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COLD SPRING HARBOR PERSPECTIVES IN MEDICINE, ISSN 2157-1422, 12/2018, Volume 8, Issue 12
MRAS is the closest relative to the classical RAS oncoproteins and shares most regulatory and effector interactions. However, it also has unique functions,... 
R-RAS | MEDICINE, RESEARCH & EXPERIMENTAL | NOONAN SYNDROME | CRYSTAL-STRUCTURE | NUCLEOTIDE EXCHANGE FACTOR | BINDING-PROTEIN | GENE-EXPRESSION | ACTIVATED M-RAS | NEURONAL DIFFERENTIATION | GROWTH-FACTOR | CELL POLARITY
Journal Article
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 02/2019, Volume 116, Issue 9, pp. 3536 - 3545
Journal Article
Oncogene, ISSN 0950-9232, 02/2002, Volume 21, Issue 9, pp. 1381 - 1390
Nore and RASSF1A are noncatalytic proteins that share 50% identity over their carboxyterminal 300 AA, a segment that encompasses a putative Ras-Rap association... 
RASSF1 | Ras | Tumor suppressor | Norel | Apoptosis | Nore1 | BIOCHEMISTRY & MOLECULAR BIOLOGY | tumor suppressor | apoptosis | M-RAS/R-RAS3 | IDENTIFICATION | FAMILY | CELL BIOLOGY | EFFECTOR | ONCOLOGY | PATHWAY | GENETICS & HEREDITY | DOMAINS
Journal Article
Journal Article
Microscopy, ISSN 0022-0744, 04/2018, Volume 67, Issue 2, pp. 68 - 74
Ratiometric image analysis demonstrated that M-Ras was concentrated in the membrane of forming phagosomes. Our analysis of M-Ras mutant expression showed that... 
Ratiometric imaging | Endocytosis | Live-cell imaging | Macrophages | FcγR-mediated phagocytosis | M-Ras GTPase | TARGET | CELLS | Fc gamma R-mediated phagocytosis | ACTIVATION | PROTEIN | R-RAS3 | PATTERNS | IDENTIFICATION | MICROSCOPY | ratiometric imaging | macrophages | live-cell imaging | MACROPINOCYTOSIS | GROWTH | endocytosis | RECEPTORS
Journal Article
PLoS ONE, ISSN 1932-6203, 10/2015, Volume 10, Issue 10, p. e0141493
Here we show that male, but not female mice lacking expression of the GTPase M-Ras developed urinary retention with distention of the bladder that exacerbated... 
BLADDER CONTRACTIONS | SMOOTH-MUSCLE | DETRUSOR MUSCLE | CYCLIC-AMP | OVERACTIVE BLADDER | M-RAS | MULTIDISCIPLINARY SCIENCES | CONSTITUTIVELY ACTIVE MUTANT | FUNCTIONAL-ROLE | GTPASE-ACTIVATING PROTEIN | M-2 RECEPTORS | Monomeric GTP-Binding Proteins - physiology | Receptor, Muscarinic M2 - genetics | Male | Receptor, Muscarinic M3 - physiology | Urinary Retention - genetics | Urinary Bladder - pathology | Receptor, Muscarinic M2 - physiology | Urinary Retention - physiopathology | RNA, Messenger - biosynthesis | Aging - genetics | Urinary Bladder, Overactive - physiopathology | Female | Receptor, Muscarinic M3 - biosynthesis | Urinary Incontinence - physiopathology | Urinary Bladder - metabolism | Mice, Inbred C57BL | Gene Expression Regulation | Monomeric GTP-Binding Proteins - genetics | Muscle, Smooth - metabolism | Proteinuria - genetics | Sex Characteristics | Receptor, Muscarinic M3 - genetics | Monomeric GTP-Binding Proteins - deficiency | Receptor, Muscarinic M2 - biosynthesis | Mice, Knockout | Proteinuria - physiopathology | Phenotype | Animals | Muscle Contraction | Aging - physiology | Urinary Bladder, Overactive - genetics | Urination - physiology | Mice | Urinary Incontinence - genetics | Acetylcholine - physiology | Urinary incontinence | Epinephrine | Care and treatment | Receptors | Physiological aspects | Development and progression | Research | Health sciences | Neurosciences | Nuclear magnetic resonance--NMR | Biomedical research | Acetylcholine receptors (muscarinic) | Bladder | Smooth muscle | Males | Retention | Urology | Proteins | Rodents | Physiology | Life sciences | Sexual dimorphism | Urogenital system | Age | Urine | Phenotypes | Abnormalities | Muscles | Muscle contraction | Carbachol | Fibrosis | Regulation | Females | Guanosinetriphosphatase | Nuclear magnetic resonance | NMR
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 11/2004, Volume 279, Issue 47, pp. 49488 - 49496
Journal Article