
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:
Mechanism of the allosteric activation of the ClpP protease machinery by substrates and active-site inhibitors
Jan Félix, Katharina Weinhäupl, Christophe Chipot, et al.
Science Advances (2019) Vol. 5, Iss. 9
Open Access | Times Cited: 50
Jan Félix, Katharina Weinhäupl, Christophe Chipot, et al.
Science Advances (2019) Vol. 5, Iss. 9
Open Access | Times Cited: 50
Showing 1-25 of 50 citing articles:
Solid-state NMR spectroscopy
Bernd Reif, Sharon E. Ashbrook, Lyndon Emsley, et al.
Nature Reviews Methods Primers (2021) Vol. 1, Iss. 1
Open Access | Times Cited: 359
Bernd Reif, Sharon E. Ashbrook, Lyndon Emsley, et al.
Nature Reviews Methods Primers (2021) Vol. 1, Iss. 1
Open Access | Times Cited: 359
1H-Detected Biomolecular NMR under Fast Magic-Angle Spinning
Tanguy Le Marchand, Tobias Schubeis, Marta Bonaccorsi, et al.
Chemical Reviews (2022) Vol. 122, Iss. 10, pp. 9943-10018
Open Access | Times Cited: 104
Tanguy Le Marchand, Tobias Schubeis, Marta Bonaccorsi, et al.
Chemical Reviews (2022) Vol. 122, Iss. 10, pp. 9943-10018
Open Access | Times Cited: 104
Isothermal titration calorimetry
Margarida Bastos, Olga Abián, C. Mark Johnson, et al.
Nature Reviews Methods Primers (2023) Vol. 3, Iss. 1
Closed Access | Times Cited: 93
Margarida Bastos, Olga Abián, C. Mark Johnson, et al.
Nature Reviews Methods Primers (2023) Vol. 3, Iss. 1
Closed Access | Times Cited: 93
Solid-State NMR: Methods for Biological Solids
Sahil Ahlawat, Kaustubh R. Mote, Nils‐Alexander Lakomek, et al.
Chemical Reviews (2022) Vol. 122, Iss. 10, pp. 9643-9737
Closed Access | Times Cited: 73
Sahil Ahlawat, Kaustubh R. Mote, Nils‐Alexander Lakomek, et al.
Chemical Reviews (2022) Vol. 122, Iss. 10, pp. 9643-9737
Closed Access | Times Cited: 73
Allosteric drugs and mutations: chances, challenges, and necessity
Enrico Guarnera, Igor N. Berezovsky
Current Opinion in Structural Biology (2020) Vol. 62, pp. 149-157
Closed Access | Times Cited: 91
Enrico Guarnera, Igor N. Berezovsky
Current Opinion in Structural Biology (2020) Vol. 62, pp. 149-157
Closed Access | Times Cited: 91
β-Lactams against the Fortress of the Gram-Positive Staphylococcus aureus Bacterium
Jed F. Fisher, Shahriar Mobashery
Chemical Reviews (2020) Vol. 121, Iss. 6, pp. 3412-3463
Open Access | Times Cited: 82
Jed F. Fisher, Shahriar Mobashery
Chemical Reviews (2020) Vol. 121, Iss. 6, pp. 3412-3463
Open Access | Times Cited: 82
Recent structural insights into the mechanism of ClpP protease regulation by AAA+ chaperones and small molecules
Mark Mabanglo, Walid A. Houry
Journal of Biological Chemistry (2022) Vol. 298, Iss. 5, pp. 101781-101781
Open Access | Times Cited: 43
Mark Mabanglo, Walid A. Houry
Journal of Biological Chemistry (2022) Vol. 298, Iss. 5, pp. 101781-101781
Open Access | Times Cited: 43
Imaging active site chemistry and protonation states: NMR crystallography of the tryptophan synthase α-aminoacrylate intermediate
Jacob B. Holmes, Viktoriia Liu, Bethany G. Caulkins, et al.
