Witold K. Surewicz

Biochemistry, Genetics and Molecular BiologyNursingNeuroscienceMedicine

Pilot corpus only

This score is computed over theSindex pilot corpus and does not cover the full scientific literature. Scores are relative to papers we have ingested — papers, authors, and institutions outside the pilot are not represented. Methodology.

Top 100%percentile

0Author DataRank

Indexed papers

0in pilot corpus

datarank_citation_only_1hop_v6· scope data_onlyMethodology

Papers

Driven by 20 papers. Top paper: “Small molecules as potent biphasic modulators of protein liquid-liquid phase separation”.

Small molecules as potent biphasic modulators of protein liquid-liquid phase separation

Nature Communications(2020)10.1038/s41467-020-19211-z

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0DataRank · unranked

213 citations

Benjamin K. Dumm, Sarah Venus, Solomiia Boyko, Andrea Putnam, Eckhard Jankowsky +2 more

Liquid–Liquid Phase Separation and Its Mechanistic Role in Pathological Protein Aggregation

Journal of Molecular Biology(2020)10.1016/j.jmb.2020.03.004

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305 citations

Witold K. Surewicz, W. Michael Babinchak

Regulatory mechanisms of tau protein fibrillation under the conditions of liquid–liquid phase separation

Proceedings of the National Academy of Sciences(2020)10.1073/pnas.2012460117

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136 citations

Krystyna Surewicz, Witold K. Surewicz, Solomiia Boyko

Zinc promotes liquid–liquid phase separation of tau protein

Journal of Biological Chemistry(2020)10.1074/jbc.ac120.013166

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120 citations

Ling Xu, Solomiia Boyko, Krystyna Surewicz, Witold K. Surewicz, Virender Singh

A novel mechanism of phenotypic heterogeneity in Creutzfeldt-Jakob disease

Acta Neuropathologica Communications(2020)10.1186/s40478-020-00966-x

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42 citations

Xiangzhu Xiao, Ignazio Calì, Laura Cracco, Gianfranco Puoti, M. Nigro +8 more

Studying Protein Aggregation in the Context of Liquid-liquid Phase Separation Using Fluorescence and Atomic Force Microscopy, Fluorescence and Turbidity Assays, and FRAP

BIO-PROTOCOL(2020)10.21769/bioprotoc.3489

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24 citations

W. Michael Babinchak, Witold K. Surewicz

13C and 15N chemical shift assignments of A117V and M129V human Y145Stop prion protein amyloid fibrils

Biomolecular NMR Assignments(2020)10.1007/s12104-020-09981-4

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3 citations

May Z. Hlaing, Yixuan Ma, Krystyna Surewicz, Witold K. Surewicz, Christopher P. Jaroniec +1 more

Cryo-EM structure of amyloid fibrils formed by the entire low complexity domain of TDP-43

bioRxiv (Cold Spring Harbor Laboratory)(2020)10.1101/2020.12.14.422689

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27 citations

W. Michael Babinchak, Witold K. Surewicz, Qiuye Li

Cryo-EM structure of amyloid fibrils formed by the entire low complexity domain of TDP-43

Nature Communications(2021)10.1038/s41467-021-21912-y

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144 citations

W. Michael Babinchak, Witold K. Surewicz, Qiuye Li

Cryo-EM structure of disease-related prion fibrils provides insights into seeding barriers

bioRxiv (Cold Spring Harbor Laboratory)(2021)10.1101/2021.08.10.455830

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7 citations

Christopher P. Jaroniec, Witold K. Surewicz, Qiuye Li

Tau liquid–liquid phase separation in neurodegenerative diseases

Trends in Cell Biology(2022)10.1016/j.tcb.2022.01.011

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197 citations

Witold K. Surewicz, Solomiia Boyko

Influence of the Dynamically Disordered N-Terminal Tail Domain on the Amyloid Core Structure of Human Y145Stop Prion Protein Fibrils

Frontiers in Molecular Biosciences(2022)10.3389/fmolb.2022.841790

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5 citations

Krystyna Surewicz, Witold K. Surewicz, Christopher P. Jaroniec, Zhe Qi

Domain-specific modulatory effects of phosphomimetic substitutions on liquid-liquid phase separation of tau protein

Journal of Biological Chemistry(2023)10.1016/j.jbc.2023.104722

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18 citations

Witold K. Surewicz, Solomiia Boyko

Phosphomimetic substitutions in TDP-43’s transiently α-helical region suppress phase separation

Biophysical Journal(2024)10.1016/j.bpj.2024.01.001

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28 citations

Srinivasa R. Penumutchu, Solomiia Boyko, Witold K. Surewicz, Raza Haider

Pathological C‐terminal phosphomimetic substitutions alter the mechanism of liquid–liquid phase separation of TDP‐43 low complexity domain

Protein Science(2024)10.1002/pro.5179

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14 citations

Brandon Shipley, Krystyna Surewicz, Michael Hinczewski, Witold K. Surewicz, Raza Haider

Copper binding alters the core structure of amyloid fibrils formed by Y145Stop human prion protein

Physical Chemistry Chemical Physics(2024)10.1039/d4cp03593c

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6 citations

Tara George, Daniel W. Conroy, Zach Shaffer, Witold K. Surewicz, Christopher P. Jaroniec +1 more

Pathological C-terminal phosphomimetic substitutions alter the mechanism of liquid-liquid phase separation of TDP-43 low complexity domain

bioRxiv (Cold Spring Harbor Laboratory)(2024)10.1101/2024.03.21.586202

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1 citations

Brandon Shipley, Krystyna Surewicz, Michael Hinczewski, Witold K. Surewicz, Raza Haider

Variably protease-sensitive prionopathy: mass spectrometry analysis of the pathogenic prion protein provides a new perspective

Acta Neuropathologica Communications(2025)10.1186/s40478-025-02079-9

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0DataRank · unranked

1 citations

Xinxin Xiao, Silvio Notari, Ignazio Calì, Kristina Lundberg, Laura Cracco +5 more

Distinct liquid-liquid phase separation properties of end-binding proteins EB1 and EB3

Journal of Biological Chemistry(2025)10.1016/j.jbc.2025.110849

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1 citations

Qiuye Li, Krystyna Surewicz, Witold K. Surewicz, Solomiia Boyko

Structural exposure of different microtubule binding domains determines the propagation and toxicity of pathogenic tau conformers in Alzheimer’s disease

PLoS Pathogens(2025)10.1371/journal.ppat.1012926

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0DataRank · unranked

0 citations

Chae Kim, Tracy Haldiman, Mohammad Khursheed Siddiqi, Krystyna Surewicz, Kiley Urquhart +10 more