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  • 1
    Publication Date: 2019
    Description: 〈p〉RIT1 oncoproteins have emerged as an etiologic factor in Noonan syndrome and cancer. Despite the resemblance of RIT1 to other members of the Ras small guanosine triphosphatases (GTPases), mutations affecting RIT1 are not found in the classic hotspots but rather in a region near the switch II domain of the protein. We used an isogenic germline knock-in mouse model to study the effects of RIT1 mutation at the organismal level, which resulted in a phenotype resembling Noonan syndrome. By mass spectrometry, we detected a RIT1 interactor, leucine zipper–like transcription regulator 1 (LZTR1), that acts as an adaptor for protein degradation. Pathogenic mutations affecting either RIT1 or LZTR1 resulted in incomplete degradation of RIT1. This led to RIT1 accumulation and dysregulated growth factor signaling responses. Our results highlight a mechanism of pathogenesis that relies on impaired protein degradation of the Ras GTPase RIT1.〈/p〉
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    Electronic ISSN: 1095-9203
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  • 2
    Publication Date: 1998-02-21
    Description: Protein kinase B (PKB) is activated in response to phosphoinositide 3-kinases and their lipid products phosphatidylinositol 3,4, 5-trisphosphate [PtdIns(3,4,5)P3] and PtdIns(3,4)P2 in the signaling pathways used by a wide variety of growth factors, antigens, and inflammatory stimuli. PKB is a direct target of these lipids, but this regulation is complex. The lipids can bind to the pleckstrin homologous domain of PKB, causing its translocation to the membrane, and also enable upstream, Thr308-directed kinases to phosphorylate and activate PKB. Four isoforms of these PKB kinases were purified from sheep brain. They bound PtdIns(3,4,5)P3 and associated with lipid vesicles containing it. These kinases contain an NH2-terminal catalytic domain and a COOH-terminal pleckstrin homologous domain, and their heterologous expression augments receptor activation of PKB, which suggests they are the primary signal transducers that enable PtdIns(3,4,5)P3 or PtdIns- (3,4)P2 to activate PKB and hence to control signaling pathways regulating cell survival, glucose uptake, and glycogen metabolism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stephens, L -- Anderson, K -- Stokoe, D -- Erdjument-Bromage, H -- Painter, G F -- Holmes, A B -- Gaffney, P R -- Reese, C B -- McCormick, F -- Tempst, P -- Coadwell, J -- Hawkins, P T -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 1998 Jan 30;279(5351):710-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Inositide Laboratory, The Babraham Institute, Babraham, Cambridge CB2 4AT, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9445477" target="_blank"〉PubMed〈/a〉
    Keywords: 3-Phosphoinositide-Dependent Protein Kinases ; Alternative Splicing ; Amino Acid Sequence ; Animals ; Cell Line ; Cell Membrane/enzymology ; Cloning, Molecular ; DNA, Complementary ; Drosophila ; Drosophila Proteins ; Enzyme Activation ; Humans ; Liposomes/metabolism ; Molecular Sequence Data ; Open Reading Frames ; Phosphatidylinositol Phosphates/*metabolism ; Phosphorylation ; Platelet-Derived Growth Factor/pharmacology ; Protein-Serine-Threonine Kinases/chemistry/genetics/isolation & ; purification/*metabolism ; Proto-Oncogene Proteins/*metabolism ; Proto-Oncogene Proteins c-akt ; Rats ; Recombinant Proteins/metabolism ; Sheep ; *Signal Transduction
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1999-08-14
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉McCormick, D A -- New York, N.Y. -- Science. 1999 Jul 23;285(5427):541-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Section of Neurobiology, Yale University School of Medicine, New Haven, CT 06510, USA. david.mccormick@yale.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10447487" target="_blank"〉PubMed〈/a〉
    Keywords: Action Potentials ; Animals ; Brain/*physiology ; Calcium/metabolism ; Cerebral Cortex/physiology ; Ferrets ; Geniculate Bodies/*physiology ; Nerve Net/physiology ; Neural Pathways/physiology ; Neuronal Plasticity ; Neurons/physiology ; Retina/*physiology ; Sleep ; Visual Cortex/physiology ; Visual Pathways/*physiology
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    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1997-10-06
