I
Iva Pritišanac
Researcher at University of Toronto
Publications - 34
Citations - 522
Iva Pritišanac is an academic researcher from University of Toronto. The author has contributed to research in topics: Biology & Computer science. The author has an hindex of 6, co-authored 27 publications receiving 213 citations. Previous affiliations of Iva Pritišanac include University of Oxford & Hospital for Sick Children.
Papers
More filters
Journal ArticleDOI
Phase Separation as a Missing Mechanism for Interpretation of Disease Mutations
TL;DR: The authors found that autism spectrum disorder (ASD) and cancer-associated proteins are enriched for predicted phase separation propensities, suggesting that IDR mutations disrupt phase separation in key cellular processes.
Journal ArticleDOI
Local unfolding of the HSP27 monomer regulates chaperone activity.
T. Reid Alderson,T. Reid Alderson,Julien Roche,Julien Roche,Heidi Y. Gastall,David M. Dias,Iva Pritišanac,Jinfa Ying,Ad Bax,Justin L. P. Benesch,Andrew Baldwin +10 more
TL;DR: While HSP27 assembles into oligomers, it is shown that the monomers formed upon reduction are highly active chaperones in vitro, but are susceptible to self-aggregation.
Journal ArticleDOI
Automatic Assignment of Methyl-NMR Spectra of Supramolecular Machines Using Graph Theory
Iva Pritišanac,Matteo T. Degiacomi,T. Reid Alderson,Marta G Carneiro,Eiso Ab,Gregg Siegal,Andrew Baldwin +6 more
TL;DR: By providing an exact and robust solution to methyl resonance assignment, MAGMA can facilitate significantly accelerated studies of supramolecular machines using methyl-based NMR spectroscopy and enables a user to distinguish between alternative protein structures.
Journal ArticleDOI
Entropy and Information within Intrinsically Disordered Protein Regions
TL;DR: It is argued that the information in IDR sequences cannot be fully revealed through positional conservation, which largely measures stable structural contacts and interaction motifs, and instead considerations of evolutionary conservation of molecular features can reveal the full extent of information inIDRs.
Posted ContentDOI
Systematic identification of conditionally folded intrinsically disordered regions by AlphaFold2
TL;DR: A large majority of IDR sequences in the proteomes of human and other eukaryotes would be expected to function in the absence of conditional folding, and up to 80% of IDRs in archaea and bacteria are predicted to conditionally fold, but less than 20% of eUKaryotic IDRs.