
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:
Structure determination of high-energy states in a dynamic protein ensemble
J. Stiller, Renee Otten, Daniel Häußinger, et al.
Nature (2022) Vol. 603, Iss. 7901, pp. 528-535
Open Access | Times Cited: 75
J. Stiller, Renee Otten, Daniel Häußinger, et al.
Nature (2022) Vol. 603, Iss. 7901, pp. 528-535
Open Access | Times Cited: 75
Showing 1-25 of 75 citing articles:
Tuning sterol extraction kinetics yields a renal-sparing polyene antifungal
Arun Maji, Corinne P. Soutar, Jiabao Zhang, et al.
Nature (2023) Vol. 623, Iss. 7989, pp. 1079-1085
Open Access | Times Cited: 47
Arun Maji, Corinne P. Soutar, Jiabao Zhang, et al.
Nature (2023) Vol. 623, Iss. 7989, pp. 1079-1085
Open Access | Times Cited: 47
The lens epithelium as a major determinant in the development, maintenance, and regeneration of the crystalline lens
Zhenzhen Liu, Shan Huang, Yingfeng Zheng, et al.
Progress in Retinal and Eye Research (2022) Vol. 92, pp. 101112-101112
Closed Access | Times Cited: 54
Zhenzhen Liu, Shan Huang, Yingfeng Zheng, et al.
Progress in Retinal and Eye Research (2022) Vol. 92, pp. 101112-101112
Closed Access | Times Cited: 54
Design of stimulus-responsive two-state hinge proteins
Florian Praetorius, Philip J. Y. Leung, Maxx H. Tessmer, et al.
Science (2023) Vol. 381, Iss. 6659, pp. 754-760
Open Access | Times Cited: 39
Florian Praetorius, Philip J. Y. Leung, Maxx H. Tessmer, et al.
Science (2023) Vol. 381, Iss. 6659, pp. 754-760
Open Access | Times Cited: 39
Protein Dynamics and Enzymatic Catalysis
Steven D. Schwartz
The Journal of Physical Chemistry B (2023) Vol. 127, Iss. 12, pp. 2649-2660
Open Access | Times Cited: 36
Steven D. Schwartz
The Journal of Physical Chemistry B (2023) Vol. 127, Iss. 12, pp. 2649-2660
Open Access | Times Cited: 36
Protein dynamics: The future is bright and complicated!
Kwangho Nam, Magnus Wolf‐Watz
Structural Dynamics (2023) Vol. 10, Iss. 1, pp. 014301-014301
Open Access | Times Cited: 30
Kwangho Nam, Magnus Wolf‐Watz
Structural Dynamics (2023) Vol. 10, Iss. 1, pp. 014301-014301
Open Access | Times Cited: 30
Rapidly determining the 3D structure of proteins by surface-enhanced Raman spectroscopy
Hao Ma, Sen Yan, Xinyu Lu, et al.
Science Advances (2023) Vol. 9, Iss. 47
Open Access | Times Cited: 29
Hao Ma, Sen Yan, Xinyu Lu, et al.
Science Advances (2023) Vol. 9, Iss. 47
Open Access | Times Cited: 29
What can molecular assembly learn from catalysed assembly in living organisms?
Zhi‐Chao Lei, Xinchang Wang, Liulin Yang, et al.
Chemical Society Reviews (2024) Vol. 53, Iss. 4, pp. 1892-1914
Closed Access | Times Cited: 9
Zhi‐Chao Lei, Xinchang Wang, Liulin Yang, et al.
Chemical Society Reviews (2024) Vol. 53, Iss. 4, pp. 1892-1914
Closed Access | Times Cited: 9
Contributions of Hyperactive Mutations in Mpro from SARS-CoV-2 to Drug Resistance
Julia M. Flynn, Sarah N. Zvornicanin, Tenzin Tsepal, et al.
ACS Infectious Diseases (2024) Vol. 10, Iss. 4, pp. 1174-1184
Closed Access | Times Cited: 9
Julia M. Flynn, Sarah N. Zvornicanin, Tenzin Tsepal, et al.
ACS Infectious Diseases (2024) Vol. 10, Iss. 4, pp. 1174-1184
Closed Access | Times Cited: 9
Identifying protein conformational states in the Protein Data Bank: Toward unlocking the potential of integrative dynamics studies
Joseph I. J. Ellaway, Stephen Anyango, Sreenath Nair, et al.
Structural Dynamics (2024) Vol. 11, Iss. 3
Open Access | Times Cited: 9
Joseph I. J. Ellaway, Stephen Anyango, Sreenath Nair, et al.
Structural Dynamics (2024) Vol. 11, Iss. 3
Open Access | Times Cited: 9
Emerging Time-Resolved X-Ray Diffraction Approaches for Protein Dynamics
Doeke R. Hekstra
Annual Review of Biophysics (2023) Vol. 52, Iss. 1, pp. 255-274
Open Access | Times Cited: 21
Doeke R. Hekstra
Annual Review of Biophysics (2023) Vol. 52, Iss. 1, pp. 255-274
Open Access | Times Cited: 21
Intrinsic structural dynamics dictate enzymatic activity and inhibition
Vaibhav Kumar Shukla, Lucas Siemons, D. Flemming Hansen
Proceedings of the National Academy of Sciences (2023) Vol. 120, Iss. 41
Open Access | Times Cited: 18
Vaibhav Kumar Shukla, Lucas Siemons, D. Flemming Hansen
Proceedings of the National Academy of Sciences (2023) Vol. 120, Iss. 41
Open Access | Times Cited: 18
Dominant negative mutations in yeast Hsp90 reveal triage decision mechanism targeting client proteins for degradation
Julia M. Flynn, Margot E. Joyce, Daniel N. Bolon
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 7
Julia M. Flynn, Margot E. Joyce, Daniel N. Bolon
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 7
Switching Go̅-Martini for Investigating Protein Conformational Transitions and Associated Protein–Lipid Interactions
Song Yang, Chen Song
Journal of Chemical Theory and Computation (2024) Vol. 20, Iss. 6, pp. 2618-2629
Open Access | Times Cited: 7
Song Yang, Chen Song
Journal of Chemical Theory and Computation (2024) Vol. 20, Iss. 6, pp. 2618-2629
Open Access | Times Cited: 7
Integration of a Randomized Sequence Scanning Approach in AlphaFold2 and Local Frustration Profiling of Conformational States Enable Interpretable Atomistic Characterization of Conformational Ensembles and Detection of Hidden Allosteric States in the ABL1 Protein Kinase
Nishank Raisinghani, Mohammed Alshahrani, Grace Gupta, et al.
