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1. Full Text Rap1 in endothelial biology
by Chrzanowska-Wodnicka, Magdalena
Current Opinion in Hematology, ISSN 1065-6251, 02/2017, Volume 24, Issue 3, pp. 248 - 255
PURPOSE OF REVIEWUbiquitously-expressed small GTPase Rap1 is a key modulator of integrin- and cadherin-regulated processes. In endothelium, Rap1 promotes... 
vessel formation | endothelial homeostasis | shear stress sensing | signal transduction | mechanotransduction | ANGIOGENESIS | BARRIER FUNCTION | VASCULAR MORPHOGENESIS | CELL JUNCTIONS | SIGNALING PATHWAY | SHEAR-STRESS | VE-CADHERIN | SMALL GTPASE RAP1 | GROWTH-FACTOR | HEMATOLOGY | ZONULA ADHERENS | Inflammation - pathology | rap1 GTP-Binding Proteins - metabolism | Shear Strength | Signal Transduction | Endothelial Cells - metabolism | Stress, Physiological - genetics | Humans | Adherens Junctions - metabolism | Neovascularization, Pathologic - pathology | Inflammation - metabolism | Animals | Carrier Proteins - metabolism | Biomarkers | Protein Binding | Neovascularization, Pathologic - genetics | Microfilament Proteins - metabolism | Neovascularization, Pathologic - metabolism | Nitric Oxide - metabolism | Neovascularization, Physiologic
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2. Full Text KRIT-1/CCM1 Is a Rap1 Effector That Regulates Endothelial Cell-Cell Junctions
by Angela Glading and Jaewon Han and Rebecca A. Stockton and Mark H. Ginsberg
The Journal of Cell Biology, ISSN 0021-9525, 10/2007, Volume 179, Issue 2, pp. 247 - 254
Cerebral cavernous malformation (CCM), a disease associated with defective endothelial junctions, result from autosomal dominant CCM1 mutations that cause loss... 
Proteins | Intercellular junctions | Transfection | Small interfering RNA | Antibodies | Actins | Reports | Gene expression regulation | Physiological regulation | CHO cells | Endothelial cells | PATHOGENESIS | CEREBRAL CAVERNOUS MALFORMATIONS | ADHESION | PERMEABILITY | ANGIOGENESIS | KRIT1 | CCM1 | PROTEIN ICAP-1 | EPAC | ASSOCIATION | CELL BIOLOGY | Microtubule-Associated Proteins - chemistry | Protein Structure, Tertiary | Proto-Oncogene Proteins - metabolism | rap1 GTP-Binding Proteins - metabolism | Cricetinae | Cricetulus | KRIT1 Protein | Endothelial Cells - metabolism | Microtubule-Associated Proteins - metabolism | Antibodies, Monoclonal - pharmacology | Humans | Intercellular Junctions - metabolism | Protein Transport - drug effects | Proto-Oncogene Proteins - chemistry | Animals | Cattle | Endothelial Cells - cytology | Cell Membrane Permeability - drug effects | Protein Binding - drug effects | CHO Cells
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3. Full Text Activation of Rap1 promotes prostate cancer metastasis
by Bailey, Candice L and Kelly, Patrick and Casey, Patrick J
Cancer Research, ISSN 0008-5472, 06/2009, Volume 69, Issue 12, pp. 4962 - 4968
Elucidating the mechanisms of prostate cancer (Cap) survival and metastasis are critical to the discovery of novel therapeutic targets. The monomeric G protein... 
BREAST-CANCER | MIGRATION | ADHESION | INVASION | HETEROTRIMERIC G-PROTEINS | ONCOLOGY | PATHWAY | SQUAMOUS-CELL CARCINOMA | G12 FAMILY | BONE | TUMOR-GROWTH | Prostatic Neoplasms - metabolism | Prostatic Neoplasms - pathology | rap1 GTP-Binding Proteins - metabolism | Neoplasm Metastasis | RNA Interference | Neoplasm Invasiveness | Humans | Cell Line, Tumor | Male | Cell Adhesion | Cell Movement | migration | integrins | invasion | metastasis | Rap1
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4. Full Text Control of cell adhesion dynamics by Rap1 signaling
by Boettner, Benjamin and Van Aelst, Linda
Current Opinion in Cell Biology, ISSN 0955-0674, 2009, Volume 21, Issue 5, pp. 684 - 693
Individual cells in their particular environments adhere to the extracellular matrix (ECM) and their neighbours via integrin-containing and cadherin-containing... 
