
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:
Click Chemistry in Proteomic Investigations
Christopher G. Parker, Matthew R. Pratt
Cell (2020) Vol. 180, Iss. 4, pp. 605-632
Open Access | Times Cited: 294
Christopher G. Parker, Matthew R. Pratt
Cell (2020) Vol. 180, Iss. 4, pp. 605-632
Open Access | Times Cited: 294
Showing 1-25 of 294 citing articles:
Bioorthogonal chemistry
Samuel L. Scinto, Didier A. Bilodeau, Robert Hincapie, et al.
Nature Reviews Methods Primers (2021) Vol. 1, Iss. 1
Open Access | Times Cited: 344
Samuel L. Scinto, Didier A. Bilodeau, Robert Hincapie, et al.
Nature Reviews Methods Primers (2021) Vol. 1, Iss. 1
Open Access | Times Cited: 344
The emerging role of mass spectrometry-based proteomics in drug discovery
Felix Meissner, Jennifer Geddes‐McAlister, Matthias Mann, et al.
Nature Reviews Drug Discovery (2022) Vol. 21, Iss. 9, pp. 637-654
Closed Access | Times Cited: 226
Felix Meissner, Jennifer Geddes‐McAlister, Matthias Mann, et al.
Nature Reviews Drug Discovery (2022) Vol. 21, Iss. 9, pp. 637-654
Closed Access | Times Cited: 226
Sulfonyl fluorides as targets and substrates in the development of new synthetic methods
Terry Shing‐Bong Lou, Michael C. Willis
Nature Reviews Chemistry (2022) Vol. 6, Iss. 2, pp. 146-162
Closed Access | Times Cited: 185
Terry Shing‐Bong Lou, Michael C. Willis
Nature Reviews Chemistry (2022) Vol. 6, Iss. 2, pp. 146-162
Closed Access | Times Cited: 185
A Pragmatic Guide to Enrichment Strategies for Mass Spectrometry–Based Glycoproteomics
Nicholas M. Riley, Carolyn R. Bertozzi, Sharon J. Pitteri
Molecular & Cellular Proteomics (2020) Vol. 20, pp. 100029-100029
Open Access | Times Cited: 178
Nicholas M. Riley, Carolyn R. Bertozzi, Sharon J. Pitteri
Molecular & Cellular Proteomics (2020) Vol. 20, pp. 100029-100029
Open Access | Times Cited: 178
Glycoproteomics
Ieva Bagdonaite, Stacy A. Malaker, Daniel A. Polasky, et al.
Nature Reviews Methods Primers (2022) Vol. 2, Iss. 1
Open Access | Times Cited: 153
Ieva Bagdonaite, Stacy A. Malaker, Daniel A. Polasky, et al.
Nature Reviews Methods Primers (2022) Vol. 2, Iss. 1
Open Access | Times Cited: 153
High-Throughput Screening Platforms in the Discovery of Novel Drugs for Neurodegenerative Diseases
Hasan Aldewachi, Radhwan Nidal Al-Zidan, Matthew T. Conner, et al.
Bioengineering (2021) Vol. 8, Iss. 2, pp. 30-30
Open Access | Times Cited: 150
Hasan Aldewachi, Radhwan Nidal Al-Zidan, Matthew T. Conner, et al.
Bioengineering (2021) Vol. 8, Iss. 2, pp. 30-30
Open Access | Times Cited: 150
Metal-free bioorthogonal click chemistry in cancer theranostics
Dan Wu, Kuikun Yang, Zhankui Zhang, et al.
Chemical Society Reviews (2022) Vol. 51, Iss. 4, pp. 1336-1376
Closed Access | Times Cited: 114
Dan Wu, Kuikun Yang, Zhankui Zhang, et al.
Chemical Society Reviews (2022) Vol. 51, Iss. 4, pp. 1336-1376
Closed Access | Times Cited: 114
The lipid peroxidation product 4-hydroxynonenal inhibits NLRP3 inflammasome activation and macrophage pyroptosis
Chia George Hsu, Camila Lage Chávez, Chongyang Zhang, et al.
Cell Death and Differentiation (2022) Vol. 29, Iss. 9, pp. 1790-1803
Open Access | Times Cited: 91
Chia George Hsu, Camila Lage Chávez, Chongyang Zhang, et al.
Cell Death and Differentiation (2022) Vol. 29, Iss. 9, pp. 1790-1803
Open Access | Times Cited: 91
Shining New Light on Biological Systems: Luminescent Transition Metal Complexes for Bioimaging and Biosensing Applications
Lawrence Cho‐Cheung Lee, Kenneth Kam‐Wing Lo
Chemical Reviews (2024) Vol. 124, Iss. 15, pp. 8825-9014
Open Access | Times Cited: 35
Lawrence Cho‐Cheung Lee, Kenneth Kam‐Wing Lo
Chemical Reviews (2024) Vol. 124, Iss. 15, pp. 8825-9014
Open Access | Times Cited: 35
Enhanced mapping of small-molecule binding sites in cells
Jacob M. Wozniak, Weichao Li, Paolo Governa, et al.
