Valeria Pesiri
Overview
Explore the profile of Valeria Pesiri including associated specialties, affiliations and a list of published articles.
Author names and details appear as published. Due to indexing inconsistencies, multiple individuals may share a name, and a single author may have variations. MedLuna displays this data as publicly available, without modification or verification
Snapshot
Snapshot
Articles
8
Citations
135
Followers
0
Related Specialties
Related Specialties
Top 10 Co-Authors
Top 10 Co-Authors
Published In
Published In
Affiliations
Affiliations
Soon will be listed here.
Recent Articles
1.
Pesiri V, Di Muzio E, Polticelli F, Acconcia F
IUBMB Life
. 2016 May;
68(7):569-77.
PMID: 27193211
Ubiquitin (Ub)-binding domains (UBDs) noncovalently contact the Ub modification on binding partners. Ub possesses seven lysine (K) residues (i.e., K6, K11, K27, K29, K33, K48, and K63) that can be...
2.
Pesiri V, Totta P, Segatto M, Bianchi F, Pallottini V, Marino M, et al.
Cell Signal
. 2015 Sep;
27(12):2380-8.
PMID: 26348925
17β-Estradiol (E2)-dependent cell proliferation requires both estrogen receptor α (ERα)-based integrated control of gene transcription and kinase pathways activation. Such coordination of intracellular E2:ERα-dependent signaling mechanisms is finely tuned by...
3.
Totta P, Pesiri V, Enari M, Marino M, Acconcia F
Mol Endocrinol
. 2015 Apr;
29(5):739-55.
PMID: 25860340
17β-estradiol (E2)-induced signaling and control of estrogen receptor (ER)α degradation both play a major role in breast cancer cell proliferation. We recently reported the involvement of lysosomal function in both...
4.
Pesiri V, Totta P, Marino M, Acconcia F
IUBMB Life
. 2014 Aug;
66(8):578-85.
PMID: 25138535
The sex steroid hormone 17β-estradiol (E2) regulates breast cancer (BC) cell proliferation and migration through the activation of a plethora of signal transduction cascades (e.g., PI3K/AKT activation) starting after E2...
5.
Totta P, Pesiri V, Marino M, Acconcia F
PLoS One
. 2014 Apr;
9(4):e94880.
PMID: 24736371
The homeostatic control of the cellular proteome steady-state is dependent either on the 26S proteasome activity or on the lysosome function. The sex hormone 17β-estradiol (E2) controls a plethora of...
6.
Pesiri V, La Rosa P, Stano P, Acconcia F
J Cell Sci
. 2013 Apr;
126(Pt 12):2577-82.
PMID: 23591816
Ubiquitin (Ub)-binding domains (UBDs) located in Ub receptors decode the ubiquitination signal by non-covalently engaging the Ub modification on their binding partners and transduce the Ub signalling through Ub-based molecular...
7.
La Rosa P, Pesiri V, Leclercq G, Marino M, Acconcia F
Mol Endocrinol
. 2012 Mar;
26(5):762-74.
PMID: 22446104
The estrogen receptor-α (ERα) is a transcription factor that regulates gene expression through the binding to its cognate hormone 17β-estradiol (E2). ERα transcriptional activity is regulated by E2-evoked 26S proteasome-mediated...
8.
La Rosa P, Pesiri V, Marino M, Acconcia F
Cell Signal
. 2011 Mar;
23(7):1128-35.
PMID: 21356307
Protein monoubiquitination (monoUbq) (i.e., the attachment of one single ubiquitin to the substrate) is a non-proteolytic reversible modification that controls protein functions. Among other proteins, the estrogen receptor α (ERα),...