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Anna Rodina

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Articles 44
Citations 1901
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Recent Articles
1.
Bay S, Rodina A, Haut F, Roychowdhury T, Argyrousi E, Staniszewski A, et al.
Res Sq . 2025 Feb; PMID: 39989971
Alzheimer's disease (AD) progresses as a continuum, from preclinical stages to late-stage cognitive decline, yet the molecular mechanisms driving this progression remain poorly understood. Here, we provide a systems-level map...
2.
Roychowdhury T, McNutt S, Pasala C, Nguyen H, Thornton D, Sharma S, et al.
Nat Commun . 2024 Oct; 15(1):8912. PMID: 39414766
The intricate network of protein-chaperone interactions is crucial for maintaining cellular function. Recent discoveries have unveiled the existence of specialized chaperone assemblies, known as epichaperomes, which serve as scaffolding platforms...
3.
Magni A, Sciva C, Castelli M, Digwal C, Rodina A, Sharma S, et al.
Chemistry . 2024 Jul; 30(54):e202401957. PMID: 39042517
Post-translational modifications such as protein N-glycosylation, significantly influence cellular processes. Dysregulated N-glycosylation, exemplified in Grp94, a member of the Hsp90 family, leads to structural changes and the formation of epichaperomes,...
4.
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...
5.
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,...
6.
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...
7.
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...
8.
Rodina A, Xu C, Digwal C, Joshi S, Patel Y, Santhaseela A, et al.
Nat Commun . 2023 Jun; 14(1):3742. PMID: 37353488
Systems-level assessments of protein-protein interaction (PPI) network dysfunctions are currently out-of-reach because approaches enabling proteome-wide identification, analysis, and modulation of context-specific PPI changes in native (unengineered) cells and tissues are...
9.
Castelli M, Yan P, Rodina A, Digwal C, Panchal P, Chiosis G, et al.
Structure . 2023 Jun; 31(8):987-1004.e8. PMID: 37343552
Protein-assembly defects due to an enrichment of aberrant conformational protein variants are emerging as a new frontier in therapeutics design. Understanding the structural elements that rewire the conformational dynamics of...
10.
Joshi S, Gomes E, Wang T, Corben A, Taldone T, Gandu S, et al.
Commun Biol . 2021 Nov; 4(1):1333. PMID: 34824367
Cancer cell plasticity due to the dynamic architecture of interactome networks provides a vexing outlet for therapy evasion. Here, through chemical biology approaches for systems level exploration of protein connectivity...