Author

I. Pritisanac

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biochemistry· 3 Biophysics· 2 Cell Biology· 1 Scientific Communication & Education· 1

Signature Assays, Organisms & Methods

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Organism:human· 4 Research Focus:cell signaling & trafficking· 3 Research Focus:protein folding & dynamics· 3 Assay:proteomics· 3 Approach:deep learning· 2 Approach:experimental assay· 2 Assay:protein structure· 2 Research Focus:protein structure prediction· 2

Frequent Co-Authors

T. R. Alderson· 4 shared J. D. Forman-Kay· 3 shared A. M. Moses· 2 shared H. Y. Gastall· 2 shared J. L. P. Benesch· 2 shared A. Baldwin· 1 shared A. Bax· 1 shared A. Chong· 1 shared

Activity by Year

2018-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 17 mutual co-author links

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4 shared papersBiochemistry

T. R. Alderson

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Author profile →

7 papers

Recent·Most cited

MIADE metadata guidelines: Minimum Information About a Disorder Experiment

B. Meszaros, A. Hatos, N. Palopoli, F. Quaglia, E. Salladini, K. Van Roey, H. Arthanari, Z. Dosztanyi, I. C. Felli, P. D. Fischer, J. Hoch, C. M. Jeffries, S. Longhi, E. Maiani, S. Orchard, , N. E. Davey

The paper introduces MIADE guidelines to standardize metadata for experiments studying intrinsically disordered proteins, improving data interpretation and reproducibility.

bioRxiv · Jul 12, 2022 · PreprintScientific Communication & Education

Systematic identification of conditionally folded intrinsically disordered regions by AlphaFold2

T. R. Alderson, I. Pritisanac, Đesika Kolaric, A. M. Moses, J. D. Forman-Kay

This paper shows AlphaFold2 can predict structures of conditionally folded intrinsically disordered regions with high precision, revealing their prevalence in human and prokaryotic proteins and their association with disease mutations.

bioRxiv · Feb 18, 2022Biochemistry

O-GlcNAcylation reduces phase separation and aggregation of the EWS N-terminal low complexity region

M. L. Nosella, M. Tereshchenko, I. Pritisanac, A. Chong, J. A. Toretsky, H. O. Lee, J. D. Forman-Kay

bioRxiv · May 11, 2021 · PreprintBiochemistry

Identifying molecular features that are associated with biological function of intrinsically disordered protein regions

T. Zarin, B. Strome, G. Peng, I. Pritisanac, J. D. Forman-Kay, A. M. Moses

The paper identifies molecular features in intrinsically disordered protein regions that predict functional roles and validates their importance in mitochondrial targeting.

bioRxiv · Jun 23, 2020Cell Biology

Dysregulated interactions triggered by a neuropathy-causing mutation in the IPV motif of HSP27

T. R. Alderson, E. Adriaenssens, B. Asselbergh, I. Pritisanac, H. Y. Gastall, M. A. Walti, J. M. Louis, V. Timmerman, A. Baldwin, J. L. P. Benesch

This study investigates how the P182L mutation in HSP27's IxI/V motif disrupts protein interactions, leading to aggregation and disease.

bioRxiv · Sep 10, 2019 · PreprintBiochemistry

Automatic structure-based NMR methyl resonance assignment in large proteins

I. Pritisanac, J. M. Würz, T. R. Alderson, P. Güntert

MethylFLYA automatically assigns methyl groups in large proteins using NOESY data, achieving high accuracy and efficiency compared to manual methods.

bioRxiv · Apr 4, 2019Biophysics

Local unfolding of the HSP27 monomer regulates chaperone activity

T. R. Alderson, J. Roche, H. Y. Gastall, I. Pritisanac, J. Ying, A. Bax, J. L. P. Benesch, A. J. Baldwin

This study shows that redox-induced monomerization of HSP27 enhances its chaperone activity but also increases aggregation risk, with mutations in an unstructured region linked to neuropathies.

bioRxiv · Jun 14, 2018Biophysics