Her primary scientific interests are in Amyloid precursor protein, P3 peptide, Biochemistry, Amyloid precursor protein secretase and Alpha secretase. She usually deals with Amyloid precursor protein and limits it to topics linked to Thrombin and Platelet activation and Proteolysis. Genevieve Evin regularly links together related areas like Amyloid in her Biochemistry studies.
Her Amyloid precursor protein secretase study necessitates a more in-depth grasp of Alzheimer's disease. The study incorporates disciplines such as GSK-3, Neurodegeneration and Pharmacology in addition to Alzheimer's disease. Her Alpha secretase research is multidisciplinary, incorporating elements of Disease gene, APH-1, PRESENILIN 2, Presenilin and Beta amyloid precursor protein.
Her scientific interests lie mostly in Amyloid precursor protein, Biochemistry, Amyloid precursor protein secretase, Presenilin and Cell biology. Her study with Amyloid precursor protein involves better knowledge in Alzheimer's disease. Genevieve Evin works mostly in the field of Alzheimer's disease, limiting it down to topics relating to Neurodegeneration and, in certain cases, BACE1-AS.
Genevieve Evin has researched Biochemistry in several fields, including Renin–angiotensin system and Amyloid. Her work in Amyloid precursor protein secretase covers topics such as Pharmacology which are related to areas like Disease, Dementia and Neuregulin. Her Presenilin research integrates issues from Acetylcholinesterase, Plasma protein binding and Colocalization.
Her primary areas of study are Amyloid precursor protein, Biochemistry, Cell biology, Amyloid precursor protein secretase and Disease. The Amyloid precursor protein study combines topics in areas such as Plasma protein binding and Presenilin. As a part of the same scientific family, Genevieve Evin mostly works in the field of Biochemistry, focusing on Copper and, on occasion, Superoxide dismutase and Zinc.
Metalloproteinase is closely connected to Amyloid in her research, which is encompassed under the umbrella topic of Cell biology. Amyloid precursor protein secretase is a primary field of her research addressed under Alzheimer's disease. Her Disease study combines topics in areas such as Frontal cortex and Pharmacology.
Biochemistry, Amyloid precursor protein secretase, Gamma secretase, Amyloid precursor protein and Alzheimer's disease are her primary areas of study. Her Biochemistry research is multidisciplinary, incorporating perspectives in Biomarker and Cell biology. Her studies in Amyloid precursor protein secretase integrate themes in fields like Protease, Pharmacology and Endosome.
Her Gamma secretase research includes elements of Genetically modified mouse, Transgene, Insulysin, Neprilysin and Amyloid. Her Amyloid precursor protein research is mostly focused on the topic P3 peptide. Genevieve Evin combines subjects such as Oxidative stress, Cerebrospinal fluid and Pathogenesis with her study of Alzheimer's disease.
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Reactifs de couplage peptidique I (1) - l'hexafluorophosphate de benzotriazolyl N-oxytrisdimethylamino phosphonium (B.O.P.)
B. Castro;J.R. Dormoy;G. Evin;C. Selve.
Tetrahedron Letters (1975)
Increased expression of the amyloid precursor β‐secretase in Alzheimer's disease
R. M. Damian Holsinger;Catriona A. McLean;Konrad Beyreuther;Colin L. Masters.
Annals of Neurology (2002)
A Novel ε-Cleavage within the Transmembrane Domain of the Alzheimer Amyloid Precursor Protein Demonstrates Homology with Notch Processing†
Andreas Weidemann;Simone Eggert;Friedrich B M Reinhard;Markus Vogel.
Biochemistry (2002)
Degradation of the Alzheimer disease amyloid beta-peptide by metal-dependent up-regulation of metalloprotease activity.
Anthony R White;Anthony R White;Tai Du;Tai Du;Katrina M Laughton;Irene Volitakis.
Journal of Biological Chemistry (2006)
Formation of stable complexes between two Alzheimer's disease gene products: presenilin-2 and beta-amyloid precursor protein.
A. Weidemann;K. Paliga;U. Dürrwang;C. Czech.
Nature Medicine (1997)
The proteolytic processing of the amyloid precursor protein gene family members APLP-1 and APLP-2 involves alpha-, beta-, gamma-, and epsilon-like cleavages: modulation of APLP-1 processing by n-glycosylation.
Simone Eggert;Krzysztof Paliga;Peter Soba;Genevieve Evin.
Journal of Biological Chemistry (2004)
Biogenesis and metabolism of Alzheimer’s disease Aβ amyloid peptides
Geneviève Evin;Andreas Weidemann.
Peptides (2002)
Proteolytic Processing of the Alzheimer’s Disease Amyloid Precursor Protein within Its Cytoplasmic Domain by Caspase-like Proteases
Andreas Weidemann;Krzysztof Paliga;Ulrike Dürrwang;Friedrich B.M. Reinhard.
Journal of Biological Chemistry (1999)
Secretion of Alzheimer's disease Abeta amyloid peptide by activated human platelets.
Q X Li;S Whyte;J E Tanner;G Evin.
Laboratory Investigation (1998)
The C-terminal fragment of the Alzheimer's disease amyloid protein precursor is degraded by a proteasome-dependent mechanism distinct from gamma-secretase.
Janelle Nunan;Mark S. Shearman;Frédéric Checler;Roberto Cappai.
FEBS Journal (2001)
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