Información*
| Nombre | ROBERTO SANCHEZ OLEA |
|---|---|
| Área | BIOLOGÍA Y QUÍMICA |
| Campo | CIENCIAS DE LA VIDA |
| Disciplina | BIOLOGÍA CELULAR |
| Especialidad | GTPASAS |
| CVU | 248190 |
| Institución | |
|---|---|
| Dependencia | INSTITUTO DE FISICA |
| Entidad | SAN LUIS POTOSI |
| Nivel | 2 |
| Vigencia | Inicio: 01/01/2023 |
| Fin: 31/12/2027 |
* Información del primer trimestre de 2026.
Fuente: SECIHTI.
Publicaciones ORCID
- 2025
- Characterization of the carboxy‐terminal domain of the GPN‐loop GTPase Npa3 reveals an intrinsically disordered region and phosphorylation‐dependent regulation in the absence of BUD27 The FEBS Journal
- Proposal of Chemical Inhibitors That Compete with the Binding of RNA Polymerase II Subunits to Essential GTPases GPN Npa3 and Gpn1 ACS Omega
- 2022
- Synthetic negative genome screen of the GPN-loop GTPase NPA3 in Saccharomyces cerevisiae Current Genetics
- 2019
- FRET‐based analysis and molecular modeling of the human GPN-loop GTPases 1 and 3 heterodimer unvelis a dominant-negative protein complex The FEBS Journal
- Gpn3 Is Essential for Cell Proliferation of Breast Cancer Cells Independent of Their Malignancy Degree Technology in Cancer Research & Treatment
- 2017
- Gpn3 is polyubiquitinated on lysine 216 and degraded by the proteasome in the cell nucleus in a Gpn1-inhibitable manner FEBS Letters
- The Gpn3 Q279* cancer-associated mutant inhibits Gpn1 nuclear export and is deficient in RNA polymerase II nuclear targeting FEBS Letters
- Human Gpn1 purified from bacteria binds guanine nucleotides and hydrolyzes GTP as a protein dimer stabilized by its C-terminal tail Protein Expression and Purification
- Npa3/ Sc Gpn1 carboxy-terminal tail is dispensable for cell viability and RNA polymerase II nuclear targeting but critical for microtubule stability and function Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
- 2014
- Gpn1 and Gpn3 associate tightly and their protein levels are mutually dependent in mammalian cells FEBS Letters

