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Notch intracellular domain overexpression in o

by unknown authors
"... le ns is i ls ..."
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le ns is i ls

CRMP2 in transgenic mice expressing APP intracellular domain

by Kathleen A. Ryan, Sanjay W. Pimplikar
"... Amyloid precursor protein (APP), implicated in Alzheimer’s disease, is a trans-membrane protein of undetermined function. APP is cleaved by �-secretase that releases the APP intracellular domain (AICD) in the cytoplasm. In vitro studies have implicated AICD in cell signaling and transcriptional regu ..."
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Amyloid precursor protein (APP), implicated in Alzheimer’s disease, is a trans-membrane protein of undetermined function. APP is cleaved by �-secretase that releases the APP intracellular domain (AICD) in the cytoplasm. In vitro studies have implicated AICD in cell signaling and transcriptional

JCB Article Back signaling by the Nrg-1 intracellular domain

by Jianxin Bao, Deon Wolpowitz, Lorna W. Role, David A. Talmage
"... ligands for erbB receptors, include an extracellular domain with an EGF-like sequence and a highly conserved intracellular domain (ICD) of unknown function. In this paper, we demonstrate that transmembrane isoforms of Nrg-1 are bidirectional signaling molecules in neurons. The stimuli for Nrg-1 back ..."
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ligands for erbB receptors, include an extracellular domain with an EGF-like sequence and a highly conserved intracellular domain (ICD) of unknown function. In this paper, we demonstrate that transmembrane isoforms of Nrg-1 are bidirectional signaling molecules in neurons. The stimuli for Nrg-1

An in-frame complex germline mutation in the juxtamembrane intracellular domain causing RET activation in familial medullary thyroid carcinoma

by Daniela Cordella, Marina Muzza, Luisella Alberti, Paolo Colombo, Pietro Travaglini, Paolo Beck-peccoz, Laura Fugazzola, Luca Persani , 2006
"... An in-frame complex germline mutation in the juxtamembrane intracellular domain causing RET activation in familial medullary thyroid carcinoma ..."
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An in-frame complex germline mutation in the juxtamembrane intracellular domain causing RET activation in familial medullary thyroid carcinoma

c-Secretase Dependent Production of Intracellular Domains Is Reduced in Adult Compared to Embryonic

by Rat Brain Membranes, Jenny Fra˚nberg* Helena Karlström , 2010
"... Background: c-Secretase is an intramembrane aspartyl protease whose cleavage of the amyloid precursor protein (APP) generates the amyloid b-peptide (Ab) and the APP intracellular domain. Ab is widely believed to have a causative role in Alzheimer’s disease pathogenesis, and therefore modulation of c ..."
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Background: c-Secretase is an intramembrane aspartyl protease whose cleavage of the amyloid precursor protein (APP) generates the amyloid b-peptide (Ab) and the APP intracellular domain. Ab is widely believed to have a causative role in Alzheimer’s disease pathogenesis, and therefore modulation

THE CONTRIBUTION OF THE INTRACELLULAR DOMAINS TO P2X1 RECEPTOR REGULATION

by Hairuo Wen , 2009
"... The contribution of the intracellular domains to P2X1 receptor regulation Hairuo Wen P2X1 receptors are expressed throughout the body and contribute to a range of physiological process, e.g. thrombosis and smooth muscle tone. The intracellular terminals of the P2X1 receptor have been shown to be inv ..."
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The contribution of the intracellular domains to P2X1 receptor regulation Hairuo Wen P2X1 receptors are expressed throughout the body and contribute to a range of physiological process, e.g. thrombosis and smooth muscle tone. The intracellular terminals of the P2X1 receptor have been shown

Tyr 682 in the Intracellular Domain of APP Regulates Amyloidogenic APP Processing In Vivo

by Alessia P. M. Barbagallo, Richard Weldon, Robert Tamayev, Dawang Zhou, Luca Giliberto , 2010
"... Background: The pathogenesis of Alzheimer’s disease is attributed to misfolding of Amyloid-b (Ab) peptides. Ab is generated during amyloidogenic processing of Ab-precursor protein (APP). Another characteristic of the AD brain is increased phosphorylation of APP amino acid Tyr 682. Tyr 682 is part of ..."
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. In addition, we demonstrate the essential nature of amino acid Tyr 682 for the APP/Fe65 interaction in vivo. Conclusions/Significance: Together, these observations point to an essential role of APP intracellular domain for normal APP processing and function in vivo, and provide rationale for further studies

Visualization and Quantification of APP Intracellular Domain-Mediated Nuclear Signaling by Bimolecular

by Fluorescence Complementation, Florian Riese, Sonja Grinschgl, Manuel T. Gersbacher, Natalie Russi, Christoph Hock, Roger M. Nitsch, Uwe Konietzko
"... Background: The amyloid precursor protein (APP) intracellular domain (AICD) is released from full-length APP upon sequential cleavage by either α- or β-secretase followed by γ-secretase. Together with the adaptor protein Fe65 and the histone acetyltransferase Tip60, AICD forms nuclear multiprotein c ..."
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Background: The amyloid precursor protein (APP) intracellular domain (AICD) is released from full-length APP upon sequential cleavage by either α- or β-secretase followed by γ-secretase. Together with the adaptor protein Fe65 and the histone acetyltransferase Tip60, AICD forms nuclear multiprotein

APP Intracellular Domain Impairs Adult Neurogenesis in Transgenic Mice by Inducing Neuroinflammation

by Kaushik Ghosal, Andrea Stathopoulos, Sanjay W. Pimplikar
"... Background: A devastating aspect of Alzheimer’s disease (AD) is the progressive deterioration of memory due to neuronal loss. Amyloid precursor protein (APP) occupies a central position in AD and APP-derived amyloid-b (Ab) peptides are thought to play a pivotal role in disease pathogenesis. Nonethel ..."
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. Nonetheless, it is becoming clear that AD etiology is highly complex and that factors other than Ab also contribute to AD pathogenesis. APP intracellular domain (AICD) is generated together with Ab and we recently showed that AICD transgenic mice recapitulate pathological features of AD such as tau

Importance of the intracellular domain of NR2 subunits for NMDA receptor function in vivo

by Rolf Sprengel, Bettina Suchanek, Carla Amico, Rossella Brusa, Nail Burnashev, Andrei Rozov, Øivind Hvalby, Vidar Jensen, Ole Paulsen, Per Andersen, Jeansok J. Kim, Richard F. Thompson, William Sun, Lorna C. Webster, Seth G. N. Grant, Jens Eilers, Arthur Konnerth, Jianying Li, James O. Mcnamara, Peter H. Seeburg - Cell , 1998
"... These and NR2C�C/�C mice display deficits in motor coordination. C-terminal truncation of NR2 subunits does not interfere with the formation of gateable receptor channels that can be synaptically activated. Thus, the phenotypes of our mutants appear to reflect defective intracellular signaling. ..."
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These and NR2C�C/�C mice display deficits in motor coordination. C-terminal truncation of NR2 subunits does not interfere with the formation of gateable receptor channels that can be synaptically activated. Thus, the phenotypes of our mutants appear to reflect defective intracellular signaling.
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