Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Edgar E. Boczek"'
Autor:
Edgar E Boczek, Julius Fürsch, Marie Laura Niedermeier, Louise Jawerth, Marcus Jahnel, Martine Ruer-Gruß, Kai-Michael Kammer, Peter Heid, Laura Mediani, Jie Wang, Xiao Yan, Andrej Pozniakovski, Ina Poser, Daniel Mateju, Lars Hubatsch, Serena Carra, Simon Alberti, Anthony A Hyman, Florian Stengel
Publikováno v:
eLife, Vol 10 (2021)
Aberrant liquid-to-solid phase transitions of biomolecular condensates have been linked to various neurodegenerative diseases. However, the underlying molecular interactions that drive aging remain enigmatic. Here, we develop quantitative time-resolv
Externí odkaz:
https://doaj.org/article/85bf8344d0894177804ff718a7d76096
Autor:
Lars Hubatsch, Martine Ruer-Gruß, Xiao Yan, Andrej Pozniakovski, Ina Poser, Serena Carra, Marcus Jahnel, Laura Mediani, Peter Heid, Julius Fürsch, Louise Jawerth, Kai-Michael Kammer, Daniel Mateju, Jie Wang, Edgar E. Boczek, Marie Laura Niedermeier, Simon Alberti, Florian Stengel, Anthony A. Hyman
Publikováno v:
eLife
eLife, Vol 10 (2021)
eLife, Vol 10 (2021)
SummaryAberrant liquid-to-solid phase transitions of biomolecular condensates have been linked to various neurodegenerative diseases. However, the underlying molecular interactions that drive aging remain enigmatic. Here, we develop quantitative time
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ba0a083a6ef4852415e82562aac28413
http://europepmc.org/articles/PMC8510580
http://europepmc.org/articles/PMC8510580
Autor:
Jie Wang, Lars Hubatsch, Louise Jawerth, Ina Poser, Kai-Michael Kammer, Daniel Mateju, Andrej Pozniakovski, Edgar E. Boczek, Xiao Yan, Serena Carra, Laura Mediani, Marie Laura Niedermeier, Peter Heid, Julius Fürsch, Marcus Jahnel, Simon Alberti, Anthony A. Hyman, Florian Stengel, Martine Ruer-Gruß
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a50071ce19bfdc804160b234916e293d
https://doi.org/10.7554/elife.69377.sa2
https://doi.org/10.7554/elife.69377.sa2
Autor:
Kamran Rizzolo, Sadhna Phanse, Michael Costanzo, Charles Boone, Igor Stagljar, Hussein A. Zeineddine, Edgar E. Boczek, Mohan Babu, Carles Pons, Simon Alberti, Wen Wang, Chad L. Myers, Jennifer Huen, Walid A. Houry, James Vlasblom, Yoshito Kakihara, Jamie Snider, Ashwani Kumar, Zoran Minic, Thiago V. Seraphim
Publikováno v:
Cell Reports, Vol 20, Iss 11, Pp 2735-2748 (2017)
Summary A comprehensive view of molecular chaperone function in the cell was obtained through a systematic global integrative network approach based on physical (protein-protein) and genetic (gene-gene or epistatic) interaction mapping. This allowed
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dd3afac8eada2477b3130775654e710a
http://www.sciencedirect.com/science/article/pii/S2211124717312160
http://www.sciencedirect.com/science/article/pii/S2211124717312160
Autor:
Simon Alberti, Edgar E. Boczek
Publikováno v:
The Journal of Cell Biology
Boczek and Alberti discuss work from Grousl et al. describing how the heat shock protein Hsp42 binds and sequesters misfolded proteins.
Small heat shock proteins (sHsps) are adenosine triphosphate–independent chaperones that protect cells from
Small heat shock proteins (sHsps) are adenosine triphosphate–independent chaperones that protect cells from
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::90a578bafaee991f849876678fa35dcc
http://europepmc.org/articles/PMC5881514
http://europepmc.org/articles/PMC5881514
Autor:
Andreas Hermann, Lara Marrone, Arun Pal, Simon Alberti, Marcus Jahnel, Benjamin G. Davis, Nicolas L. Fawzi, Anatol Fritsch, Richard J. Wheeler, S Kishigami, Della C. David, Xiaojie Zhang, Anthony A. Hyman, Jared Sterneckert, T Doeleman, Hsin-Ju Lee, Anastasia C Murthy, Marc Bickle, Eric N. Anderson, Edgar E. Boczek, Andrew Baldwin, Ina Poser, Sukhleen Kour, Udai Bhan Pandey
Amyotrophic lateral sclerosis (ALS) is a neurodegenerative disease with few avenues for treatment. Many proteins implicated in ALS associate with stress granules, which are examples of liquid-like compartments formed by phase separation. Aberrant pha
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d118b62755f201552e746e0ba2642e12
The first Autumn School on Proteostasis was held at the Mediterranean Institute for Life Sciences (MedILS) in Split, Croatia, from November 12th–16th, 2018, bringing together 44 graduate students and postdoctoral fellows and 22 principal investigat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3d954a89d80f0db1a09395135cd3ad1d
https://europepmc.org/articles/PMC6527634/
https://europepmc.org/articles/PMC6527634/
Autor:
Sophie L. Mader, Michael Röpke, Andreas Seidl, Edgar E. Boczek, Marco Dehling, Johannes Buchner, Qi Luo, Ville R. I. Kaila
Publikováno v:
J Biol Chem
The prototypical kinase c-Src plays an important role in numerous signal transduction pathways, where its activity is tightly regulated by two phosphorylation events. Phosphorylation at a specific tyrosine by C-terminal Src kinase inactivates c-Src,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b3a95b47045d25b1878f6c59f8841203
https://pubmed.ncbi.nlm.nih.gov/31331936
https://pubmed.ncbi.nlm.nih.gov/31331936
Autor:
Edgar E. Boczek, Simon Alberti
Publikováno v:
Science. 361:548-549
Synaptic vesicles cluster by partitioning into phase-separated condensates
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b3b9d48e6ed1664531919f51bd146af7
https://doi.org/10.1126/science.aau5477
https://doi.org/10.1126/science.aau5477
Publikováno v:
Scientific Reports
Heat shock protein 90 (Hsp90) is an abundant molecular chaperone, involved in the folding and activation of 60% of the human kinome. The oncogenic tyrosine kinase v-Src is one of the most stringent client proteins of Hsp90, whereas its almost identic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::16238a33be52c68656749cea4d7270c9
https://pubmed.ncbi.nlm.nih.gov/28290541
https://pubmed.ncbi.nlm.nih.gov/28290541