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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:

The Role of Protein Loops and Linkers in Conformational Dynamics and Allostery
Elena Papaleo, Giorgio Saladino, Matteo Lambrughi, et al.
Chemical Reviews (2016) Vol. 116, Iss. 11, pp. 6391-6423
Open Access | Times Cited: 376

Showing 1-25 of 376 citing articles:

Illuminating G-Protein-Coupling Selectivity of GPCRs
Asuka Inoue, Francesco Raimondi, Francois Marie Ngako Kadji, et al.
Cell (2019) Vol. 177, Iss. 7, pp. 1933-1947.e25
Open Access | Times Cited: 541
NMR Provides Unique Insight into the Functional Dynamics and Interactions of Intrinsically Disordered Proteins
Aldo R. Camacho‐Zarco, Vincent Schnapka, Serafima Guseva, et al.
Chemical Reviews (2022) Vol. 122, Iss. 10, pp. 9331-9356
Open Access | Times Cited: 95
Thermal stability enhancement: Fundamental concepts of protein engineering strategies to manipulate the flexible structure
Mahdie Rahban, Samaneh Zolghadri, Najmeh Salehi, et al.
International Journal of Biological Macromolecules (2022) Vol. 214, pp. 642-654
Closed Access | Times Cited: 81
Loop dynamics and the evolution of enzyme activity
Marina Corbella, Gaspar Pinto, Shina Caroline Lynn Kamerlin
Nature Reviews Chemistry (2023) Vol. 7, Iss. 8, pp. 536-547
Closed Access | Times Cited: 79
Role of distal sites in enzyme engineering
Jie Gu, Yan Xu, Yao Nie
Biotechnology Advances (2023) Vol. 63, pp. 108094-108094
Closed Access | Times Cited: 52
GōMartini 3: From large conformational changes in proteins to environmental bias corrections
Paulo C. T. Souza, Luís Borges-Araújo, Chris Brasnett, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 21
Effective concentrations enforced by intrinsically disordered linkers are governed by polymer physics
Charlotte S. Sørensen, Magnus Kjærgaard
Proceedings of the National Academy of Sciences (2019) Vol. 116, Iss. 46, pp. 23124-23131
Open Access | Times Cited: 144
The entropic force generated by intrinsically disordered segments tunes protein function
Nicholas D. Keul, Krishnadev Oruganty, Elizabeth T. Schaper Bergman, et al.
Nature (2018) Vol. 563, Iss. 7732, pp. 584-588
Open Access | Times Cited: 138
Enzyme Fusions in Biocatalysis: Coupling Reactions by Pairing Enzymes
Friso S. Aalbers, Marco W. Fraaije
ChemBioChem (2018) Vol. 20, Iss. 1, pp. 20-28
Open Access | Times Cited: 132
The application of ion-mobility mass spectrometry for structure/function investigation of protein complexes
Gili Ben‐Nissan, Michal Sharon
Current Opinion in Chemical Biology (2017) Vol. 42, pp. 25-33
Open Access | Times Cited: 122
Expanding the Paradigm: Intrinsically Disordered Proteins and Allosteric Regulation
Rebecca B. Berlow, H. Jane Dyson, Peter E. Wright
Journal of Molecular Biology (2018) Vol. 430, Iss. 16, pp. 2309-2320
Open Access | Times Cited: 114
Computational Drug Design Methods—Current and Future Perspectives
Fernando D. Prieto‐Martínez, Edgar López‐López, K. Eurídice Juárez‐Mercado, et al.
Elsevier eBooks (2019), pp. 19-44
Closed Access | Times Cited: 114
Loop Motion in Triosephosphate Isomerase Is Not a Simple Open and Shut Case
Qinghua Liao, Yashraj Kulkarni, Ushnish Sengupta, et al.
Journal of the American Chemical Society (2018) Vol. 140, Iss. 46, pp. 15889-15903
Open Access | Times Cited: 106
Dynamics of proteins in solution
Marco Grimaldo, Felix Roosen‐Runge, Fajun Zhang, et al.
Quarterly Reviews of Biophysics (2019) Vol. 52
Open Access | Times Cited: 106
Symmetry, Rigidity, and Allosteric Signaling: From Monomeric Proteins to Molecular Machines
D. Thirumalai, Changbong Hyeon, Pavel I. Zhuravlev, et al.
Chemical Reviews (2019) Vol. 119, Iss. 12, pp. 6788-6821
Open Access | Times Cited: 102
An optimal distance cutoff for contact-based Protein Structure Networks using side-chain centers of mass
Juan Salamanca Viloria, Maria Francesca Allega, Matteo Lambrughi, et al.
Scientific Reports (2017) Vol. 7, Iss. 1
Open Access | Times Cited: 93
Solution conformations of Zika NS2B-NS3pro and its inhibition by natural products from edible plants
Amrita Roy, Liangzhong Lim, Shagun Srivastava, et al.
PLoS ONE (2017) Vol. 12, Iss. 7, pp. e0180632-e0180632
Open Access | Times Cited: 89
On the perturbation nature of allostery: sites, mutations, and signal modulation
Enrico Guarnera, Igor N. Berezovsky
Current Opinion in Structural Biology (2018) Vol. 56, pp. 18-27
Closed Access | Times Cited: 88
Unlocked potential of dynamic elements in protein structures: channels and loops
Nico Kreß, Julia M. Halder, Lea R. Rapp, et al.
Current Opinion in Chemical Biology (2018) Vol. 47, pp. 109-116
Closed Access | Times Cited: 86
Conformational Entropy as a Means to Control the Behavior of Poly(diketoenamine) Vitrimers In and Out of Equilibrium
Changfei He, Peter R. Christensen, Trevor J. Seguin, et al.
Angewandte Chemie International Edition (2019) Vol. 59, Iss. 2, pp. 735-739
Open Access | Times Cited: 82
Loop Dynamics and Enzyme Catalysis in Protein Tyrosine Phosphatases
Rory Crean, Michal Biler, Marc W. van der Kamp, et al.
Journal of the American Chemical Society (2021) Vol. 143, Iss. 10, pp. 3830-3845
Open Access | Times Cited: 67
Benchmarking the Accuracy of AlphaFold 2 in Loop Structure Prediction
Amy O. Stevens, Yi He
Biomolecules (2022) Vol. 12, Iss. 7, pp. 985-985
Open Access | Times Cited: 60
An Adaptable Water-Soluble Molecular Boat for Selective Separation of Phenanthrene from Isomeric Anthracene
Arppitha Baby Sainaba, Mangili Venkateswarulu, Pallab Bhandari, et al.
Journal of the American Chemical Society (2022) Vol. 144, Iss. 16, pp. 7504-7513
Closed Access | Times Cited: 56
Flexibility Regulation of Loops Surrounding the Tunnel Entrance in Cytochrome P450 Enhanced Substrate Access Substantially
Zhongyu Li, Shuaiqi Meng, Kaili Nie, et al.
ACS Catalysis (2022) Vol. 12, Iss. 20, pp. 12800-12808
Closed Access | Times Cited: 52
Overcoming universal restrictions on metal selectivity by protein design
Tae Su Choi, F. Akif Tezcan
Nature (2022) Vol. 603, Iss. 7901, pp. 522-527
Open Access | Times Cited: 49
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