Transduction
info:eu-repo/semantics/article
URL :
http://orbilu.uni.lu/handle/10993/788">http://orbilu.uni.lu/handle/10993/788
Zasób elektroniczny
Tytuł :
Janus kinase (Jak) subcellular localization revisited: the exclusive membrane localization of endogenous Janus kinase 1 by cytokine receptor interaction uncovers the Jak.receptor complex to be equivalent to a receptor tyrosine kinase
Index Terms :
Cell Line
Receptors, Cytokine/metabolism
Receptor Protein-Tyrosine Kinases/metabolism
Proto-Oncogene Proteins/metabolism
Protein-Tyrosine Kinases/metabolism
Protein Binding
Janus Kinase 2
Janus Kinase 1
Humans
Enzyme Activation
Cell Membrane/metabolism
Signal Transduction
info:eu-repo/semantics/article
URL :
http://orbilu.uni.lu/handle/10993/788">http://orbilu.uni.lu/handle/10993/788
Zasób elektroniczny
Tytuł :
Retraction Notice of the Article: The DYRK-family kinase Pom1 phosphorylates the F-BAR protein Cdc15 to prevent division at cell poles
Index Terms :
Actomyosin/metabolism; Cell Cycle Proteins/metabolism; Cell Division/physiology; Cytokinesis/physiology; Cytoskeletal Proteins/metabolism; GTP-Binding Proteins/metabolism; Phosphorylation/physiology; Protein Kinases/metabolism; Protein-Serine-Threonine Kinases/metabolism; Protein-Tyrosine Kinases/metabolism; Schizosaccharomyces/metabolism; Schizosaccharomyces pombe Proteins/metabolism
info:eu-repo/semantics/article
article
URL :
http://nbn-resolving.org/urn/resolver.pl?urn=urn:nbn:ch:serval-BIB_F2038D08BF680">http://nbn-resolving.org/urn/resolver.pl?urn=urn:nbn:ch:serval-BIB_F2038D08BF680
Zasób elektroniczny
Tytuł :
IFN-alpha5 mediates stronger Tyk2-stat-dependent activation and higher expression of 2',5'-oligoadenylate synthetase than IFN-alpha2 in liver cells
Index Terms :
2',5'-Oligoadenylate synthetase/metabolism
DNA-Binding proteins/metabolism
Hepatocytes/drug effects
Interferon-alpha/pharmacology
Protein-tyrosine kinases/metabolism
Trans-activators/metabolism
Article
info:eu-repo/semantics/article
URL :
http://hdl.handle.net/10171/23014">http://hdl.handle.net/10171/23014
http://online.liebertpub.com/doi/abs/10.1089/1079990041689601">http://online.liebertpub.com/doi/abs/10.1089/1079990041689601
Zasób elektroniczny
Tytuł :
SHIP2 multiple functions: a balance between a negative control of PtdIns(3,4,5)P₃ level, a positive control of PtdIns(3,4)P₂ production, and intrinsic docking properties.