Internal Medicine | DROSOPHILA PDZ-GEF | INTEGRIN ALPHA-IIB-BETA-3 | CEREBRAL CAVERNOUS MALFORMATIONS | CYCLIC-AMP | CAENORHABDITIS-ELEGANS | EMBRYONIC STEM-CELLS | VASCULAR INTEGRITY | ADHERENS JUNCTIONS | ENDOTHELIAL BARRIER FUNCTION | MEDIATES RAP1-INDUCED ADHESION | CELL BIOLOGY | Gap Junctions - metabolism | rap1 GTP-Binding Proteins - metabolism | Animals | Signal Transduction | Guanine Nucleotide Exchange Factors - metabolism | Humans | Cell Adhesion
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5. Full Text Rap1 signalling: adhering to new models
by de Rooij, Johan and Bos, Johannes L and Reedquist, Kris A
Nature Reviews Molecular Cell Biology, ISSN 1471-0072, 05/2001, Volume 2, Issue 5, pp. 369 - 377
Ras-like GTPases are ubiquitously expressed, evolutionarily conserved molecular switches that couple extracellular signals to various cellular responses. Rap1,... 
REGULATED KINASES ERKS | R-RAS | NUCLEOTIDE-EXCHANGE FACTOR | FUNCTIONAL INTERACTION | RAS-RELATED GENE | MAP KINASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | GTPASE-ACTIVATING-PROTEIN | CAMP-DEPENDENT KINASE | B-RAF | NERVE GROWTH-FACTOR | CELL BIOLOGY | Amino Acid Sequence | Animals | rap1 GTP-Binding Proteins - physiology | rap1 GTP-Binding Proteins - chemistry | Humans | Molecular Sequence Data | Signal Transduction - physiology
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6. Full Text Ras and Rap1: A tale of two GTPases
by Shah, Seema and Brock, Ethan J and Ji, Kyungmin and Mattingly, Raymond R
Seminars in Cancer Biology, ISSN 1044-579X, 02/2019, Volume 54, pp. 29 - 39
Ras oncoproteins play pivotal roles in both the development and maintenance of many tumor types. Unfortunately, these proteins are difficult to directly target... 
Rap1Gap | Ras | ERK/MAPK | Rap1 | FTI | Metabolism | Cell-adhesion | EMT | Integrins | BLADDER-CARCINOMA ONCOGENE | BINDING-PROTEIN | GUANINE-NUCLEOTIDE EXCHANGE | ENDOTHELIAL BARRIER FUNCTION | FARNESYL-PROTEIN TRANSFERASE | SIGNAL-REGULATED KINASES | IN-VITRO | H-RAS | ONCOLOGY | HUMAN TUMOR-CELLS | AMINO-ACID 12 | Medical colleges | Therapeutics | Stem cells | Physiological aspects | Metastasis | G proteins | Mitogens | Protein kinases | Homeopathy | Materia medica and therapeutics
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7. Full Text Human RAP1 inhibits non‐homologous end joining at telomeres
by Sarthy, Jay and Bae, Nancy S and Scrafford, Jonathan and Baumann, Peter
The EMBO Journal, ISSN 0261-4189, 11/2009, Volume 28, Issue 21, pp. 3390 - 3399
Telomeres, the nucleoprotein structures at the ends of linear chromosomes, promote genome stability by distinguishing chromosome termini from DNA double‐strand... 