Proceedings of the National Academy of Sciences (2022) Vol. 119, Iss. 2
Open Access | Times Cited: 39
Jacob B. Holmes, Viktoriia Liu, Bethany G. Caulkins, et al.
Proceedings of the National Academy of Sciences (2022) Vol. 119, Iss. 2
Open Access | Times Cited: 39
On the Binding Mode and Molecular Mechanism of Enzymatic Polyethylene Terephthalate Degradation
Patricia Falkenstein, Ziyue Zhao, Ania Di Pede-Mattatelli, et al.
ACS Catalysis (2023) Vol. 13, Iss. 10, pp. 6919-6933
Open Access | Times Cited: 25
Patricia Falkenstein, Ziyue Zhao, Ania Di Pede-Mattatelli, et al.
ACS Catalysis (2023) Vol. 13, Iss. 10, pp. 6919-6933
Open Access | Times Cited: 25
Activation Mechanism and Structural Assembly of the Mycobacterium tuberculosis ClpP1P2 Protease and Its Associated ATPases.
Katharina Weinhäupl, Tatos Akopian, Olga Krandor, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2025)
Closed Access | Times Cited: 1
Katharina Weinhäupl, Tatos Akopian, Olga Krandor, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2025)
Closed Access | Times Cited: 1
Structural Insights into Bortezomib-Induced Activation of the Caseinolytic Chaperone-Protease System in Mycobacterium tuberculosis
Biao Zhou, Yamin Gao, Heyu Zhao, et al.
Nature Communications (2025) Vol. 16, Iss. 1
Open Access | Times Cited: 1
Biao Zhou, Yamin Gao, Heyu Zhao, et al.
Nature Communications (2025) Vol. 16, Iss. 1
Open Access | Times Cited: 1
An allosteric switch regulates Mycobacterium tuberculosis ClpP1P2 protease function as established by cryo-EM and methyl-TROSY NMR
Siavash Vahidi, Zev A. Ripstein, Jordan B. Juravsky, et al.
Proceedings of the National Academy of Sciences (2020) Vol. 117, Iss. 11, pp. 5895-5906
Open Access | Times Cited: 56
Siavash Vahidi, Zev A. Ripstein, Jordan B. Juravsky, et al.
Proceedings of the National Academy of Sciences (2020) Vol. 117, Iss. 11, pp. 5895-5906
Open Access | Times Cited: 56
From Angstroms to Nanometers: Measuring Interatomic Distances by Solid-State NMR
A. Shcherbakov, João Medeiros‐Silva, Nhi Tran, et al.
Chemical Reviews (2021) Vol. 122, Iss. 10, pp. 9848-9879
Open Access | Times Cited: 49
A. Shcherbakov, João Medeiros‐Silva, Nhi Tran, et al.
Chemical Reviews (2021) Vol. 122, Iss. 10, pp. 9848-9879
Open Access | Times Cited: 49
Chemical tools to expand the ligandable proteome: diversity-oriented synthesis-based photoreactive stereoprobes
Daisuke Ogasawara, David B. Konrad, Zher Yin Tan, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 7
Daisuke Ogasawara, David B. Konrad, Zher Yin Tan, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 7
Deuteration for High-Resolution Detection of Protons in Protein Magic Angle Spinning (MAS) Solid-State NMR
Bernd Reif
Chemical Reviews (2021) Vol. 122, Iss. 10, pp. 10019-10035
Closed Access | Times Cited: 36
Bernd Reif
Chemical Reviews (2021) Vol. 122, Iss. 10, pp. 10019-10035
Closed Access | Times Cited: 36
Chemical tools to expand the ligandable proteome: Diversity-oriented synthesis-based photoreactive stereoprobes
Daisuke Ogasawara, David B. Konrad, Zher Yin Tan, et al.
Cell chemical biology (2024)
Open Access | Times Cited: 5
Daisuke Ogasawara, David B. Konrad, Zher Yin Tan, et al.
