The Rap1 GTPase functions as a regulator of morphogenesis in vivo.
about
PDZ-GEF1, a guanine nucleotide exchange factor specific for Rap1 and Rap2The junctional multidomain protein AF-6 is a binding partner of the Rap1A GTPase and associates with the actin cytoskeletal regulator profilinPlexins function in epithelial repair in both Drosophila and zebrafish.Signaling of hepatocyte growth factor/scatter factor (HGF) to the small GTPase Rap1 via the large docking protein Gab1 and the adapter protein CRKLRequirement for C3G-dependent Rap1 activation for cell adhesion and embryogenesisThe small GTPase Rap1 promotes cell movement rather than stabilizes adhesion in epithelial cells responding to insulin-like growth factor I.The Crk signaling pathway contributes to the bombesin-induced activation of the small GTPase Rap1 in Swiss 3T3 cells.RAP-1 and the RAL-1/exocyst pathway coordinate hypodermal cell organization in Caenorhabditis elegansMesoderm migration in Drosophila is a multi-step process requiring FGF signaling and integrin activity.Radil controls neutrophil adhesion and motility through β2-integrin activation.Helicobacter pylori CagA induces Ras-independent morphogenetic response through SHP-2 recruitment and activation.Control of cell adhesion dynamics by Rap1 signaling.Rap1 is a potent activation signal for leukocyte function-associated antigen 1 distinct from protein kinase C and phosphatidylinositol-3-OH kinase.The small GTPase Rap1 is activated by turbulence and is involved in integrin [alpha]IIb[beta]3-mediated cell adhesion in human megakaryocytes.Drosophila PDZ-GEF, a guanine nucleotide exchange factor for Rap1 GTPase, reveals a novel upstream regulatory mechanism in the mitogen-activated protein kinase signaling pathway.Beyond the RING: CBL proteins as multivalent adapters.Novel Rap1 dominant-negative mutants interfere selectively with C3G and Epac.A Ral guanine exchange factor-Ral pathway is conserved in Drosophila melanogaster and sheds new light on the connectivity of the Ral, Ras, and Rap pathwaysActivation and function of the Rap1 GTPase in B lymphocytes.Presenilin-based genetic screens in Drosophila melanogaster identify novel notch pathway modifiers.A misexpression screen identifies genes that can modulate RAS1 pathway signaling in Drosophila melanogasterThe AF-6 homolog canoe acts as a Rap1 effector during dorsal closure of the Drosophila embryo.Global gene expression profiling of individual human oocytes and embryos demonstrates heterogeneity in early development.Adherens junctions: new insight into assembly, modulation and function.The Rap1-Rgl-Ral signaling network regulates neuroblast cortical polarity and spindle orientation.Impaired fertility and spermiogenetic disorders with loss of cell adhesion in male mice expressing an interfering Rap1 mutant.Fine-Tuning of the Actin Cytoskeleton and Cell Adhesion During Drosophila Development by the Unconventional Guanine Nucleotide Exchange Factors Myoblast City and Sponge.Small GTPase Rap1 Is Essential for Mouse Development and Formation of Functional Vasculature.Rap1 GTPase is required for mouse lens epithelial maintenance and morphogenesis.Ras-proximate-1 GTPase-activating protein and Rac2 may play pivotal roles in the initial development of myelodysplastic syndrome.Regulation of immune cell adhesion and migration by regulator of adhesion and cell polarization enriched in lymphoid tissues.The Rap GTPase activator Drosophila PDZ-GEF regulates