Anna Rodina
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Explore the profile of Anna Rodina including associated specialties, affiliations and a list of published articles.
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Recent Articles
11.
Bolaender A, Zatorska D, He H, Joshi S, Sharma S, Digwal C, et al.
Nat Commun
. 2021 Aug;
12(1):4669.
PMID: 34344873
Diseases are a manifestation of how thousands of proteins interact. In several diseases, such as cancer and Alzheimer's disease, proteome-wide disturbances in protein-protein interactions are caused by alterations to chaperome...
12.
Jhaveri K, Dos Anjos C, Taldone T, Wang R, Comen E, Fornier M, et al.
JCO Precis Oncol
. 2020 Dec;
4.
PMID: 33283132
Purpose: Epichaperome network maintenance is vital to survival of tumors that express it. PU-H71 is an epichaperome inhibitor that binds to the ATP-binding site of HSP90 and has demonstrated antitumor...
13.
Yan P, Patel H, Sharma S, Corben A, Wang T, Panchal P, et al.
Cell Rep
. 2020 Jul;
31(13):107840.
PMID: 32610141
Stresses associated with disease may pathologically remodel the proteome by both increasing interaction strength and altering interaction partners, resulting in proteome-wide connectivity dysfunctions. Chaperones play an important role in these...
14.
Inda M, Joshi S, Wang T, Bolaender A, Gandu S, Koren Iii J, et al.
Nat Commun
. 2020 Jan;
11(1):319.
PMID: 31949159
Optimal functioning of neuronal networks is critical to the complex cognitive processes of memory and executive function that deteriorate in Alzheimer's disease (AD). Here we use cellular and animal models...
15.
Pillarsetty N, Jhaveri K, Taldone T, Caldas-Lopes E, Punzalan B, Joshi S, et al.
Cancer Cell
. 2019 Nov;
36(5):559-573.e7.
PMID: 31668946
Alterations in protein-protein interaction networks are at the core of malignant transformation but have yet to be translated into appropriate diagnostic tools. We make use of the kinetic selectivity properties...
16.
Taldone T, Wang T, Rodina A, Pillarsetty N, Digwal C, Sharma S, et al.
Cold Spring Harb Perspect Biol
. 2019 Apr;
12(4).
PMID: 30936118
Cancer is often associated with alterations in the chaperome, a collection of chaperones, cochaperones, and other cofactors. Changes in the expression levels of components of the chaperome, in the interaction...
17.
Wang T, Rodina A, Dunphy M, Corben A, Modi S, Guzman M, et al.
J Biol Chem
. 2018 Nov;
294(6):2162-2179.
PMID: 30409908
The chaperome is the collection of proteins in the cell that carry out molecular chaperoning functions. Changes in the interaction strength between chaperome proteins lead to an assembly that is...
18.
Kishinevsky S, Wang T, Rodina A, Chung S, Xu C, Philip J, et al.
Nat Commun
. 2018 Oct;
9(1):4345.
PMID: 30341316
Environmental and genetic risk factors contribute to Parkinson's Disease (PD) pathogenesis and the associated midbrain dopamine (mDA) neuron loss. Here, we identify early PD pathogenic events by developing methodology that...
19.
Giulino-Roth L, van Besien H, Dalton T, Totonchy J, Rodina A, Taldone T, et al.
Mol Cancer Ther
. 2017 Jun;
16(9):1779-1790.
PMID: 28619753
Hsp90 is a molecular chaperone that protects proteins, including oncogenic signaling complexes, from proteolytic degradation. PU-H71 is a next-generation Hsp90 inhibitor that preferentially targets the functionally distinct pool of Hsp90...
20.
Rodina A, Wang T, Yan P, Gomes E, Dunphy M, Pillarsetty N, et al.
Nature
. 2016 Oct;
538(7625):397-401.
PMID: 27706135
Transient, multi-protein complexes are important facilitators of cellular functions. This includes the chaperome, an abundant protein family comprising chaperones, co-chaperones, adaptors, and folding enzymes-dynamic complexes of which regulate cellular homeostasis...