Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Filters

C Haass

Showing results (61-70 of 101) with videos related to

Pageof 11
Sort By:
Nature Medicine|December 1, 1995
The Swedish mutation causes early-onset Alzheimer's disease by beta-secretase cleavage within the secretory pathwayC Haass, C A Lemere, A Capell, et al.
EMBO Reports|August 25, 2001
Presenilin-dependent gamma-secretase processing of beta-amyloid precursor protein at a site corresponding to the S3 cleavage of NotchM Sastre, H Steiner, K Fuchs, et al.
Journal of Neuroscience Research|May 26, 1999
Analysis of presenilin 1 and presenilin 2 expression and processing by newly developed monoclonal antibodiesA Diehlmann, N Ida, S Weggen, et al.
Annals of the New York Academy of Sciences|January 17, 1996
The role of APP processing and trafficking pathways in the formation of amyloid beta-proteinD J Selkoe, T Yamazaki, M Citron, et al.
Biochemistry|November 5, 1999
Amyloidogenic function of the Alzheimer's disease-associated presenilin 1 in the absence of endoproteolysisH Steiner, H Romig, B Pesold, et al.
The Journal of Biological Chemistry|March 30, 2001
Phosphorylation regulates intracellular trafficking of beta-secretaseJ Walter, R Fluhrer, B Hartung, et al.
Neuroreport|November 27, 1998
Truncated presenilin 2 derived from differentially spliced mRNA does not affect the ratio of amyloid beta-peptide 1-42/1-40J Grünberg, J Walter, C Eckman, et al.
The Journal of Biological Chemistry|August 15, 1997
Presenilins are processed by caspase-type proteasesH Loetscher, U Deuschle, M Brockhaus, et al.
The Journal of Biological Chemistry|March 7, 1998
The proteolytic fragments of the Alzheimer's disease-associated presenilin-1 form heterodimers and occur as a 100-150-kDa molecular mass complexA Capell, J Grünberg, B Pesold, et al.
Journal of Neurochemistry|May 22, 2001
Sensitivity to MPTP is not increased in Parkinson's disease-associated mutant alpha-synuclein transgenic miceS Rathke-Hartlieb, P J Kahle, M Neumann, et al.
Pageof 11

Showing results (61-70 of 101) with videos related to

Sort By:
Pageof 11
Nature Medicine|December 1, 1995
The Swedish mutation causes early-onset Alzheimer's disease by beta-secretase cleavage within the secretory pathwayC Haass, C A Lemere, A Capell, et al.
EMBO Reports|August 25, 2001
Presenilin-dependent gamma-secretase processing of beta-amyloid precursor protein at a site corresponding to the S3 cleavage of NotchM Sastre, H Steiner, K Fuchs, et al.
Journal of Neuroscience Research|May 26, 1999
Analysis of presenilin 1 and presenilin 2 expression and processing by newly developed monoclonal antibodiesA Diehlmann, N Ida, S Weggen, et al.
Annals of the New York Academy of Sciences|January 17, 1996
The role of APP processing and trafficking pathways in the formation of amyloid beta-proteinD J Selkoe, T Yamazaki, M Citron, et al.
Biochemistry|November 5, 1999
Amyloidogenic function of the Alzheimer's disease-associated presenilin 1 in the absence of endoproteolysisH Steiner, H Romig, B Pesold, et al.
The Journal of Biological Chemistry|March 30, 2001
Phosphorylation regulates intracellular trafficking of beta-secretaseJ Walter, R Fluhrer, B Hartung, et al.
Neuroreport|November 27, 1998
Truncated presenilin 2 derived from differentially spliced mRNA does not affect the ratio of amyloid beta-peptide 1-42/1-40J Grünberg, J Walter, C Eckman, et al.
The Journal of Biological Chemistry|August 15, 1997
Presenilins are processed by caspase-type proteasesH Loetscher, U Deuschle, M Brockhaus, et al.
The Journal of Biological Chemistry|March 7, 1998
The proteolytic fragments of the Alzheimer's disease-associated presenilin-1 form heterodimers and occur as a 100-150-kDa molecular mass complexA Capell, J Grünberg, B Pesold, et al.
Journal of Neurochemistry|May 22, 2001
Sensitivity to MPTP is not increased in Parkinson's disease-associated mutant alpha-synuclein transgenic miceS Rathke-Hartlieb, P J Kahle, M Neumann, et al.
Pageof 11