Monografie
Presenilin-1 differentially facilitates endoproteolysis of the beta-amyloid precursor protein and Notch
- Sprache
-
Englisch
- Anmerkungen
-
In: Nature cell biology, Vol. 2, No. 4, 2000. - London : Nature Publ. Group
- Standort
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München, Bayerische Staatsbibliothek -- 4 Z 99.796-2,1/6#S.205-211
Beteiligte Personen und Organisationen
Erschienen
London : Nature Publ. Group, 2000
- URN
-
urn:nbn:de:bvb:12-bsb00064353-2
- Letzte Aktualisierung
-
16.04.2024, 14:01 MESZ
Beteiligte
Entstanden
- London : Nature Publ. Group, 2000
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Amyloid beta-peptide is produced by cultured cells during normal metabolism
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Glycine 384 is required for presenilin-1 function and is conserved in bacterial polytopic aspartyl proteases
A gamma-secretase-like intramembrane cleavage of TNFAlpha by the GxGD aspartyl protease SPPL2b
Assembling the mitochondrial outer membrane
Presenilins mediate a dual intramembranous gamma-secretase cleavag of Notch-1
Unsupported boron-carbon sigma-coordination to platinum as an isolable snapshot of sigma-bond activation
Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins
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