Simon Alberti

ORCID: 0000-0003-4017-6505
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About
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Research Areas
  • RNA Research and Splicing
  • RNA modifications and cancer
  • Heat shock proteins research
  • Endoplasmic Reticulum Stress and Disease
  • RNA and protein synthesis mechanisms
  • Fungal and yeast genetics research
  • Prion Diseases and Protein Misfolding
  • Nuclear Structure and Function
  • Cellular Mechanics and Interactions
  • Ubiquitin and proteasome pathways
  • Protein Structure and Dynamics
  • Amyotrophic Lateral Sclerosis Research
  • RNA regulation and disease
  • Enzyme Structure and Function
  • Genetic Neurodegenerative Diseases
  • Microtubule and mitosis dynamics
  • Advanced Fluorescence Microscopy Techniques
  • Microfluidic and Bio-sensing Technologies
  • Biochemical and Molecular Research
  • Neurogenetic and Muscular Disorders Research
  • Autophagy in Disease and Therapy
  • Advanced Proteomics Techniques and Applications
  • Proteins in Food Systems
  • Neurological diseases and metabolism
  • Spaceflight effects on biology

TU Dresden
2019-2025

Center for Systems Biology Dresden
2019-2024

Max Planck Institute of Molecular Cell Biology and Genetics
2015-2024

National Center for Genetic Engineering and Biotechnology
2020-2024

Regione del Veneto
2023

Institute of Molecular Biology
2018

University of Bonn
2001-2014

Max Planck Society
2013

Whitehead Institute for Biomedical Research
2007-2012

Howard Hughes Medical Institute
2007

Daniel J. Klionsky Amal Kamal Abdel‐Aziz Sara Abdelfatah Mahmoud Abdellatif Asghar Abdoli and 95 more Steffen Abel Hagai Abeliovich Marie H. Abildgaard Yakubu Princely Abudu Abraham Acevedo‐Arozena Iannis E. Adamopoulos Khosrow Adeli Timon E. Adolph Annagrazia Adornetto Elma Aflaki Galila Agam Anupam Agarwal Bharat B. Aggarwal Maria Agnello Patrizia Agostinis Javed N. Agrewala Alexander Agrotis Patricia V. Aguilar S. Tariq Ahmad Zubair M. Ahmed Ulises Ahumada-Castro Sonja Aits Shu Aizawa Yunus Akkoç Tonia Akoumianaki Hafize Aysin Akpinar Ahmed M. Al‐Abd Lina Al-Akra Abeer Gharaibeh Moulay A. Alaoui‐Jamali Simon Alberti Elísabet Alcocer‐Gómez Cristiano Alessandri Muhammad Ali Md. Abdul Alim Al‐Bari Saeb Aliwaini Javad Alizadeh Eugènia Almacellas Alexandru Almasan Alicia Alonso G. Alonso Nihal Altan‐Bonnet Dario C. Altieri Élida Álvarez Sara Alves Cristine Alvès da Costa Mazen M. Alzaharna Marialaura Amadio Consuelo Amantini Cristina Amaral Susanna Ambrosio Amal O. Amer Veena Ammanathan Zhenyi An Stig Uggerhøj Andersen Shaida A. Andrabi Magaiver Andrade-Silva Allen M. Andres Sabrina Angelini David K. Ann Uche C. Anozie Mohammad Y. Ansari Pedro Antas Adam Antebi Zuriñe Antón Tahira Anwar Lionel Apétoh Nadezda Apostolova Toshiyuki Araki Yasuhiro Araki Kohei Arasaki Wagner L. Araújo Jun Araya Catherine Arden María‐Ángeles Arévalo Sandro Argüelles Esperanza Arias Jyothi Arikkath Hirokazu Arimoto Aileen Ariosa Darius Armstrong‐James Laetitia Pelloquin Ángeles Aroca Daniela S. Arroyo Ivica Arsov Rubén Artero Dalia Maria Lucia Asaro Michael Aschner Milad Ashrafizadeh Osnat Ashur‐Fabian Atanas G. Atanasov Alicia K. Au Patrick Auberger Holger W. Auner Laure Aurelian

In 2008, we published the first set of guidelines for standardizing research in autophagy. Since then, this topic has received increasing attention, and many scientists have entered field. Our knowledge base relevant new technologies also been expanding. Thus, it is important to formulate on a regular basis updated monitoring autophagy different organisms. Despite numerous reviews, there continues be confusion regarding acceptable methods evaluate autophagy, especially multicellular...

10.1080/15548627.2020.1797280 article EN cc-by-nc-sa Autophagy 2021-01-02

RNA and membraneless organelles Membraneless compartments can form in cells through liquidliquid phase separation (see the Perspective by Polymenidou). But what prevents these cellular condensates from randomly fusing together? Using RNA-binding protein (RBP) Whi3, Langdon et al. demonstrated that secondary structure of different components determines distinct biophysical biological properties two types Whi3 forms. Several RBPs, such as FUS TDP43, contain prion-like domains are linked to...

