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OpenAlex Citation Counts

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OpenAlex is a bibliographic catalogue of scientific papers, authors and institutions accessible in open access mode, named after the Library of Alexandria. It's citation coverage is excellent and I hope you will find utility in this listing of citing articles!

If you click the article title, you'll navigate to the article, as listed in CrossRef. If you click the Open Access links, you'll navigate to the "best Open Access location". Clicking the citation count will open this listing for that article. Lastly at the bottom of the page, you'll find basic pagination options.

Requested Article:

Refining conformational ensembles of flexible proteins against small-angle x-ray scattering data
Francesco Pesce, Kresten Lindorff‐Larsen
Biophysical Journal (2021) Vol. 120, Iss. 22, pp. 5124-5135
Open Access | Times Cited: 30

Showing 1-25 of 30 citing articles:

Improving Martini 3 for Disordered and Multidomain Proteins
F. Emil Thomasen, Francesco Pesce, Mette Ahrensback Roesgaard, et al.
Journal of Chemical Theory and Computation (2022) Vol. 18, Iss. 4, pp. 2033-2041
Open Access | Times Cited: 126
Rescaling protein-protein interactions improves Martini 3 for flexible proteins in solution
F. Emil Thomasen, Tórur Skaalum, Ashutosh Kumar, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 19
Conformational ensembles of intrinsically disordered proteins and flexible multidomain proteins
F. Emil Thomasen, Kresten Lindorff‐Larsen
Biochemical Society Transactions (2022) Vol. 50, Iss. 1, pp. 541-554
Open Access | Times Cited: 70
Architecture of the MKK6-p38α complex defines the basis of MAPK specificity and activation
Pauline Juyoux, Ioannis Galdadas, Dorothea Gobbo, et al.
Science (2023) Vol. 381, Iss. 6663, pp. 1217-1225
Open Access | Times Cited: 24
Design of intrinsically disordered protein variants with diverse structural properties
Francesco Pesce, Anne Bremer, Giulio Tesei, et al.
Science Advances (2024) Vol. 10, Iss. 35
Open Access | Times Cited: 16
The ribosome lowers the entropic penalty of protein folding
Julian O. Streit, Ivana V. Bukvin, Sammy H. S. Chan, et al.
Nature (2024) Vol. 633, Iss. 8028, pp. 232-239
Open Access | Times Cited: 10
Assessment of models for calculating the hydrodynamic radius of intrinsically disordered proteins
Francesco Pesce, Estella A. Newcombe, Pernille Seiffert, et al.
Biophysical Journal (2022) Vol. 122, Iss. 2, pp. 310-321
Open Access | Times Cited: 30
Transient interdomain interactions in free USP14 shape its conformational ensemble
Johannes Salomonsson, Björn Wallner, Linda Sjöstrand, et al.
Protein Science (2024) Vol. 33, Iss. 5
Open Access | Times Cited: 6
Combining experiments and simulations to examine the temperature-dependent behaviour of a disordered protein
Francesco Pesce, Kresten Lindorff‐Larsen
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 10
GōMartini 3: From large conformational changes in proteins to environmental bias corrections
Paulo C. T. Souza, Luís Borges-Araújo, Christopher Brasnett, et al.
Nature Communications (2025) Vol. 16, Iss. 1
Open Access
Hierarchy in regulator interactions with distant transcriptional activation domains empowers rheostatic regulation
Amanda D. Due, Norman E. Davey, F. Emil Thomasen, et al.
Protein Science (2025) Vol. 34, Iss. 6
Open Access
Reweighting methods for elucidation of conformation ensembles of proteins
Raquel Gama Lima Costa, David Fushman
Current Opinion in Structural Biology (2022) Vol. 77, pp. 102470-102470
Open Access | Times Cited: 16
The effect of linker conformation on performance and stability of a two-domain lytic polysaccharide monooxygenase
Zarah Forsberg, Anton A. Stepnov, Giulio Tesei, et al.
Journal of Biological Chemistry (2023) Vol. 299, Iss. 11, pp. 105262-105262
Open Access | Times Cited: 9
Simultaneous refinement of molecular dynamics ensembles and forward models using experimental data
Thorben Fröhlking, Mattia Bernetti, Giovanni Bussi
The Journal of Chemical Physics (2023) Vol. 158, Iss. 21
Open Access | Times Cited: 7
Integrative Conformational Ensembles of Sic1 Using Different Initial Pools and Optimization Methods
Gregory-Neal W. Gomes, Ashley Namini, Claudiu C. Gradinaru
Frontiers in Molecular Biosciences (2022) Vol. 9
Open Access | Times Cited: 11
Conformational and oligomeric states of SPOP from small-angle X-ray scattering and molecular dynamics simulations
F. Emil Thomasen, M.J. Cuneo, Tanja Mittag, et al.
eLife (2023) Vol. 12
Open Access | Times Cited: 6
Rescaling protein-protein interactions improves Martini 3 for flexible proteins in solution
F. Emil Thomasen, Tórur Skaalum, Ashutosh Kumar, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 6
Data-driven models for predicting intrinsically disordered protein polymer physics directly from composition or sequence
Tzu‐Hsuan Chao, Shiv Rekhi, Jeetain Mittal, et al.
Molecular Systems Design & Engineering (2023) Vol. 8, Iss. 9, pp. 1146-1155
Closed Access | Times Cited: 6
Combining Experiments and Simulations to Examine the Temperature-Dependent Behavior of a Disordered Protein
Francesco Pesce, Kresten Lindorff‐Larsen
The Journal of Physical Chemistry B (2023) Vol. 127, Iss. 28, pp. 6277-6286
Closed Access | Times Cited: 6
Design of intrinsically disordered protein variants with diverse structural properties
Francesco Pesce, Anne Bremer, Giulio Tesei, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 5
Bayesian methods in integrative structure modeling
Michael Habeck
Biological Chemistry (2023) Vol. 404, Iss. 8-9, pp. 741-754
Open Access | Times Cited: 4
Assessment of models for calculating the hydrodynamic radius of intrinsically disordered proteins
Francesco Pesce, Estella A. Newcombe, Pernille Seiffert, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access | Times Cited: 7
Towards accurate, force field independent conformational ensembles of intrinsically disordered proteins
Kaushik Borthakur, Thomas R. Sisk, Francesco Paolo Panei, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 1
Recent Developments in Data-Assisted Modeling of Flexible Proteins
Cezary Czaplewski, Zhou Gong, Emilia A. Lubecka, et al.
Frontiers in Molecular Biosciences (2021) Vol. 8
Open Access | Times Cited: 9
Small-angle x-ray and neutron scattering of MexR and its complex with DNA supports a conformational selection binding model
Francesca Caporaletti, Zuzanna Pietras, Vivian Morad, et al.
Biophysical Journal (2022) Vol. 122, Iss. 2, pp. 408-418
Open Access | Times Cited: 4
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