cancer | genome instability | DNA repair | telomeres | Genome instability | Telomeres | Cancer | MULTIPLE PATHWAYS | FISSION YEAST | PROTEIN | MAMMALIAN TELOMERES | DNA-DAMAGE RESPONSE | BIOCHEMISTRY & MOLECULAR BIOLOGY | LENGTH | BINDING DOMAIN | TRF2 | CELL BIOLOGY | DYSFUNCTIONAL TELOMERES | LOOPS | Genomic Instability | Gene Expression | Humans | DNA - metabolism | Telomere | DNA-Binding Proteins - metabolism | Schizosaccharomyces - metabolism | DNA Repair | Schizosaccharomyces pombe Proteins - metabolism | Telomeric Repeat Binding Protein 2 - metabolism | DNA Damage | HeLa Cells | Telomeric Repeat Binding Protein 2 - genetics | Telomere-Binding Proteins - metabolism | Molecular biology | Chromosomes | Genomics | DNA damage
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8. Full Text Vascular endothelial-cadherin stabilizes at cell-cell junctions by anchoring to circumferential actin bundles through α- and β-catenins in cyclic AMP-Epac-Rap1 signal-activated endothelial cells
by Noda, Kazuomi and Zhang, Jianghui and Fukuhara, Shigetomo and Kunimoto, Satoshi and Yoshimura, Michihiro and Mochizuki, Naoki
Molecular Biology of the Cell, ISSN 1059-1524, 02/2010, Volume 21, Issue 4, pp. 584 - 596
Vascular endothelial (VE)-cadherin is a cell-cell adhesion molecule involved in endothelial barrier functions. Previously, we reported that cAMP-Epac-Rap1... 
BARRIER DYSFUNCTION | F-ACTIN | ADHESION | COMPLEX | EPITHELIAL-CELLS | RAP1 EFFECTOR | VE-CADHERIN | SRC ACTIVITY | ADHERENS JUNCTIONS | EXCHANGE FACTORS | CELL BIOLOGY | RNA, Small Interfering - genetics | Platelet Endothelial Cell Adhesion Molecule-1 - genetics | Thiazolidines - metabolism | Cadherins - metabolism | Fluorescence Recovery After Photobleaching | alpha Catenin - metabolism | Humans | Actins - metabolism | Guanosine Triphosphate - metabolism | Antigens, CD - genetics | Recombinant Fusion Proteins - metabolism | Actins - genetics | Antigens, CD - metabolism | Colforsin - metabolism | Guanine Nucleotide Exchange Factors - metabolism | Platelet Endothelial Cell Adhesion Molecule-1 - metabolism | Cadherins - genetics | Cyclic AMP - metabolism | Bridged Bicyclo Compounds, Heterocyclic - metabolism | Cell Line | rap1 GTP-Binding Proteins - metabolism | Guanine Nucleotide Exchange Factors - genetics | Endothelial Cells - metabolism | Intercellular Junctions - metabolism | beta Catenin - metabolism | beta Catenin - genetics | Animals | Endothelial Cells - cytology | Cyclic AMP Response Element-Binding Protein - metabolism | Recombinant Fusion Proteins - genetics | Signal Transduction - physiology | alpha Catenin - genetics | rap1 GTP-Binding Proteins - genetics | RNA, Small Interfering - metabolism
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9. Full Text Rap1 ameliorates renal tubular injury in diabetic nephropathy
by Xiao, Li and Zhu, Xuejing and Yang, Shikun and Liu, Fuyou and Zhou, Zhiguang and Zhan, Ming and Xie, Ping and Zhang, Dongshan and Li, Jun and Song, Panai and Kanwar, Yashpal S and Sun, Lin
Diabetes, ISSN 0012-1797, 04/2014, Volume 63, Issue 4, pp. 1366 - 1380
Rap1b ameliorates high glucose (HG)-induced mitochondrial dysfunction in tubular cells. However, its role and precise mechanism in diabetic nephropathy (DN) in... 