    Description: The inhibitory gamma-aminobutyric acid-containing (GABAergic) neurons of the thalamic reticular and perigeniculate nuclei are involved in the generation of normal and abnormal synchronized activity in thalamocortical networks. An important factor controlling the generation of activity in this system is the amplitude and duration of inhibitory postsynaptic potentials (IPSPs) in thalamocortical cells, which depend on the pattern of activity generated in thalamic reticular and perigeniculate cells. Activation of single ferret perigeniculate neurons generated three distinct patterns of GABAergic IPSPs in thalamocortical neurons of the dorsal lateral geniculate nucleus: Low-frequency tonic discharge resulted in small-amplitude IPSPs mediated by GABAA receptors, burst firing resulted in large-amplitude GABAA IPSPs, and prolonged burst firing activated IPSPs mediated by GABAA and GABAB receptors. These functional properties of GABAergic inhibition can reconfigure the operations of thalamocortical networks into patterns of activity associated with waking, slow-wave sleep, and generalized seizures.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kim, U -- Sanchez-Vives, M V -- McCormick, D A -- New York, N.Y. -- Science. 1997 Oct 3;278(5335):130-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Section of Neurobiology, Yale University School of Medicine, New Haven, CT 06510, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9311919" target="_blank"〉PubMed〈/a〉
    Keywords: Action Potentials ; Animals ; Bicuculline/analogs & derivatives/pharmacology ; Dendrites/physiology/ultrastructure ; Ferrets ; GABA Agonists/pharmacology ; GABA Antagonists/pharmacology ; Geniculate Bodies/cytology/physiology ; Glutamic Acid/pharmacology ; In Vitro Techniques ; Lysine/analogs & derivatives/pharmacology ; Neurons/*physiology/ultrastructure ; Organophosphorus Compounds/pharmacology ; Patch-Clamp Techniques ; Presynaptic Terminals/ultrastructure ; Receptors, GABA-A/*physiology ; Receptors, GABA-B/*physiology ; *Synaptic Transmission ; Thalamic Nuclei/cytology/*physiology ; gamma-Aminobutyric Acid/pharmacology/*physiology
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  • 5
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-04-26
    Description: Ras-GAP (GTPase activating protein) is a regulatory protein that stimulates the intrinsic guanosine triphosphatase (GTPase) activity of the proto-oncogene product p21ras. A domain of the neurofibromatosis gene product (NF1) that has sequence similarity to the catalytic domain of Ras-GAP and to yeast IRA gene products also has a specific stimulatory activity toward p21ras GTPase. Arachidonic acid and phosphatidic acid inactivate GAP, but no agents have been identified that stimulate GAP and thereby switch p21ras off. With the use of recombinant Ha-c-Ras and Ras-GAP, NF1, and GAP catalytic domains, it was found that prostaglandins PGF2 alpha and PGA2 stimulated Ras-GAP and that prostacyclin PGI2 inhibited Ras-GAP. The stimulatory effect of PGF2 alpha was saturable and structure-specific and competed with the inhibitory effect of arachidonic acid. Arachidonic acid also inhibited the catalytic activity of NF1, but prostaglandins were not stimulatory. These results suggest a mechanism for the allosteric control of Ras function through the modulation of arachidonate metabolism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Han, J W -- McCormick, F -- Macara, I G -- CA 38888/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1991 Apr 26;252(5005):576-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biophysics, University of Rochester Medical Center, NY 14642.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1902323" target="_blank"〉PubMed〈/a〉
    Keywords: Arachidonic Acid ; Arachidonic Acids/pharmacology ; Dinoprost/pharmacology ; GTP Phosphohydrolases/metabolism ; GTPase-Activating Proteins ; Gene Expression Regulation/drug effects ; Genes, ras/*drug effects ; Guanosine Triphosphate/metabolism ; Humans ; Kinetics ; Neurofibromatosis 1/genetics ; Neurofibromin 1 ; Prostaglandins/*pharmacology ; Proteins/*genetics ; Proto-Oncogene Proteins p21(ras)/metabolism ; Recombinant Proteins/metabolism ; ras GTPase-Activating Proteins
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  • 6
    Publication Date: 1992-01-10
