Výsledky vyhledávání - "Barry, Panaretou"

Akademický článek

Activation of autophagy depends on Atg1/Ulk1-mediated phosphorylation and inhibition of the Hsp90 chaperone machinery

Autor: Sarah J. Backe, Rebecca A. Sager, Jennifer A. Heritz, Laura A. Wengert, Katherine A. Meluni, Xavier Aran-Guiu, Barry Panaretou, Mark R. Woodford, Chrisostomos Prodromou, Dimitra Bourboulia, Mehdi Mollapour

Publikováno v: Cell Reports, Vol 42, Iss 7, Pp 112807- (2023)

Summary: Cellular homeostasis relies on both the chaperoning of proteins and the intracellular degradation system that delivers cytoplasmic constituents to the lysosome, a process known as autophagy. The crosstalk between these processes and their un

Externí odkaz: https://doaj.org/article/4372f2b85d70407f912e42e25ea43467

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Akademický článek

Bolaamphiphile Analogues of 12-bis-THA Cl2 Are Potent Antimicrobial Therapeutics with Distinct Mechanisms of Action against Bacterial, Mycobacterial, and Fungal Pathogens

Publikováno v: mSphere, Vol 8, Iss 1 (2023)

ABSTRACT 12-Bis-THA Cl2 [12,12′-(dodecane-1,12-diyl)-bis-(9-amino-1,2,3,4-tetrahydroacridinium) chloride] is a cationic bolalipid adapted from dequalinium chloride (DQC), a bactericidal anti-infective indicated for bacterial vaginosis (BV). Here, w

Externí odkaz: https://doaj.org/article/8625d87284694eff9568dd55269bba7a

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Akademický článek

ADAM8 signaling drives neutrophil migration and ARDS severity

Publikováno v: JCI Insight, Vol 7, Iss 3 (2022)

Acute respiratory distress syndrome (ARDS) results in catastrophic lung failure and has an urgent, unmet need for improved early recognition and therapeutic development. Neutrophil influx is a hallmark of ARDS and is associated with the release of ti

Externí odkaz: https://doaj.org/article/254cf7c552124bd6aa63f41af70b7891

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A simplified and easy‐to‐use HIP HOP assay provides insights into chalcone antifungal mechanisms of action

Autor: Thomas A. K. Prescott, Laura Anaissi‐Afonso, Keith R. Fox, Anthony Maxwell, Barry Panaretou, Félix Machín

Publikováno v: FEBS Letters. 596:3087-3102

Elucidating the mechanism of action of an antifungal or cytotoxic compound is a time-consuming process. Yeast chemogenomic profiling provides a compelling solution to the problem but is experimentally complex. Here, we demonstrate the use of a highly

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d8beb04939f1db69cd1504fcb49f3043
https://doi.org/10.1002/1873-3468.14483

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Akademický článek

The FNIP co-chaperones decelerate the Hsp90 chaperone cycle and enhance drug binding

Autor: Mark R. Woodford, Diana M. Dunn, Adam R. Blanden, Dante Capriotti, David Loiselle, Chrisostomos Prodromou, Barry Panaretou, Philip F. Hughes, Aaron Smith, Wendi Ackerman, Timothy A. Haystead, Stewart N. Loh, Dimitra Bourboulia, Laura S. Schmidt, W. Marston Linehan, Gennady Bratslavsky, Mehdi Mollapour

Publikováno v: Nature Communications, Vol 7, Iss 1, Pp 1-15 (2016)

Hsp90 is required for the folding, stability and activity of several drivers of oncogenesis. Here the authors show that Folliculin-interacting proteins (FNIP) 1 and 2, whose expression correlates with the cellular response to Hsp90 inhibitors, are co

Externí odkaz: https://doaj.org/article/51f03ab61e4442f99c334fc8fe1d2ccd

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Akademický článek

Mps1 Mediated Phosphorylation of Hsp90 Confers Renal Cell Carcinoma Sensitivity and Selectivity to Hsp90 Inhibitors

Publikováno v: Cell Reports, Vol 14, Iss 4, Pp 872-884 (2016)

The molecular chaperone Hsp90 protects deregulated signaling proteins that are vital for tumor growth and survival. Tumors generally display sensitivity and selectivity toward Hsp90 inhibitors; however, the molecular mechanism underlying this phenoty

Externí odkaz: https://doaj.org/article/94836c555dfb4543879e4bab5562ec97

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Akademický článek

c-Abl Mediated Tyrosine Phosphorylation of Aha1 Activates Its Co-chaperone Function in Cancer Cells

Publikováno v: Cell Reports, Vol 12, Iss 6, Pp 1006-1018 (2015)

The ability of Heat Shock Protein 90 (Hsp90) to hydrolyze ATP is essential for its chaperone function. The co-chaperone Aha1 stimulates Hsp90 ATPase activity, tailoring the chaperone function to specific “client” proteins. The intracellular signa

Externí odkaz: https://doaj.org/article/513261747e0342e1bf436072b173cab8

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