PROTEIN-KINASE-C | OXIDATIVE STRESS | ACTIVATION | BIOGENESIS | PGC-1-ALPHA | ENDOCRINOLOGY & METABOLISM | DOWN-REGULATION | MITOCHONDRIAL DYSFUNCTION | RECEPTOR | HIGH-GLUCOSE | BETA | Cell Line | Kidney - drug effects | Kidney - pathology | Kidney Tubules - drug effects | Signal Transduction | Apoptosis - drug effects | Antioxidants - metabolism | Diabetic Nephropathies - metabolism | Humans | Rats | Male | Transcription Factors - antagonists & inhibitors | Mitochondria - drug effects | Rats, Sprague-Dawley | Animals | Diabetic Nephropathies - physiopathology | Peroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alpha | Oxidative Stress - drug effects | CCAAT-Enhancer-Binding Protein-beta - antagonists & inhibitors | Diabetes Mellitus, Experimental - metabolism | Kidney Tubules - metabolism | rap GTP-Binding Proteins - metabolism | Physiological aspects | Diabetic neuropathies | Mitochondria | Research | Analysis | Oncogenes | Complications
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10. Full Text Human Rap1 modulates TRF2 attraction to telomeric DNA
by Janoušková, Eliška and Nečasová, Ivona and Pavloušková, Jana and Zimmermann, Michal and Hluchý, Milan and Marini, Victoria and Nováková, Monika and Hofr, Ctirad
Nucleic Acids Research, ISSN 0305-1048, 03/2015, Volume 43, Issue 5, pp. 2691 - 2700
More than two decades of genetic research have identified and assigned main biological functions of shelterin proteins that safeguard telomeres. However, a... 
RECRUITMENT | PROTEIN | MAMMALIAN TELOMERES | PROTECTION | BIOCHEMISTRY & MOLECULAR BIOLOGY | LOOP | SHELTERIN | END | ATM | HOLLIDAY JUNCTIONS | BINDING | Surface Plasmon Resonance | Sodium Chloride - pharmacology | Humans | Spectrometry, Fluorescence | Telomeric Repeat Binding Protein 2 - chemistry | DNA - metabolism | Static Electricity | Binding, Competitive - drug effects | DNA - genetics | Telomere-Binding Proteins - genetics | DNA - chemistry | Protein Binding - drug effects | Telomeric Repeat Binding Protein 2 - metabolism | Telomere - metabolism | Telomere-Binding Proteins - chemistry | Kinetics | Telomeric Repeat Binding Protein 2 - genetics | Fluorescence Polarization | Telomere-Binding Proteins - metabolism | Telomere - genetics | Genome Integrity, Repair and
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11. Full Text Increased sugar uptake promotes oncogenesis via EPAC/RAP1 and O-GlcNAc pathways
by Onodera, Yasuhito and Nam, Jin-Min and Bissell, Mina J
Journal of Clinical Investigation, ISSN 0021-9738, 01/2014, Volume 124, Issue 1, pp. 367 - 384
There is a considerable resurgence of interest in the role of aerobic glycolysis in cancer; however, increased glycolysis is frequently viewed as a consequence... 
MEDICINE, RESEARCH & EXPERIMENTAL | GENE-EXPRESSION SIGNATURE | SOLUBLE ADENYLYL-CYCLASE | VIRUS-TRANSFORMED CELLS | GLUCOSE-METABOLISM | PYRUVATE-KINASE M2 | EPIDERMAL-GROWTH-FACTOR | RECONSTITUTED BASEMENT-MEMBRANE | EXTRACELLULAR-MATRIX | HUMAN BREAST CELLS | MAMMARY EPITHELIAL-CELLS | Up-Regulation | Humans | Glucose Transporter Type 3 - metabolism | Acetylglucosamine - metabolism | Breast Neoplasms - metabolism | Receptor, Epidermal Growth Factor - metabolism | Guanine Nucleotide Exchange Factors - metabolism | Female | Membrane Proteins - metabolism | Proto-Oncogene Proteins c-akt - metabolism | Telomere-Binding Proteins - metabolism | Oncogenes | Second Messenger Systems | Cell Line | Oxygen Consumption | Biosynthetic Pathways | Glycosylation | MAP Kinase Kinase Kinases - metabolism | Adenylyl Cyclases - metabolism | Cell Transformation, Neoplastic - metabolism | Integrin beta1 - metabolism | Phenotype | Carrier Proteins - metabolism | Thyroid Hormones - metabolism | Glucose - metabolism | Glycolysis | Breast Neoplasms - mortality | Protein Processing, Post-Translational | Complications and side effects | Care and treatment | Patient outcomes | Physiological aspects | Development and progression | Research | Carcinogenesis | Risk factors | Integrins | Medical research | Dehydrogenases | Metabolites | Cloning | Breast cancer | Glucose | Metabolism | Gene expression
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