Cell chemical biology (2024)
Open Access | Times Cited: 5
Protein structural dynamics by Magic-Angle Spinning NMR
Marta Bonaccorsi, Tanguy Le Marchand, Guido Pintacuda
Current Opinion in Structural Biology (2021) Vol. 70, pp. 34-43
Open Access | Times Cited: 31
Marta Bonaccorsi, Tanguy Le Marchand, Guido Pintacuda
Current Opinion in Structural Biology (2021) Vol. 70, pp. 34-43
Open Access | Times Cited: 31
Applications of isothermal titration calorimetry in pure and applied research from 2016 to 2020
Robert J. Falconer, Boelo Schuur, Anthony Mittermaier
Journal of Molecular Recognition (2021) Vol. 34, Iss. 10
Open Access | Times Cited: 28
Robert J. Falconer, Boelo Schuur, Anthony Mittermaier
Journal of Molecular Recognition (2021) Vol. 34, Iss. 10
Open Access | Times Cited: 28
Functional control of a 0.5 MDa TET aminopeptidase by a flexible loop revealed by MAS NMR
Diego F. Gauto, Pavel Macek, Duccio Malinverni, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 22
Diego F. Gauto, Pavel Macek, Duccio Malinverni, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 22
Deciphering the competitive binding interaction of β-lactoglobulin with benzaldehyde and vanillic acid via high-spatial-resolution multi-spectroscopic
Rong Zhang, Wei Jia
Food Hydrocolloids (2023) Vol. 141, pp. 108724-108724
Closed Access | Times Cited: 12
Rong Zhang, Wei Jia
Food Hydrocolloids (2023) Vol. 141, pp. 108724-108724
Closed Access | Times Cited: 12
Mechanism of allosteric activation in human mitochondrial ClpP protease
Monica M. Goncalves, Adwaith B. Uday, Taylor J. B. Forrester, et al.
Proceedings of the National Academy of Sciences (2025) Vol. 122, Iss. 16
Open Access
Monica M. Goncalves, Adwaith B. Uday, Taylor J. B. Forrester, et al.
Proceedings of the National Academy of Sciences (2025) Vol. 122, Iss. 16
Open Access
Molecular insights into the dynamic modulation of bacterial ClpP function and oligomerization by peptidomimetic boronate compounds
B. Alves Franca, Sven Falke, Holger Rohde, et al.
Scientific Reports (2024) Vol. 14, Iss. 1
Open Access | Times Cited: 2
B. Alves Franca, Sven Falke, Holger Rohde, et al.
Scientific Reports (2024) Vol. 14, Iss. 1
Open Access | Times Cited: 2
Structural basis to repurpose boron-based proteasome inhibitors Bortezomib and Ixazomib as β-lactamase inhibitors
Markus Perbandt, N. Werner, Andreas Prester, et al.
Scientific Reports (2022) Vol. 12, Iss. 1
Open Access | Times Cited: 10
Markus Perbandt, N. Werner, Andreas Prester, et al.
Scientific Reports (2022) Vol. 12, Iss. 1
Open Access | Times Cited: 10
Discovery and Mechanistic Study of Novel Mycobacterium tuberculosis ClpP1P2 Inhibitors
Yang Yang, Ninglin Zhao, Xin Xu, et al.
Journal of Medicinal Chemistry (2023) Vol. 66, Iss. 24, pp. 16597-16614
Closed Access | Times Cited: 6
Yang Yang, Ninglin Zhao, Xin Xu, et al.
Journal of Medicinal Chemistry (2023) Vol. 66, Iss. 24, pp. 16597-16614
Closed Access | Times Cited: 6
Biological Calorimetry: Old Friend, New Insights
Olga Abián, Sonia Vega, Adrián Velázquez‐Campoy
Biophysica (2023) Vol. 3, Iss. 1, pp. 21-34
Open Access | Times Cited: 5
Olga Abián, Sonia Vega, Adrián Velázquez‐Campoy
Biophysica (2023) Vol. 3, Iss. 1, pp. 21-34
Open Access | Times Cited: 5