    Description: The interaction between the low molecular weight G protein ras p21 and a guanosine triphosphatase activating protein (GAP) uncouples a heterotrimeric G protein (Gk) from muscarinic receptors. Through the use of isolated atrial cell membranes and genetically engineered GAP deletion mutants, the src homology regions (SH2-SH3) at the amino terminus of GAP have been identified as the domains responsible for this effect. Deletion of the domain required to stimulate the guanosine triphosphatase activity of ras p21 relieves the requirement for ras p21 in this system. A model is presented that suggests that ras p21 induces a conformational change in GAP, which allows the SH2-SH3 regions of GAP to function.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Martin, G A -- Yatani, A -- Clark, R -- Conroy, L -- Polakis, P -- Brown, A M -- McCormick, F -- CA51992-01/CA/NCI NIH HHS/ -- HL36930/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1992 Jan 10;255(5041):192-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Cetus Corporation, Emeryville, CA 94608.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1553544" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Baculoviridae ; Cell Membrane/metabolism ; Cells, Cultured ; Cloning, Molecular ; GTP-Binding Proteins/*physiology ; GTPase-Activating Proteins ; Genetic Engineering ; Genetic Vectors ; Guanosine 5'-O-(3-Thiotriphosphate)/pharmacology ; Guanosine Triphosphate/pharmacology ; Guinea Pigs ; Heart/*physiology ; Heart Atria ; Models, Biological ; Polymerase Chain Reaction ; Potassium Channels/drug effects/*physiology ; Proteins/genetics/*physiology ; Proto-Oncogene Proteins p21(ras)/*metabolism ; Receptors, Muscarinic/drug effects/*physiology ; ras GTPase-Activating Proteins
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  • 7
    Publication Date: 1990-07-13
    Description: Krev-1 is known to suppress transformation by ras. However, the mechanism of the suppression is unclear. The protein product of Krev-1, Rap1A-p21, is identical to Ras-p21 proteins in the region where interaction with guanosine triphosphatase (GTPase) activating protein (GAP) is believed to occur. Therefore, the ability of GAP to interact with Rap1A-p21 was tested. Rap1A-p21 was not activated by GAP but bound tightly to GAP and was an effective competitive inhibitor of GAP-mediated Ras-GTPase activity. Binding of GAP to Rap1A-p21 was strictly guanosine triphosphate (GTP)-dependent. The ability of Rap1A-p21 to bind tightly to GAP may account for Krev-1 suppression of transformation by ras. This may occur by preventing interaction of GAP with Ras-p21 or with other cellular proteins necessary for GAP-mediated Ras GTPase activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Frech, M -- John, J -- Pizon, V -- Chardin, P -- Tavitian, A -- Clark, R -- McCormick, F -- Wittinghofer, A -- New York, N.Y. -- Science. 1990 Jul 13;249(4965):169-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max-Planck-Institute fur medizinische Forschung, Abteilung Biophysik, Heidelberg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2164710" target="_blank"〉PubMed〈/a〉
    Keywords: Binding, Competitive ; Enzyme Activation ; Escherichia coli/enzymology/genetics ; GTP Phosphohydrolases/genetics/*metabolism ; GTP-Binding Proteins/genetics/*metabolism ; GTPase-Activating Proteins ; Oncogene Protein p21(ras)/*metabolism ; Phosphoric Monoester Hydrolases/*metabolism ; Protein Binding ; Proteins/*antagonists & inhibitors ; *Suppression, Genetic ; rap GTP-Binding Proteins ; ras GTPase-Activating Proteins
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  • 8
    Publication Date: 1991-12-13
    Description: Guanosine triphosphatase (GTPase) activity of Ras is increased by interaction with Ras-GAP (GTPase-activating protein) or with the GAP-related domain of the type 1 neurofibromatosis protein (NF1-GRD), but Ras is not affected by interaction with cytoplasmic and membrane forms of Rap-GAP; Rap1A, whose effector function can suppress transformation by Ras, is sensitive to both forms of Rap-GAP and resistant to Ras-GAP and NF1-GRD. A series of chimeric proteins composed of portions of Ras and Rap were constructed; some were sensitive to Ras-GAP but resistant to NF1-GRD, and others were sensitive to cytoplasmic Rap-GAP but resistant to membrane Rap-GAP. Sensitivity of chimeras to Ras-GAP and cytoplasmic Rap-GAP was mediated by amino acids that are carboxyl-terminal to the effector region. Residues 61 to 65 of Ras conferred Ras-GAP sensitivity, but a larger number of Rap1A residues were required for sensitivity to cytoplasmic Rap-GAP. Chimeras carrying the Ras effector region that were sensitive only to Ras-GAP or only to cytoplasmic Rap-GAP transformed NIH 3T3 cells poorly. Thus, distinct amino acids of Ras and Rap1A mediate sensitivity to each of the proteins with GAP activity, and transforming potential of Ras and sensitivity of Ras to Ras-GAP are at least partially independent properties.