Index Terms :
Sciences biomédicales
Animals
Cytoskeletal Proteins -- metabolism
Feedback, Physiological
Humans
Phosphatidylinositol Phosphates -- metabolism
Phosphoric Monoester Hydrolases -- metabolism
Phosphorylation
Protein Binding
Receptor Protein-Tyrosine Kinases -- metabolism
5-Phosphatase
Phosphatidylinositol metabolism
SHIP2
Signal transduction
info:eu-repo/semantics/article
info:ulb-repo/semantics/articlePeerReview
info:ulb-repo/semantics/openurl/article
URL :
http://hdl.handle.net/2013/ULB-DIPOT:oai:dipot.ulb.ac.be:2013/125509">http://hdl.handle.net/2013/ULB-DIPOT:oai:dipot.ulb.ac.be:2013/125509
http://worldcat.org/search?q=on:EQY+http://difusion-oai.ulb.ac.be/oai/request+DCG_ENTIRE_REPOSITORY+CNTCOLL">http://worldcat.org/search?q=on:EQY+http://difusion-oai.ulb.ac.be/oai/request+DCG_ENTIRE_REPOSITORY+CNTCOLL
Zasób elektroniczny
Tytuł :
EphB maintains dendritic spine morphology through focal adhesion kinase
Index Terms :
Animals
Dendritic Spines: physiology
Focal Adhesion Protein-Tyrosine Kinases: genetics
Focal Adhesion Protein-Tyrosine Kinases: metabolism
Models, Biological
Neurons: cytology
Receptors, Eph Family: physiology
Article
URL :
http://repository.ust.hk/ir/Record/1783.1-44872">http://repository.ust.hk/ir/Record/1783.1-44872
http://lbdiscover.ust.hk/uresolver?url_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rfr_id=info:sid/HKUST:SPI&rft.genre=article&rft.issn=1529-2401(online)&rft.volume=29&rft.issue=42&rft.date=2009&rft.spage=13091&rft.aulast=Chen&rft.aufirst=Yu&rft.atitle=EphB+maintains+dendritic+spine+morphology+through+focal+adhesion+kinase&rft.title=The+Journal+of+neuroscience+%3A+the+official+journal+of+the+Society+for+Neuroscience">http://lbdiscover.ust.hk/uresolver?url_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rfr_id=info:sid/HKUST:SPI&rft.genre=article&rft.issn=1529-2401(online)&rft.volume=29&rft.issue=42&rft.date=2009&rft.spage=13091&rft.aulast=Chen&rft.aufirst=Yu&rft.atitle=EphB+maintains+dendritic+spine+morphology+through+focal+adhesion+kinase&rft.title=The+Journal+of+neuroscience+%3A+the+official+journal+of+the+Society+for+Neuroscience
http://gateway.isiknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=LinksAMR&SrcApp=PARTNER_APP&DestLinkType=FullRecord&DestApp=WOS&KeyUT=000271002600001">http://gateway.isiknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=LinksAMR&SrcApp=PARTNER_APP&DestLinkType=FullRecord&DestApp=WOS&KeyUT=000271002600001
Zasób elektroniczny
Tytuł :
Tenascin-X induces cell detachment through p38 mitogen-activated protein kinase activation.
Index Terms :
Animals
Cell Adhesion/physiology
Cells, Cultured
Extracellular Matrix Proteins/metabolism
Fibroblasts/metabolism
Focal Adhesion Protein-Tyrosine Kinases/metabolism
Mice
Phosphorylation
Signal Transduction
Tenascin/metabolism
p38 Mitogen-Activated Protein Kinases/metabolism
499
article
URL :
http://hdl.handle.net/2115/53700">http://hdl.handle.net/2115/53700
http://dx.doi.org/10.1248/bpb.32.1795">http://dx.doi.org/10.1248/bpb.32.1795
Zasób elektroniczny
Tytuł :
Mechanism of the cross talk between growth hormone receptor and epidermal growth factor receptor
Index Terms :
Growth Hormone -- physiology Protein-Tyrosine Kinases -- metabolism Receptor, Epidermal Growth Factor -- metabolism Receptor Cross-Talk -- physiology
Text
Źródło :
Thesis (Ph.D.)--University of Alabama at Birmingham, 2008
URL :
http://contentdm.mhsl.uab.edu/cdm/ref/collection/etd/id/605">http://contentdm.mhsl.uab.edu/cdm/ref/collection/etd/id/605
http://worldcat.org/search?q=on:ABC+http://contentdm.mhsl.uab.edu/oai/oai.php+etd+CNTCOLL">http://worldcat.org/search?q=on:ABC+http://contentdm.mhsl.uab.edu/oai/oai.php+etd+CNTCOLL
http://worldcat.org/oclc/878068924/viewonline">http://worldcat.org/oclc/878068924/viewonline
Zasób elektroniczny
Tytuł :
Phosphorylated HER-2 tyrosine kinase and Her-2/neu gene amplification as predictive factors of response to trastuzumab in patients with HER-2 overexpressing metastatic breast cancer (MBC).
