Gabriela Chiosis
Overview
Explore the profile of Gabriela Chiosis including associated specialties, affiliations and a list of published articles.
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169
Citations
6235
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Recent Articles
11.
Bay S, Digwal C, Rodilla Martin A, Sharma S, Stanisavljevic A, Rodina A, et al.
Biomedicines
. 2024 Jun;
12(6).
PMID: 38927459
Neurodegenerative disorders, including Alzheimer's disease (AD) and Parkinson's disease (PD), represent debilitating conditions with complex, poorly understood pathologies. Epichaperomes, pathologic protein assemblies nucleated on key chaperones, have emerged as critical...
12.
McNutt S, Roychowdhury T, Pasala C, Nguyen H, Thornton D, Sharma S, et al.
Res Sq
. 2024 Apr;
PMID: 38645031
The intricate protein-chaperone network is vital for cellular function. Recent discoveries have unveiled the existence of specialized chaperone complexes called epichaperomes, protein assemblies orchestrating the reconfiguration of protein-protein interaction networks,...
13.
Cerchietti L, Lopes E, Yang S, Hatzi K, Bunting K, Tsikitas L, et al.
Nat Med
. 2024 Apr;
30(5):1503.
PMID: 38570701
No abstract available.
14.
Pasala C, Sharma S, Roychowdhury T, Moroni E, Colombo G, Chiosis G
Biomolecules
. 2024 Mar;
14(3).
PMID: 38540703
Glycosylation, a prevalent post-translational modification, plays a pivotal role in regulating intricate cellular processes by covalently attaching glycans to macromolecules. Dysregulated glycosylation is linked to a spectrum of diseases, encompassing...
15.
Mayer M, Blair L, Blatch G, Borges T, Chadli A, Chiosis G, et al.
Cell Stress Chaperones
. 2024 Feb;
29(1):143-157.
PMID: 38311120
Preserving and regulating cellular homeostasis in the light of changing environmental conditions or developmental processes is of pivotal importance for single cellular and multicellular organisms alike. To counteract an imbalance...
16.
Sharma S, Joshi S, Kalidindi T, Digwal C, Panchal P, Lee S, et al.
Biomedicines
. 2023 Oct;
11(10).
PMID: 37892973
Drugs with a long residence time at their target sites are often more efficacious in disease treatment. The mechanism, however, behind prolonged retention at the site of action is often...
17.
Svirsky S, Li Y, Henchir J, Rodina A, Carlson S, Chiosis G, et al.
Neurobiol Dis
. 2023 Oct;
188:106331.
PMID: 37863370
Under normal conditions, heat shock proteins work in unison through dynamic protein interactions collectively referred to as the "chaperome." Recent work revealed that during cellular stress, the functional interactions of...
18.
Que N, Seidler P, Aw W, Chiosis G, Gewirth D
bioRxiv
. 2023 Aug;
PMID: 37577523
Grp94 is the endoplasmic reticulum paralog of the hsp90 family of chaperones, which have been targeted for therapeutic intervention via their highly conserved ATP binding sites. The design of paralog-selective...
19.
Roychowdhury T, Santhaseela A, Sharma S, Panchal P, Rodina A, Chiosis G
Methods Mol Biol
. 2023 Aug;
2693:175-191.
PMID: 37540435
Epichaperomes are disease-associated pathologic scaffolds, composed of tightly bound chaperones, co-chaperones, and other factors. They mediate anomalous protein-protein interactions inside cells, which aberrantly affects the function of protein networks, and...
20.
Chiosis G, Digwal C, Trepel J, Neckers L
Nat Rev Mol Cell Biol
. 2023 Jul;
24(11):797-815.
PMID: 37524848
Heat shock protein 90 (HSP90) is a chaperone with vital roles in regulating proteostasis, long recognized for its function in protein folding and maturation. A view is emerging that identifies...