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhang, K -- Papageorge, A G -- Martin, P -- Vass, W C -- Olah, Z -- Polakis, P G -- McCormick, F -- Lowy, D R -- New York, N.Y. -- Science. 1991 Dec 13;254(5038):1630-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Cellular Oncology, National Cancer Institute, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1749934" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Membrane/metabolism ; Cytosol/metabolism ; Enzyme Activation ; GTP-Binding Proteins/*physiology ; GTPase-Activating Proteins ; Genes, Neurofibromatosis 1 ; In Vitro Techniques ; Proteins/*physiology ; Proto-Oncogene Proteins p21(ras)/*physiology ; Recombinant Fusion Proteins ; Structure-Activity Relationship ; rap GTP-Binding Proteins ; ras GTPase-Activating Proteins
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  • 9
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2007-08-04
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉McCormick, Sheila -- New York, N.Y. -- Science. 2007 Aug 3;317(5838):606-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Plant Gene Expression Center, USDA Agricultural Research Service-UC Berkeley, 800 Buchanan Street, Albany, CA 94710, USA. sheilamc@nature.berkeley.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17673644" target="_blank"〉PubMed〈/a〉
    Keywords: Arabidopsis/enzymology/genetics/*physiology ; Arabidopsis Proteins/genetics/*metabolism ; Cell Membrane/enzymology ; Crosses, Genetic ; Evolution, Molecular ; Flowers/cytology/enzymology/*physiology ; Genes, Plant ; Ligands ; Models, Biological ; Mutation ; Phosphotransferases/*genetics/*metabolism ; Pollen Tube/growth & development/*physiology ; Reproduction ; Signal Transduction ; Species Specificity
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  • 10
    Publication Date: 2008-02-16
    Description: Searches for extrasolar planets have uncovered an astonishing diversity of planetary systems, yet the frequency of solar system analogs remains unknown. The gravitational microlensing planet search method is potentially sensitive to multiple-planet systems containing analogs of all the solar system planets except Mercury. We report the detection of a multiple-planet system with microlensing. We identify two planets with masses of approximately 0.71 and approximately 0.27 times the mass of Jupiter and orbital separations of approximately 2.3 and approximately 4.6 astronomical units orbiting a primary star of mass approximately 0.50 solar mass at a distance of approximately 1.5 kiloparsecs. This system resembles a scaled version of our solar system in that the mass ratio, separation ratio, and equilibrium temperatures of the planets are similar to those of Jupiter and Saturn. These planets could not have been detected with other techniques; their discovery from only six confirmed microlensing planet detections suggests that solar system analogs may be common.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gaudi, B S -- Bennett, D P -- Udalski, A -- Gould, A -- Christie, G W -- Maoz, D -- Dong, S -- McCormick, J -- Szymanski, M K -- Tristram, P J -- Nikolaev, S -- Paczynski, B -- Kubiak, M -- Pietrzynski, G -- Soszynski, I -- Szewczyk, O -- Ulaczyk, K -- Wyrzykowski, L -- OGLE Collaboration -- Depoy, D L -- Han, C -- Kaspi, S -- Lee, C-U -- Mallia, F -- Natusch, T -- Pogge, R W -- Park, B-G -- MuFUN Collaboration -- Abe, F -- Bond, I A -- Botzler, C S -- Fukui, A -- Hearnshaw, J B -- Itow, Y -- Kamiya, K -- Korpela, A V -- Kilmartin, P M -- Lin, W -- Masuda, K -- Matsubara, Y -- Motomura, M -- Muraki, Y -- Nakamura, S -- Okumura, T -- Ohnishi, K -- Rattenbury, N J -- Sako, T -- Saito, To -- Sato, S -- Skuljan, L -- Sullivan, D J -- Sumi, T -- Sweatman, W L -- Yock, P C M -- MOA Collaboration -- Albrow, M D -- Allan, A -- Beaulieu, J-P -- Burgdorf, M J -- Cook, K H -- Coutures, C -- Dominik, M -- Dieters, S -- Fouque, P -- Greenhill, J -- Horne, K -- Steele, I -- Tsapras, Y -- PLANET and RoboNet Collaborations -- Chaboyer, B -- Crocker, A -- Frank, S -- Macintosh, B -- New York, N.Y. -- Science. 2008 Feb 15;319(5865):927-30. doi: 10.1126/science.1151947.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Astronomy, Ohio State University, 140 West 18th Avenue, Columbus, OH 43210, USA. gaudi@astronomy.ohio-state.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18276883" target="_blank"〉PubMed〈/a〉
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