Výsledky vyhledávání - "Julie Carimalo"

Codon 129 Polymorphism Specific Cerebrospinal Fluid Proteome Pattern in Sporadic Creutzfeldt−Jakob Disease and the Implication of Glycolytic Enzymes in Prion-Induced Pathology

Autor: Inga Zerr, Uta Heinemann, Jan-Hendrik Streich, Hassan Dihazi, Abdul R. Asif, Joanna Gawinecka, Walter J. Schulz-Schaeffer, Julie Carimalo, Jana K Dieks

Publikováno v: Journal of Proteome Research. 9:5646-5657

Cerebrospinal fluid (CSF) contains a dynamic and complex mixture of proteins, which can reflect a physiological and pathological state of the central nervous system. In our present study, we show CSF protein patterns from patients with the two most f

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8a716e10cfb7d2da7f74e218024b54a5
https://doi.org/10.1021/pr1004604

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Codon 129 polymorphism and the E200K mutation do not affect the cellular prion protein isoform composition in the cerebrospinal fluid from patients with Creutzfeldt-Jakob disease

Autor: Daniela Varges, Badrul Hasan, Julie Carimalo, Michael Beekes, Eva Mitrova, Markus Schlomm, Inga Zerr, Matthias Schmitz, Carsten Korth, Andreas Breil, Joanna Gawinecka

Publikováno v: European Journal of Neuroscience. 31:2024-2031

The cellular prion protein (PrP(c)) is a multifunctional, highly conserved and ubiquitously expressed protein. It undergoes a number of modifications during its post-translational processing, resulting in different PrP(c) glycoforms and truncated PrP

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https://doi.org/10.1111/j.1460-9568.2010.07224.x

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Cellular prion protein directly interacts with and enhances lactate dehydrogenase expression under hypoxic conditions

Autor: Matthias Schmitz, Walter J. Schulz-Schaeffer, Abdul R. Asif, Inga Zerr, Arne Wrede, Sara Schenkel, Jens Weise, Julie Carimalo, Thorsten R. Doeppner, Sanja Ramljak, Saima Zafar

Publikováno v: Experimental neurology 271, 155-167 (2015). doi:10.1016/j.expneurol.2015.04.025

Although a physiological function of the cellular prion protein (PrP(c)) is still not fully clarified, a PrP(c)-mediated neuroprotection against hypoxic/ischemic insult is intriguing. After ischemic stroke prion protein knockout mice (Prnp(0/0)) disp

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https://pubmed.ncbi.nlm.nih.gov/26024859

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Endogenous prion protein conversion is required for prion-induced neuritic alterations and neuronal death

Autor: Sabrina Cronier, Vincent Béringue, Emilie Jaumain, Marie-Christine Miquel, Hubert Laude, Julie Carimalo, Brigitte Schaeffer, Jean-Michel Peyrin

Publikováno v: FASEB Journal
FASEB Journal, Federation of American Society of Experimental Biology, 2012, 26 (9), pp.3854-3861. ⟨10.1096/fj.11-201772⟩
FASEB Journal, 2012, 26 (9), pp.3854-3861. ⟨10.1096/fj.11-201772⟩

PubMed - PMID : 22661006; International audience; Prions cause fatal neurodegenerative conditions and result from the conversion of host-encoded cellular prion protein (PrPC) into abnormally folded scrapie PrP (PrPSc). Prions can propagate both in ne

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d9fee0ef9a2ca249acff7937458a0414
https://hal.archives-ouvertes.fr/hal-01542871