Mariano Tabios

ORCID: 0000-0003-0616-7939
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About
Contact & Profiles
Research Areas
  • SARS-CoV-2 and COVID-19 Research
  • Parkinson's Disease Mechanisms and Treatments
  • interferon and immune responses
  • Heat shock proteins research
  • Protein Structure and Dynamics
  • Cellular transport and secretion
  • RNA and protein synthesis mechanisms
  • Neurological disorders and treatments
  • Enzyme Structure and Function
  • Invertebrate Immune Response Mechanisms
  • Click Chemistry and Applications
  • Protein Degradation and Inhibitors
  • Molecular Communication and Nanonetworks
  • Genomics and Phylogenetic Studies
  • Ubiquitin and proteasome pathways
  • Bacteriophages and microbial interactions
  • Monoclonal and Polyclonal Antibodies Research
  • Insect Resistance and Genetics
  • SARS-CoV-2 detection and testing
  • Peptidase Inhibition and Analysis
  • Signaling Pathways in Disease

University of California, San Francisco
2019-2023

Molecular Biology Consortium
2021

Howard Hughes Medical Institute
2019

Exelixis (United States)
2004-2005

Abstract The SARS-CoV-2 protein Nsp2 has been implicated in a wide range of viral processes, but its exact functions, and the structural basis those remain unknown. Here, we report an atomic model for full-length obtained by combining cryo-electron microscopy with deep learning-based structure prediction from AlphaFold2. resulting reveals highly-conserved zinc ion-binding site, suggesting role RNA binding. Mapping emerging mutations variants on shows potential host-Nsp2 interaction regions....

10.1101/2021.05.10.443524 preprint EN cc-by-nc-nd bioRxiv (Cold Spring Harbor Laboratory) 2021-05-12

The Hsp90 molecular chaperone collaborates with the phosphorylated Cdc37 cochaperone for folding and activation of its many client kinases. As kinases, kinase CRaf is activated by phosphorylation at specific regulatory sites. phosphatase PP5 dephosphorylates in an Hsp90-dependent manner. Although dephosphorylating has been proposed as a mechanism releasing Hsp90-bound here we show that bound kinases sterically inhibit dephosphorylation indicating release must occur before dephosphorylation....

10.1038/s41467-023-37659-7 article EN cc-by Nature Communications 2023-04-17

Abstract The over-expression and aggregation of α-synuclein (αSyn) are linked to the onset pathology Parkinson’s disease. Native monomeric αSyn exists in an intrinsically disordered ensemble interconverting conformations, which has made its therapeutic targeting by small molecules highly challenging. Nonetheless, here we successfully target structural thereby identify novel drug-like that impact multiple pathogenic processes. Using a surface plasmon resonance high-throughput screen, is...

10.1038/s41598-019-52598-4 article EN cc-by Scientific Reports 2019-11-18

The SARS-CoV-2 protein Nsp2 has been implicated in a wide range of viral processes, but its exact functions, and the structural basis those remain unknown. Here, we report an atomic model for full-length obtained by combining cryo-electron microscopy with deep learning-based structure prediction from AlphaFold2. resulting reveals highly-conserved zinc ion-binding site, suggesting role RNA binding. Mapping emerging mutations variants on shows potential host-Nsp2 interaction regions. Using...

10.21203/rs.3.rs-515215/v1 preprint EN cc-by Research Square (Research Square) 2021-05-19

Mutations that inactivate the retinoblastoma (Rb) pathway are common in human tumors. Such mutations promote tumor growth by deregulating G1 cell cycle checkpoint. However, uncontrolled progression can also produce new liabilities for survival. To uncover such Rb mutant cells, we performed a clonal screen Drosophila eye to identify second-site eliminate Rbf(-) but allow Rbf(+) cells survive. Here report identification of mutation novel highly conserved peptidyl prolyl isomerase (PPIase)...

10.1534/genetics.104.036343 article EN Genetics 2005-03-03

Abstract The Hsp90 molecular chaperone collaborates with the phosphorylated Cdc37 cochaperone to maintain kinase proteostasis through folding and activation of its many client kinases. As kinases, CRaf is activated by phosphorylation at specific regulatory sites. phosphatase PP5 dephosphorylates but also in an Hsp90-dependent manner. Although dephosphorylating has been proposed as a mechanism for releasing Hsp90-bound here we show that bound kinases sterically inhibit dephosphorylation...

10.1101/2022.09.02.506407 preprint EN cc-by-nd bioRxiv (Cold Spring Harbor Laboratory) 2022-09-03

Abstract The over-expression and aggregation of α-synuclein (αSyn) are linked to the onset pathology Parkinson’s disease. Native monomeric αSyn exists in an intrinsically disordered ensemble interconverting conformations, which has made its therapeutic targeting by small molecules highly challenging. Nonetheless, here we successfully target structural thereby identify novel drug-like that impact multiple pathogenic processes. Using a surface plasmon resonance high-throughput screen, is...

10.1101/646505 preprint EN cc-by-nc-nd bioRxiv (Cold Spring Harbor Laboratory) 2019-05-24

The over-expression and aggregation of α-synuclein (αSyn) are linked to the onset pathology Parkinson's disease. Native monomeric αSyn exists in an intrinsically disordered ensemble interconverting conformations, which has made its therapeutic targeting by small molecules highly challenging. Nonetheless, here we successfully target structural thereby identify novel drug-like that impact multiple pathogenic processes. Using a surface plasmon resonance high-throughput screen, is incubated with...

10.17863/cam.47311 article EN 2019-11-18
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