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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:

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

Showing 16 citing articles:

Conformational heterogeneity and probability distributions from single-particle cryo-electron microscopy
Wai Shing Tang, Ellen D. Zhong, Sonya M. Hanson, et al.
Current Opinion in Structural Biology (2023) Vol. 81, pp. 102626-102626
Closed Access | Times Cited: 33
Ensemble Reweighting Using Cryo-EM Particle Images
Wai Shing Tang, David Silva-Sánchez, Julian Giraldo-Barreto, et al.
The Journal of Physical Chemistry B (2023) Vol. 127, Iss. 24, pp. 5410-5421
Closed Access | Times Cited: 25
Representing structures of the multiple conformational states of proteins
Theresa A. Ramelot, Roberto Tejero, G.T. Montelione
Current Opinion in Structural Biology (2023) Vol. 83, pp. 102703-102703
Open Access | Times Cited: 18
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
Protein ensemble modeling and analysis with MMMx
Gunnar Jeschke
Protein Science (2024) Vol. 33, Iss. 3
Open Access | Times Cited: 2
An ensemble of cadherin-catenin-vinculin complex employs vinculin as the major F-actin binding mode
Bright Shi, Tsutomu Matsui, Shuo Qian, et al.
Biophysical Journal (2023) Vol. 122, Iss. 12, pp. 2456-2474
Closed Access | Times Cited: 5
In silico engineering and simulation of RNA interferences nanoplatforms for osteoporosis treating and bone healing promoting
Aylar Imanpour, Hanieh Kolahi Azar, Dorna Makarem, et al.
Scientific Reports (2023) Vol. 13, Iss. 1
Open Access | Times Cited: 5
Computational Methods to Investigate Intrinsically Disordered Proteins and their Complexes.
Zi Hao Liu, Maria Tsanai, Oufan Zhang, et al.
arXiv (Cornell University) (2024)
Open Access | Times Cited: 1
Are Protein Conformational Ensembles in Agreement with Experimental Data? A Geometrical Interpretation of the Problem
Letizia Fiorucci, Marco Schiavina, Isabella C. Felli, et al.
Journal of Chemical Information and Modeling (2024) Vol. 64, Iss. 14, pp. 5392-5401
Closed Access
High‐Resolution Structures of RNA
Lukas Braun, Zahra Alirezaeizanjani, Roberta Tesch, et al.
Methods and principles in medicinal chemistry (2024), pp. 29-48
Closed Access
Effects of All-Atom and Coarse-Grained Molecular Mechanics Force Fields on Amyloid Peptide Assembly: The Case of a Tau K18 Monomer
Xibing He, Viet Hoang Man, Jie Gao, et al.
Journal of Chemical Information and Modeling (2024)
Closed Access
Representing Structures of the Multiple Conformational States of Proteins
Theresa A. Ramelot, Roberto Tejero, G.T. Montelione
(2023)
Open Access | Times Cited: 1
Representing structures of the multiple conformational states of proteins
Theresa A. Ramelot, Roberto Tejero, G.T. Montelione
(2023)
Open Access | Times Cited: 1
Conformational Dependence of Chemical Shifts in the Proline Rich Region of TAU Protein
Johannes Stöckelmaier, Chris Oostenbrink
Physical Chemistry Chemical Physics (2024) Vol. 26, Iss. 36, pp. 23856-23870
Open Access
Supramolecular Protein Assemblies: Building Blocks, Organism- or Cell-Specific Varieties, and Significance
Victoria I. Bunik
Biomolecules (2024) Vol. 14, Iss. 11, pp. 1342-1342
Open Access
How protein fold: Insights from nuclear magnetic resonance spectroscopy
Anastasia Zhuravelva
Elsevier eBooks (2023), pp. 619-635
Closed Access
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