Publications
90
Citations
2,035
Est. group size
~11
Recurring co-author estimate
Active years
36
Publishing since 1991
Alexandar L. Hansen's research uses nuclear magnetic resonance (NMR) spectroscopy and related biophysical methods to study proteins that lack a fixed, stable 3D shape (intrinsically disordered proteins) and flexible protein domains, examining how their structure and motion relate to their biological function. Work includes studying estrogen receptor disorder, RNA-binding proteins, and developing new NMR methods (such as CEST and HSQC-based techniques) to probe protein dynamics. This research is relevant to students interested in structural biology, biophysics, and methods development for studying flexible or disordered biomolecules.
Publication output has fluctuated over the last decade without a clear upward or downward trend, with peaks in 2018 and 2021 and a recent average of about 6 papers per year over the last five years.
Generated by claude-sonnet-5 from public bibliographic data · Jul 20, 2026
- The sequence–structure–function relationship of intrinsic ERα disorder
Nature · 2025
- BPS2025 - Residue-specific interactions of intrinsically disordered ERalpha with cofactor proteins
Biophysical Journal · 2025
- BPS2025 - Residue-specific interactions of intrinsically disordered ERalpha with cofactor proteins
Biophysical Journal · 2025
- BPS2025 - Integrating SAXS and pre to guide molecular simulations in IDP ensemble structure determination
Biophysical Journal · 2025
- Thermodynamic coupling of the tandem RRM domains of hnRNP A1 underlie its pleiotropic RNA binding functions
Science Advances · 2024
- ARCHE-NOAH: NMR supersequence with five different CEST experiments for studying protein conformational dynamics
Physical Chemistry Chemical Physics · 2023
- Phosphorylation modulates estrogen receptor disorder by altering long-range hydrophobic interactions
bioRxiv (Cold Spring Harbor Laboratory) · 2023
- Thermodynamic Coupling of the tandem RRM domains of hnRNP A1 underlie its Pleiotropic RNA Binding Functions
bioRxiv (Cold Spring Harbor Laboratory) · 2023
- NOAH-( <sup>15</sup> N/ <sup>13</sup> C)-CEST NMR supersequence for dynamics studies of biomolecules
Chemical Communications · 2022
- Increasing sensitivity and versatility in NMR supersequences with new HSQC-based modules
Journal of Magnetic Resonance · 2021
- Towards the NMR solution Structure and the Dynamics of the C-terminal Region of APOL1 and its G1, G2 Variants with a Membrane Mimetic
bioRxiv (Cold Spring Harbor Laboratory) · 2021
- Raw data and figures for "Increasing Sensitivity and Versatility in NMR Supersequences with New HSQC-based Modules"
Figshare · 2021
- Raw data and figures for "Increasing Sensitivity and Versatility in NMR Supersequences with New HSQC-based Modules"
Figshare · 2021
- Raw data and figures for "Increasing Sensitivity and Versatility in NMR Supersequences with New HSQC-based Modules"
Zenodo (CERN European Organization for Nuclear Research) · 2021
- Raw data and figures for "Increasing Sensitivity and Versatility in NMR Supersequences with New HSQC-based Modules"
Zenodo (CERN European Organization for Nuclear Research) · 2021
- Journal of the American Chemical Society×7
- Angewandte Chemie International Edition×5
- Angewandte Chemie×5
- Chemistry - A European Journal×4
- Zenodo (CERN European Organization for Nuclear Research)×4
- Eric J. Munson
Chemistry · Purdue University West Lafayette
- Philip J. Grandinetti
Chemistry · The Ohio State University
- Jay H. Baltisberger
Chemistry · The Ohio State University
- Christopher P. Jaroniec
Chemistry · The Ohio State University
- Rafael Brüschweiler
Biochemistry, Genetics and Molecular Biology · The Ohio State University
This profile was generated automatically from public scholarly data (OpenAlex). Group size and activity levels are estimates derived from co-authorship patterns.
Last updated Jul 19, 2026.
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