Index Terms :
Sciences bio-médicales et agricoles
Antibodies, Monoclonal -- therapeutic use
Antineoplastic Agents -- therapeutic use
Breast Neoplasms -- drug therapy
Breast Neoplasms -- genetics
Female
Gene Amplification
Genes, erbB-2 -- genetics
Humans
In Situ Hybridization, Fluorescence
Neoplasm Metastasis
Phosphorylation
Protein-Tyrosine Kinases -- genetics
Protein-Tyrosine Kinases -- metabolism
Receptor, erbB-2 -- metabolism
Retrospective Studies
Treatment Outcome
Metastatic breast cancer
Phosphorylated HER-2
Predictive factors
Trastuzumab
info:eu-repo/semantics/article
info:ulb-repo/semantics/articlePeerReview
info:ulb-repo/semantics/openurl/article
URL :
http://hdl.handle.net/2013/ULB-DIPOT:oai:dipot.ulb.ac.be:2013/54560">http://hdl.handle.net/2013/ULB-DIPOT:oai:dipot.ulb.ac.be:2013/54560
http://worldcat.org/search?q=on:EQY+http://difusion-oai.ulb.ac.be/oai/request+DCG_ENTIRE_REPOSITORY+CNTCOLL">http://worldcat.org/search?q=on:EQY+http://difusion-oai.ulb.ac.be/oai/request+DCG_ENTIRE_REPOSITORY+CNTCOLL
Zasób elektroniczny
Tytuł :
Coupling receptor tyrosine kinases to Rho GTPases--GEFs what's the link
Index Terms :
Cellular signal transduction
Guanine Nucleotide Exchange Factors/metabolism
Humans
Men
Pleckstrin homology domain
Receptor Protein-Tyrosine Kinases/metabolism
Receptor tyrosine kinase
Rho
Rho GEF
Rho GTPases
rho GTP-Binding Proteins/metabolism
Signal Transduction
Women
Life Sciences
Molecular Biology
Neurosciences
Structural Biology
Text
URL :
http://digitalscholarship.unlv.edu/sls_fac_articles/164">http://digitalscholarship.unlv.edu/sls_fac_articles/164
https://doi.org/10.1016/j.cellsig.2006.01.022">https://doi.org/10.1016/j.cellsig.2006.01.022
Zasób elektroniczny
Tytuł :
Regulated activating Thr172 phosphorylation of cyclin-dependent kinase 4(CDK4): its relationship with cyclins and CDK 'inhibitors'.
Index Terms :
Sciences bio-médicales et agricoles
Animals
Cells, Cultured
Cyclin-Dependent Kinase 4 -- analysis
Cyclin-Dependent Kinase 4 -- metabolism
Cyclin-Dependent Kinase Inhibitor p21 -- metabolism
Cyclin-Dependent Kinase Inhibitor p27 -- genetics
Cyclin-Dependent Kinase Inhibitor p27 -- metabolism
Cyclins -- metabolism
Cytoplasm -- enzymology
Dogs
Enzyme Activation
Humans
Nuclear Localization Signals -- genetics
Nuclear Localization Signals -- metabolism
Phosphorylation
Receptor Protein-Tyrosine Kinases -- metabolism
Serine -- metabolism
Threonine -- metabolism
info:eu-repo/semantics/article
info:ulb-repo/semantics/articlePeerReview
info:ulb-repo/semantics/openurl/article
URL :
http://hdl.handle.net/2013/ULB-DIPOT:oai:dipot.ulb.ac.be:2013/51525">http://hdl.handle.net/2013/ULB-DIPOT:oai:dipot.ulb.ac.be:2013/51525
http://worldcat.org/search?q=on:EQY+http://difusion-oai.ulb.ac.be/oai/request+DCG_ENTIRE_REPOSITORY+CNTCOLL">http://worldcat.org/search?q=on:EQY+http://difusion-oai.ulb.ac.be/oai/request+DCG_ENTIRE_REPOSITORY+CNTCOLL
Zasób elektroniczny

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