• Visit the USI website
  • Go back to the homepage

Institute for Research in Biomedicine
Istituto di Ricerca in Biomedicina

Via Vincenzo Vela 6 - CH-6500 Bellinzona
Tel. +41 91 820 0300 - Fax +41 91 820 0302 - info [at] irb [dot] usi [dot] ch

Tatiana Soldà

Controllo della produzione proteica

Scientist

Via Vela, 6
6500 Bellinzona, Switzerland

Progetti
Substrate-Specific Mechanisms of Protein Degradation from the ER
Novel Protein Quality Checkpoints
Disposal of Non-Glycosylated Polypeptides from the Mammalian ER
Comparative Interactomics to Identify Novel ER-Resident Quality Control Players
Pubblicazioni
ER-to-lysosome-associated degradation of proteasome-resistant ATZ polymers occurs via receptor-mediated vesicular transport
I. Fregno, E. Fasana, T. J. Bergmann, A. Raimondi, M. Loi, T. Solda, C. Galli, R. D'Antuono, D. Morone, A. Danieli, P. Paganetti, E. van Anken, M. Molinari
in EMBO J (2018)
The reductase TMX1 contributes to ERAD by preferentially acting on membrane-associated folding-defective polypeptides
C. Guerra, G. B. Pisoni, T. Solda, M. Molinari
in Biochem Biophys Res Commun (2018)
Translocon component Sec62 acts in endoplasmic reticulum turnover during stress recovery
F. Fumagalli, J. Noack, T. J. Bergmann, E. C. Presmanes, G. B. Pisoni, E. Fasana, I. Fregno, C. Galli, M. Loi, T. Solda, R. D'Antuono, A. Raimondi, M. Jung, A. Melnyk, S. Schorr, A. Schreiber, L. Simonelli, L. Varani, C. Wilson-Zbinden, O. Zerbe, K. Hofmann, M. Peter, M. Quadroni, R. Zimmermann, M. Molinari
in Nat Cell Biol (2016) vol. 18 pp1173-1184
Fumagalli, F. , Noack J. and Bergmann T. contributed equally to this work. * Recommended by the Faculty of 1000
The Protein-disulfide Isomerase ERp57 Regulates the Steady-state Levels of the Prion Protein
M. Torres, D. B. Medinas, J. M. Matamala, U. Woehlbier, V. H. Cornejo, T. Solda, C. Andreu, P. Rozas, S. Matus, N. Munoz, C. Vergara, L. Cartier, C. Soto, M. Molinari, C. Hetz
in J Biol Chem (2015) vol. 290 pp23631-45
A novel UGGT1 and p97-dependent checkpoint for native ectodomains with ionizable intramembrane residue
J. Merulla, T. Solda, M. Molinari
in Mol Biol Cell (2015) vol. 26 pp1532-42
* Recommended by the Faculty of 1000
Specificity and regulation of the endoplasmic reticulum-associated degradation machinery
J. Merulla, E. Fasana, T. Solda, M. Molinari
in Traffic (2013) vol. 14 pp767-77
Malectin Participates in a Backup Glycoprotein Quality Control Pathway in the Mammalian ER
C. Galli, R. Bernasconi, T. Solda, V. Calanca, M. Molinari
in PLoS One (2011) vol. 6 ppe16304
Cyclosporine a-sensitive, cyclophilin B-dependent endoplasmic reticulum-associated degradation
R. Bernasconi, T. Solda, C. Galli, T. Pertel, J. Luban, M. Molinari
in PLoS One (2010) vol. 5 ppe13008
Substrate-specific requirements for UGT1-dependent release from calnexin
T. Solda, C. Galli, R. J. Kaufman, M. Molinari
in Mol Cell (2007) vol. 27 pp238-49
Consequences of ERp57 deletion on oxidative folding of obligate and facultative clients of the calnexin cycle
T. Solda, N. Garbi, G. J. Hammerling, M. Molinari
in J Biol Chem (2006) vol. 281 pp6219-26
Analyzing folding and degradation of metabolically labelled polypeptides by conventional and diagonal sodium dodecyl sulfate-polyacrylamide gel electrophoresis
T. Solda, S. Olivari, M. Molinari
in Biol Proced Online (2005) vol. 7 pp136-43