cell shape in epithelial migration and morphogenesis.Rap1 promotes cell spreading by localizing Rac guanine nucleotide exchange factorsThe small GTPase Rap1 is a modulator of Hedgehog signaling.Defective angiogenesis, endothelial migration, proliferation, and MAPK signaling in Rap1b-deficient mice.Combinatorial interaction between CCM pathway genes precipitates hemorrhagic stroke.Distinct Rap1 activity states control the extent of epithelial invagination via α-catenin.Tumor cell migration and invasion are enhanced by depletion of Rap1 GTPase-activating protein (Rap1GAP)The Drosophila afadin homologue Canoe regulates linkage of the actin cytoskeleton to adherens junctions during apical constriction.Rap1a null mice have altered myeloid cell functions suggesting distinct roles for the closely related Rap1a and 1b proteins
P2860
Q22010969-A782F713-A751-4261-B2BC-6D97A0430972Q24671706-FB3C5A33-3481-4307-BA0D-61F09B6EDE0BQ27334767-86627510-6D17-460E-9180-069E6B492363Q28141139-2171AE0E-C407-4283-872B-820F635C98E6Q28343294-B051CA56-5AF6-4462-BBD6-803B2F6C05E0Q30009350-53806B08-C0AD-4F11-B669-15C9B35CE4A1Q30168471-306DC587-939A-4F10-9E72-F03E83AFFFD2Q30480845-BC91BA84-8807-4541-ADB7-117BECCCB9D1Q30494801-FBA7BEE4-B275-4F92-AB91-87369D08C74EQ30529775-DC934716-8D9E-4248-98D6-09208CCDF057Q33292148-BBDFCEC4-EE63-4B3F-8F1F-5A29944EB792Q33740476-14CEB519-567A-406F-9B13-571A67E683C1Q33786920-2E192451-9612-4B87-897A-4A9867B09F52Q34189999-3B381766-30C1-4758-BC05-A1CA573DB3A1Q34325514-D7CF6848-7267-4CCA-95AE-6D8688028914Q34405560-A749A643-2799-4ADA-B3F5-4A0E4EDE5535Q34414134-5E9ACB58-A5BB-4067-96FD-222B73A5C872Q34463200-FAEAC607-25F3-4D69-8E07-E7AC1673EA0BQ34577068-8D3318EF-7771-43C4-9BAD-7B96EF3C8BDDQ34588474-109781D2-42E1-4F66-A727-320B01026B46Q34610725-51D0FF62-F3D5-488B-A1A7-D44D26D907F7Q34618563-64B2966A-6B03-4B2F-8F30-F906E908DAA6Q34745404-E5BE3CB2-E476-40B7-8885-6D7AE6B110D0Q34811538-17E2DE1F-BFBB-4D76-98E7-0ABA71197ABDQ35670607-7AE47087-B998-49D3-8F8D-A6262CBADD9EQ35723724-37F3499A-E166-44F6-AA36-532B127A915AQ35821089-4A903514-548B-4674-A716-99E885D2D41FQ35880860-0183956E-7290-477F-BC11-EC52CF76F5AFQ36103500-57B7EC20-DF8E-4CDC-8F64-9581933AF3DCQ36110371-B13F5BF6-17CE-4112-B041-DC5B6BAC430DQ36257290-7875F0BF-5662-4C12-B928-CD358BFFC005Q36315901-1B3CDA4F-DED4-4123-961E-39BDF6A97AECQ36322667-BD8751D5-B5A3-4E35-8BA4-EF3F8DEB24D0Q36395540-EA25F151-4C3D-46B5-B66D-BEA7FD0B4035Q36478425-9DC1D6B5-6E3D-4F23-8DFD-4116CCD470EEQ36990464-4A728DB6-FD6A-435A-A060-542E34F199A9Q37089179-EE7A5AD1-F93D-4AB4-B9F5-6CA9BE30B4F9Q37112688-4D8614A7-817E-485E-BBFB-5E32D8644315Q37267715-428E38CD-A1AE-4A24-A1AE-5501A7E5C737Q37292561-142E3488-D25D-4C3F-811C-151E832653AE
P2860
The Rap1 GTPase functions as a regulator of morphogenesis in vivo.
description
1999 nî lūn-bûn
@nan
1999 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
The Rap1 GTPase functions as a regulator of morphogenesis in vivo.
@ast
The Rap1 GTPase functions as a regulator of morphogenesis in vivo.
@en
type
label
The Rap1 GTPase functions as a regulator of morphogenesis in vivo.
@ast
The Rap1 GTPase functions as a regulator of morphogenesis in vivo.
@en
prefLabel
The Rap1 GTPase functions as a regulator of morphogenesis in vivo.
@ast
The Rap1 GTPase functions as a regulator of morphogenesis in vivo.
@en
P2093
P2860
P356
P1433
P1476
The Rap1 GTPase functions as a regulator of morphogenesis in vivo.
@en
P2093
P2860
P304
P356
10.1093/EMBOJ/18.3.605
P407
P577
1999-02-01T00:00:00Z