Author

N. Kalisman

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· 3

Signature Assays, Organisms & Methods

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Assay:proteomics· 6 Approach:experimental assay· 4 Research Focus:protein folding & dynamics· 4 Approach:statistical model· 3 Research Focus:cell type annotation· 2 Organism:human· 2 Approach:biophysical modeling· 1 Research Focus:cell signaling & trafficking· 1

Frequent Co-Authors

J. Zamel· 5 shared E. Lerner· 3 shared M. Slavin· 3 shared D. Schneidman-Duhovny· 2 shared J. Chen· 2 shared K. Joron· 2 shared K. Zohar· 2 shared M. Linial· 2 shared

Activity by Year

2019-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 25 mutual co-author links

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5 shared papersBiophysics

J. Zamel

Mutual co-authors in cluster

Author profile →

6 papers

Recent·Most cited

The Interactome of DUX4 Reveals Multiple Activation Pathways

M. Slavin, K. Zohar, C. Claus, D. Schneidman-Duhovny, M. Linial, F. Coppee, N. Kalisman

This study identifies new DUX4 protein interactions and activation pathways using AP-MS and CL-MS, revealing structural and functional insights into its role in FSHD.

bioRxiv · Sep 12, 2023 · PreprintBiochemistry

Structural and Dynamic Insights Into α-Synuclein Dimer Conformations

J. Zamel, J. Chen, S. Zaer, P. D. Harris, P. Drori, M. Lebendiker, N. Kalisman, N. V. Dokholyan, E. Lerner

The paper identifies a compact, stable dimeric conformation of α-synuclein that may promote dityrosine linkage and is implicated in Parkinson's disease.

bioRxiv · Oct 21, 2022Biophysics

Evidence for a compact apo-σ70 conformation in vitro and in vivo

K. Joron, J. Zamel, N. Kalisman, E. Lerner

The paper identifies a compact apo-σ70 conformation in vitro and in vivo using CL-MS, suggesting it may be transcriptionally inactive and activated upon RNAP binding.

bioRxiv · Oct 14, 2022 · PreprintBiophysics

Targeted in situ cross-linking mass spectrometry and integrative modeling reveal the architectures of Nsp1, Nsp2, and Nucleocapsid proteins from SARS-CoV-2

M. Slavin, J. Zamel, K. Zohar, S. Eliyahu, M. Braitbard, E. Brielle, L. Baraz, M. Stolovich-Rain, A. Friedman, D. G. Wolf, A. Rouvinski, M. Linial, D. Schneidman-Duhovny, N. Kalisman

This study uses targeted in situ CLMS and integrative modeling to determine the structures of SARS-CoV-2 Nsp1, Nsp2, and N proteins, revealing key interactions and functional insights.

bioRxiv · Feb 4, 2021Biochemistry

The structural heterogeneity of α-synuclein is governed by several distinct subpopulations with interconversion times slower than milliseconds

J. Chen, S. Zaer, P. Drori, J. Zamel, K. Joron, N. Kalisman, E. Lerner, N. V. Dokholyan

This study maps the conformational space of α-synuclein monomer using simulations and experimental validations, revealing stable conformations with slow interconversion times.

bioRxiv · Nov 9, 2020Biophysics

Mass spectrometry reveals the chemistry of formaldehyde cross-linking in structured proteins

T. Tayri-Wilk, M. Slavin, J. Zamel, A. Blass, S. Cohen, A. Motzik, X. Sun, D. E. Shalev, O. Ram, N. Kalisman

This study uses mass spectrometry to show that formaldehyde cross-linking in proteins involves two carbon atoms, not one, and identifies new structural insights from cross-links in human cells.

bioRxiv · Oct 28, 2019Biochemistry