Miguel Á. Casado‐Combreras

ORCID: 0000-0003-3375-7758
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About
Contact & Profiles
Research Areas
  • Mitochondrial Function and Pathology
  • RNA Research and Splicing
  • Protein Structure and Dynamics
  • DNA Repair Mechanisms
  • RNA modifications and cancer
  • ATP Synthase and ATPases Research
  • Enzyme Structure and Function
  • Cell death mechanisms and regulation
  • Genetic factors in colorectal cancer
  • Cancer-related gene regulation
  • Estrogen and related hormone effects
  • Genomics and Chromatin Dynamics
  • Ovarian cancer diagnosis and treatment
  • Heat shock proteins research

Centro de Investigaciones Científicas Isla de la Cartuja
2019-2025

Instituto de Investigaciones Químicas
2019-2025

Universidad de Sevilla
2019-2025

Complejo Hospitalario Universitario de Granada
2020

Instituto de Investigación Biosanitaria de Granada
2020

Hospital Universitario Virgen de las Nieves
2020

Abstract Gene duplication has allowed protein evolution toward novel functions and mechanisms. The differences between paralogous genes frequently rely on the sequence of disordered regions. For instance, in mammals, chaperones ANP32A ANP32B share a common evolutionary line have some exchangeable based their similar N‐terminal domains. Nevertheless, C‐terminal low‐complexity‐acidic‐regions (LCARs) display substantial differences, unveiling degree variability them, agreement with different...

10.1002/advs.202415566 article EN cc-by Advanced Science 2025-01-31

Compartmentalization of proteins by liquid-liquid phase separation (LLPS) is used cells to control biochemical reactions spatially and temporally. Among them, the recruitment DNA foci nucleolar trafficking occur biomolecular condensation. Within this frame, oncoprotein SET/TAF-Iβ plays a key role in both chromatin remodeling damage response, as does nucleophosmin (NPM1) which indeed participates ribosome synthesis. Whereas NPM1 widely characterized, little known about that undergone...

10.1016/j.isci.2024.110435 article EN cc-by-nc-nd iScience 2024-07-02

Abstract Post‐translational modifications (PTMs) of proteins are ubiquitous processes present in all life kingdoms, involved the regulation protein stability, subcellular location and activity. In this context, cytochrome c (C ) is an excellent case study to analyze structural functional changes induced by PTMS as C a small, moonlighting playing different roles cell compartments at cell‐cycle stages. actually key component mitochondrial electron transport chain (ETC) under homeostatic...

10.1002/pro.5213 article EN cc-by Protein Science 2024-11-16

Intrinsic protein flexibility is of overwhelming relevance for intermolecular recognition and adaptability highly dynamic ensemble complexes, the phenomenon essential understanding numerous biological processes. These conformational ensembles—encounter complexes—lack a unique organization, which prevents determination well-defined high resolution structures. This case complexes involving oncoprotein SET/template-activating factor-Iβ (SET/TAF-Iβ), histone chaperone whose functions...

10.1016/j.csbj.2022.07.009 article EN cc-by-nc-nd Computational and Structural Biotechnology Journal 2022-01-01

Abstract The alternative reading frame (ARF) protein is crucial in the cellular response to oncogenic stress, being likewise second most frequently inactivated gene a wide spectrum of human cancers. ARF usually sequestered nucleolus by well-known nucleophosmin (NPM) and liberated cell damage exhibit its tumor-suppressor ability. However, mechanism underlying activation unknown. Here we show that mitochondria-to-nucleus translocation cytochrome c upon DNA leads break-off NPM-ARF ensemble...

10.1101/2020.05.07.057075 preprint EN bioRxiv (Cold Spring Harbor Laboratory) 2020-05-08
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