Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Julie Carimalo"'
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
https://doi.org/10.1021/pr1004604
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::bcd8c87fa64fe50f7e0d1dc0f73f2dec
https://doi.org/10.1111/j.1460-9568.2010.07224.x
https://doi.org/10.1111/j.1460-9568.2010.07224.x
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5ee5473e98b612d929686a6d7e7cf0ff
https://pubmed.ncbi.nlm.nih.gov/26024859
https://pubmed.ncbi.nlm.nih.gov/26024859
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⟩
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
https://hal.archives-ouvertes.fr/hal-01542871
Autor:
Matthias, Schmitz, Markus, Schlomm, Badrul, Hasan, Michael, Beekes, Eva, Mitrova, Carsten, Korth, Andreas, Breil, Julie, Carimalo, Joanna, Gawinecka, Daniela, Varges, Inga, Zerr
Publikováno v:
The European journal of neuroscience. 31(11)
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::5231b91324582676adcf8ecc2db57f38
https://pubmed.ncbi.nlm.nih.gov/20529115
https://pubmed.ncbi.nlm.nih.gov/20529115