Journal of Chemical Theory and Computation (2024) Vol. 20, Iss. 12, pp. 5317-5336
Closed Access | Times Cited: 6
Nishank Raisinghani, Mohammed Alshahrani, Grace Gupta, et al.
Journal of Chemical Theory and Computation (2024) Vol. 20, Iss. 12, pp. 5317-5336
Closed Access | Times Cited: 6
Reduced dynamic complexity allows structure elucidation of an excited state of KRASG13D
Fa-An Chao, Albert H. Chan, Srisathiyanarayanan Dharmaiah, et al.
Communications Biology (2023) Vol. 6, Iss. 1
Open Access | Times Cited: 14
Fa-An Chao, Albert H. Chan, Srisathiyanarayanan Dharmaiah, et al.
Communications Biology (2023) Vol. 6, Iss. 1
Open Access | Times Cited: 14
Interpretable Atomistic Prediction and Functional Analysis of Conformational Ensembles and Allosteric States in Protein Kinases Using AlphaFold2 Adaptation with Randomized Sequence Scanning and Local Frustration Profiling
Nishank Raisinghani, Mohammed Alshahrani, Grace Gupta, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 5
Nishank Raisinghani, Mohammed Alshahrani, Grace Gupta, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 5
A litmus test for classifying recognition mechanisms of transiently binding proteins
Kalyan S. Chakrabarti, Simon Olsson, Supriya Pratihar, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 22
Kalyan S. Chakrabarti, Simon Olsson, Supriya Pratihar, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 22
Role of Repeated Conformational Transitions in Substrate Binding of Adenylate Kinase
Jiajun Lu, David Scheerer, Gilad Haran, et al.
The Journal of Physical Chemistry B (2022) Vol. 126, Iss. 41, pp. 8188-8201
Open Access | Times Cited: 19
Jiajun Lu, David Scheerer, Gilad Haran, et al.
The Journal of Physical Chemistry B (2022) Vol. 126, Iss. 41, pp. 8188-8201
Open Access | Times Cited: 19
New Insights into the Cooperativity and Dynamics of Dimeric Enzymes
Ke-Wei Chen, Tian‐Yu Sun, Yun‐Dong Wu
Chemical Reviews (2023) Vol. 123, Iss. 16, pp. 9940-9981
Closed Access | Times Cited: 12
Ke-Wei Chen, Tian‐Yu Sun, Yun‐Dong Wu
Chemical Reviews (2023) Vol. 123, Iss. 16, pp. 9940-9981
Closed Access | Times Cited: 12
Sensitivity-enhanced NMR 15N R1 and R1ρ relaxation experiments for the investigation of intrinsically disordered proteins at high magnetic fields
Tobias Stief, Katharina Vormann, Nils‐Alexander Lakomek
Methods (2024) Vol. 223, pp. 1-15
Open Access | Times Cited: 4
Tobias Stief, Katharina Vormann, Nils‐Alexander Lakomek
Methods (2024) Vol. 223, pp. 1-15
Open Access | Times Cited: 4
A unified view on enzyme catalysis by cryo-EM study of a DNA topoisomerase
Chiung‐Wen Chang, Shunchang Wang, Chun-Hsiung Wang, et al.
Communications Chemistry (2024) Vol. 7, Iss. 1
Open Access | Times Cited: 4
Chiung‐Wen Chang, Shunchang Wang, Chun-Hsiung Wang, et al.
Communications Chemistry (2024) Vol. 7, Iss. 1
Open Access | Times Cited: 4
Probing Biomolecular Interactions with Paramagnetic Nuclear Magnetic Resonance Spectroscopy
H. Büsch, Muhammad Yasir Ateeque, Florian Taube, et al.
ChemBioChem (2025)
Open Access
H. Büsch, Muhammad Yasir Ateeque, Florian Taube, et al.
ChemBioChem (2025)
Open Access
Wide Transition-State Ensemble as Key Component for Enzyme Catalysis
Gabriel Ernesto Jara, Francesco Pontiggia, Renee Otten, et al.
(2025)
Open Access
Gabriel Ernesto Jara, Francesco Pontiggia, Renee Otten, et al.
(2025)
Open Access
Wide transition-state ensemble as key component for enzyme catalysis
Gabriel Ernesto Jara, Francesco Pontiggia, Renee Otten, et al.
eLife (2025) Vol. 12
Open Access
Gabriel Ernesto Jara, Francesco Pontiggia, Renee Otten, et al.
eLife (2025) Vol. 12
Open Access
The Evolving Landscape of Protein Allostery: From Computational and Experimental Perspectives
E. Srinivasan, Grigor Arakelov, Nikolay V. Dokholyan
Journal of Molecular Biology (2025), pp. 169060-169060
Closed Access
E. Srinivasan, Grigor Arakelov, Nikolay V. Dokholyan
Journal of Molecular Biology (2025), pp. 169060-169060
Closed Access