Mechanism of glucocerebrosidase activation and dysfunction in Gaucher disease unraveled by molecular...
Mechanism of glucocerebrosidase activation and dysfunction in Gaucher disease unraveled by molecular dynamics and deep learning
About this item
Full title
Author / Creator
Oak Ridge National Laboratory (ORNL), Oak Ridge, TN (United States) , Romero, Raquel , Ramanathan, Arvind , Yuen, Tony , Bhowmik, Debsindhu , Mathew, Mehr , Munshi, Lubna Bashir , Javaid, Seher , Bloch, Madison , Lizneva, Daria , Rahimova, Alina , Khan, Ayesha , Taneja, Charit , Kim, Se-Min , Sun, Li , New, Maria I. , Haider, Shozeb and Zaidi, Mone
Publisher
United States: National Academy of Sciences
Journal title
Language
English
Formats
Publication information
Publisher
United States: National Academy of Sciences
Subjects
More information
Scope and Contents
Contents
The lysosomal enzyme glucocerebrosidase-1 (GCase) catalyzes the cleavage of a major glycolipid glucosylceramide into glucose and ceramide. The absence of fully functional GCase leads to the accumulation of its lipid substrates in lysosomes, causing Gaucher disease, an autosomal recessive disorder that displays profound genotype–phenotype nonconcord...
Alternative Titles
Full title
Mechanism of glucocerebrosidase activation and dysfunction in Gaucher disease unraveled by molecular dynamics and deep learning
Authors, Artists and Contributors
Author / Creator
Romero, Raquel
Ramanathan, Arvind
Yuen, Tony
Bhowmik, Debsindhu
Mathew, Mehr
Munshi, Lubna Bashir
Javaid, Seher
Bloch, Madison
Lizneva, Daria
Rahimova, Alina
Khan, Ayesha
Taneja, Charit
Kim, Se-Min
Sun, Li
New, Maria I.
Haider, Shozeb
Zaidi, Mone
Identifiers
Primary Identifiers
Record Identifier
TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_6421449
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_6421449
Other Identifiers
ISSN
0027-8424
E-ISSN
1091-6490
DOI
10.1073/pnas.1818411116
