Tsui-Fen Chou
California Institute of Technology
AAA proteinsCancerMutantMolecular biologyEnzymeChemistryAutophagyATPaseUbiquitinProteasomeHistidinePhosphoramidateActive siteMutationNucleotideBiochemistryStereochemistryMedicineBiologyCell biology
Publications 80
#1Xiaoyi Zhang (Los Angeles Biomedical Research Institute)H-Index: 4
#2Lin Gui (Los Angeles Biomedical Research Institute)H-Index: 4
Last. Tsui-Fen Chou (Los Angeles Biomedical Research Institute)H-Index: 22
view all 10 authors...
p97 protein is a highly conserved, abundant, functionally diverse, structurally dynamic homohexameric AAA enzyme-containing N, D1, and D2 domains. A truncated p97 protein containing the N and D1 domains and the D1-D2 linker (ND1L) exhibits 79% of wild-type (WT) ATPase activity whereas the ND1 domain alone without the linker only has 2% of WT activity. To investigate the relationship between the D1-D2 linker and the D1 domain, we produced p97 ND1L mutants and demonstrated that this 22-residue lin...
#1Steven Q. Le (WashU: Washington University in St. Louis)H-Index: 13
#2Shih-hsin KanH-Index: 4
Last. Hemanth R. Nelvagal (WashU: Washington University in St. Louis)H-Index: 6
view all 17 authors...
Recombinant human alpha-N-acetylglucosaminidase-insulin-like growth factor-2 (rhNAGLU-IGF2) is an investigational enzyme replacement therapy for Sanfilippo B, a lysosomal storage disease. The fusion protein with IGF2 permits binding to the cation-independent mannose 6-phosphate receptor, because recombinant human NAGLU (rhNAGLU) is poorly mannose 6-phosphorylated. We previously administered rhNAGLU-IGF2 intracerebroventricularly to Sanfilippo B mice. We demonstrated therapeutic restoration of NA...
#1Purbasha Nandi (ASU: Arizona State University)
#2Po Lin Chiu (ASU: Arizona State University)H-Index: 12
Last. Andrey G. Malyutin (California Institute of Technology)H-Index: 11
view all 9 authors...
#1Purbasha Nandi (ASU: Arizona State University)
#2Shan Li (California Institute of Technology)H-Index: 6
Last. Po Lin Chiu (ASU: Arizona State University)H-Index: 12
view all 8 authors...
IBMPFD/ALS is a genetic disorder caused by a single amino acid mutation on the p97 ATPase, promoting ATPase activity and cofactor dysregulation. The disease mechanism underlying p97 ATPase malfunction remains unclear. To understand how the mutation alters the ATPase regulation, we assembled a full-length p97R155H with its p47 cofactor and first visualized their structures using single-particle cryo-EM. More than one-third of the population was the dodecameric form. Nucleotide presence dissociate...
#1Abubakar Wani (WashU: Washington University in St. Louis)H-Index: 10
#2Jiang Zhu (WashU: Washington University in St. Louis)
Last. Sara K. Pittman (WashU: Washington University in St. Louis)H-Index: 10
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The pathogenic mechanism by which dominant mutations in VCP cause multisystem proteinopathy (MSP), a rare neurodegenerative disease that presents as fronto-temporal lobar degeneration with TDP-43 inclusions (FTLD-TDP), remains unclear. To explore this, we inactivate VCP in murine postnatal forebrain neurons (VCP conditional knockout [cKO]). VCP cKO mice have cortical brain atrophy, neuronal loss, autophago-lysosomal dysfunction, and TDP-43 inclusions resembling FTLD-TDP pathology. Conditional ex...
#1Dana E Michels (California Polytechnic State University)
#2Brett Lomenick (California Institute of Technology)H-Index: 2
Last. Alexis L. Pasulka (California Polytechnic State University)H-Index: 12
view all 5 authors...
Characterizing the cell-level metabolic trade-offs that phytoplankton exhibit in response to changing environmental conditions is important for predicting the impact of these changes on marine food web dynamics and biogeochemical cycling. The time-selective proteome-labeling approach, bioorthogonal noncanonical amino acid tagging (BONCAT), has potential to provide insight into differential allocation of resources at the cellular level, especially when coupled with proteomics. However, the applic...
#1Kai-Wen Cheng (California Institute of Technology)H-Index: 8
#2Fen Wang (California Institute of Technology)
Last. Tsui-Fen Chou (California Institute of Technology)H-Index: 22
view all 7 authors...
Enzyme replacement therapy (ERT) is a scientifically rational and clinically proven treatment for lysosomal storage diseases. Most enzymes used for ERT are purified from the culture supernatant of mammalian cells. However, it is challenging to purify lysosomal enzymes with sufficient quality and quantity for clinical use due to their low secretion levels in mammalian cell systems. To improve the secretion efficiency of recombinant lysosomal enzymes, we evaluated the impact of artificial signal p...
#1Xiaohong Yang (UC Davis: University of California, Davis)
#2Xiaoxiao Yang (UC Davis: University of California, Davis)H-Index: 1
Last. Xi Chen (UC Davis: University of California, Davis)H-Index: 75
view all 9 authors...
Carbohydrate-Active enZYme (CAZY) GH89 family enzymes catalyze the cleavage of terminal α-N-acetylglucosamine from glycans and glycoconjugates. Although structurally and mechanistically similar to the human lysosomal α-N-acetylglucosaminidase (hNAGLU) in GH89 which is involved in the degradation of heparan sulfate in the lysosome, the reported bacterial GH89 enzymes characterized so far have no or low activity toward α-N-acetylglucosamine-terminated heparosan oligosaccharides, the preferred subs...
#7Shan Li (UCLA Medical Center)
During oropharyngeal candidiasis, Candida albicans activates the epidermal growth factor receptor (EGFR), which induces oral epithelial cells to both endocytose the fungus and synthesize proinflammatory mediators that orchestrate the host immune response. To elucidate the signaling pathways that are stimulated when C. albicans interacts with EGFR, we analyzed the proteins that associate with EGFR when C. albicans infects human oral epithelial cells. We identified 1214 proteins that were associat...
#1Gang Zhang (California Institute of Technology)H-Index: 1
#2Shan Li (California Institute of Technology)
Last. Tsui-Fen Chou (California Institute of Technology)
view all 4 authors...
Abstract ATPases Associated with Diverse Cellular Activity (AAA ATPase) are essential enzymes found in all organisms. They are involved in various processes such as DNA replication, protein degradation, membrane fusion, microtubule serving, peroxisome biogenesis, signal transduction, and the regulation of gene expression. Due to the importance of AAA ATPases, several researchers identified and developed small-molecule inhibitors against these enzymes. We discuss six AAA ATPases that are potentia...
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