10.1126/science.aar7366 article EN Science 2018-04-12

ATP boosts protein solubility Adenosine triphosphate (ATP) has well-characterized roles in providing energy for biochemical reactions within cells. Patel et al. find that may also enhance solubility, which could help explain why such high concentrations of are maintained cells (see the Perspective by Rice and Rosen). Protein can exceed 100 mg/ml. The authors found at act as a hydrotrope to solubilize hydrophobic proteins. results raise possibility influence processes aggregation occur...

10.1126/science.aaf6846 article EN Science 2017-05-18

Stressed cells shut down translation, release mRNA molecules from polysomes, and form stress granules (SGs) via a network of interactions that involve G3BP. Here we focus on the mechanistic underpinnings SG assembly. We show that, under non-stress conditions, G3BP adopts compact auto-inhibited state stabilized by electrostatic intramolecular between intrinsically disordered acidic tracts positively charged arginine-rich region. Upon unfolded mRNAs outcompete auto-inhibitory interactions,...

10.1016/j.cell.2020.03.049 article EN cc-by-nc-nd Cell 2020-04-01

Biophysical responses of proteins to stress Much recent work has focused on liquid-liquid phase separation as a cellular response changing physicochemical conditions. Because responds critically small changes in conditions such pH, temperature, or salt, it is principle an ideal way for cell measure and respond the environment. Small pH could, instance, induce compartments that store, protect, inactivate proteins. Franzmann et al. used yeast translation termination factor Sup35 model...

10.1126/science.aao5654 article EN Science 2018-01-05

10.1016/j.cub.2017.08.069 article EN publisher-specific-oa Current Biology 2017-10-01

RNA-protein (RNP) granules have been proposed to assemble by forming solid RNA/protein aggregates or through phase separation into a liquid phase. Which model describes RNP in living cells is still unclear. In this study, we analyze P bodies budding yeast and find that they liquid-like properties. Surprisingly, stress adopt different material state, which reminiscent of protein controlled disaggregases. By using an assay ectopically nucleate granules, further establish granule formation does...

10.7554/elife.06807 article EN cc-by eLife 2015-08-03

In the post-genomic era, academic and biotechnological research is increasingly shifting its attention from single proteins to analysis of complex protein networks. This change in experimental design requires use simple experimentally tractable organisms, such as unicellular eukaryote Saccharomyces cerevisiae, a range new high-throughput techniques. The Gateway system has emerged powerful cloning method that allows for vitro recombination DNA with high speed, accuracy reliability. Two...

10.1002/yea.1502 article EN Yeast 2007-06-21

Cells can enter into a dormant state when faced with unfavorable conditions. However, how cells and recover from this is still poorly understood. Here, we study dormancy in different eukaryotic organisms find it to be associated significant decrease the mobility of organelles foreign tracer particles. We show that reduced caused by an influx protons marked acidification cytoplasm, which leads widespread macromolecular assembly proteins triggers transition cytoplasm solid-like increased...

10.7554/elife.09347 article EN cc-by eLife 2016-03-22

Article4 April 2017Open Access Transparent process An aberrant phase transition of stress granules triggered by misfolded protein and prevented chaperone function Daniel Mateju Max Planck Institute Molecular Cell Biology Genetics, Dresden, Germany Search for more papers this author Titus M Franzmann Avinash Patel Andrii Kopach Edgar E Boczek Shovamayee Maharana Hyun O Lee Serena Carra Department Biomedical, Metabolic Neural Sciences, University Modena Reggio Emilia, Modena, Italy Anthony A...

10.15252/embj.201695957 article EN cc-by The EMBO Journal 2017-04-04

Abstract Liquid–liquid phase separation of proteins underpins the formation membraneless compartments in living cells. Elucidating molecular driving forces underlying protein transitions is therefore a key objective for understanding biological function and malfunction. Here we show that cellular proteins, which form condensates at low salt concentrations, including FUS, TDP-43, Brd4, Sox2, Annexin A11, can reenter phase-separated regime high concentrations. By bringing together experiments...

10.1038/s41467-021-21181-9 article EN cc-by Nature Communications 2021-02-17

Non-centrosomal microtubule bundles play important roles in cellular organization and function. Although many diverse proteins are known that can bundle microtubules, biochemical mechanisms by which cells could locally control the nucleation formation of understudied. Here, we demonstrate concentration tubulin into a condensed, liquid-like compartment composed unstructured neuronal protein tau is sufficient to nucleate bundles. We show that, under conditions macro-molecular crowding, forms...

10.1016/j.celrep.2017.08.042 article EN cc-by-nc-nd Cell Reports 2017-09-01

The formation of membrane-less organelles and compartments by protein phase separation is an important way in which cells organize their cytoplasm nucleoplasm. In vitro assays with purified proteins have become the standard to investigate that form compartments. By now, various been tested for ability separate liquid condensates vitro. However, phase-separating are often aggregation-prone difficult purify handle. As a consequence, results from differ between labs not easily reproduced. Thus,...

10.1016/j.jmb.2018.06.038 article EN cc-by Journal of Molecular Biology 2018-06-23
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