Nature Chemical Biology (2024) Vol. 20, Iss. 7, pp. 823-834
Open Access | Times Cited: 16
Jacob M. Wozniak, Weichao Li, Paolo Governa, et al.
Nature Chemical Biology (2024) Vol. 20, Iss. 7, pp. 823-834
Open Access | Times Cited: 16
Arylfluorosulfate‐Based Electrophiles for Covalent Protein Labeling: A New Addition to the Arsenal
Pablo Martín‐Gago, Christian A. Olsen
Angewandte Chemie International Edition (2018) Vol. 58, Iss. 4, pp. 957-966
Open Access | Times Cited: 141
Pablo Martín‐Gago, Christian A. Olsen
Angewandte Chemie International Edition (2018) Vol. 58, Iss. 4, pp. 957-966
Open Access | Times Cited: 141
A machine learning-based chemoproteomic approach to identify drug targets and binding sites in complex proteomes
Ilaria Piazza, Nigel Beaton, Roland Bruderer, et al.
Nature Communications (2020) Vol. 11, Iss. 1
Open Access | Times Cited: 124
Ilaria Piazza, Nigel Beaton, Roland Bruderer, et al.
Nature Communications (2020) Vol. 11, Iss. 1
Open Access | Times Cited: 124
Recent advances in identifying protein targets in drug discovery
Jaeyoung Ha, Hankum Park, Jongmin Park, et al.
Cell chemical biology (2020) Vol. 28, Iss. 3, pp. 394-423
Open Access | Times Cited: 117
Jaeyoung Ha, Hankum Park, Jongmin Park, et al.
Cell chemical biology (2020) Vol. 28, Iss. 3, pp. 394-423
Open Access | Times Cited: 117
Dual chemical probes enable quantitative system-wide analysis of protein prenylation and prenylation dynamics
Elisabeth M. Storck, Julia Morales‐Sanfrutos, Remigiusz A. Serwa, et al.
Nature Chemistry (2019) Vol. 11, Iss. 6, pp. 552-561
Open Access | Times Cited: 105
Elisabeth M. Storck, Julia Morales‐Sanfrutos, Remigiusz A. Serwa, et al.
Nature Chemistry (2019) Vol. 11, Iss. 6, pp. 552-561
Open Access | Times Cited: 105
Recent progress in mass spectrometry-based strategies for elucidating protein–protein interactions
Teck Yew Low, Saiful Effendi Syafruddin, M. Aiman Mohtar, et al.
Cellular and Molecular Life Sciences (2021) Vol. 78, Iss. 13, pp. 5325-5339
Open Access | Times Cited: 87
Teck Yew Low, Saiful Effendi Syafruddin, M. Aiman Mohtar, et al.
Cellular and Molecular Life Sciences (2021) Vol. 78, Iss. 13, pp. 5325-5339
Open Access | Times Cited: 87
Recent advances in developing active targeting and multi-functional drug delivery systems via bioorthogonal chemistry
Wenzhe Yi, Ping Xiao, Xiaochen Liu, et al.
Signal Transduction and Targeted Therapy (2022) Vol. 7, Iss. 1
Open Access | Times Cited: 68
Wenzhe Yi, Ping Xiao, Xiaochen Liu, et al.
Signal Transduction and Targeted Therapy (2022) Vol. 7, Iss. 1
Open Access | Times Cited: 68
Evaluation of fully-functionalized diazirine tags for chemical proteomic applications
Louis P. Conway, Appaso Mahadev Jadhav, Rick A. Homan, et al.
Chemical Science (2021) Vol. 12, Iss. 22, pp. 7839-7847
Open Access | Times Cited: 65
Louis P. Conway, Appaso Mahadev Jadhav, Rick A. Homan, et al.
Chemical Science (2021) Vol. 12, Iss. 22, pp. 7839-7847
Open Access | Times Cited: 65
Application of omics- and multi-omics-based techniques for natural product target discovery
Hongwei Zhang, Chao Lv, Lijun Zhang, et al.
Biomedicine & Pharmacotherapy (2021) Vol. 141, pp. 111833-111833
Open Access | Times Cited: 65
Hongwei Zhang, Chao Lv, Lijun Zhang, et al.
Biomedicine & Pharmacotherapy (2021) Vol. 141, pp. 111833-111833
Open Access | Times Cited: 65
SP3‐FAIMS Chemoproteomics for High‐Coverage Profiling of the Human Cysteinome**
Tianyang Yan, Heta S. Desai, Lisa M. Boatner, et al.
ChemBioChem (2021) Vol. 22, Iss. 10, pp. 1841-1851
Open Access | Times Cited: 64
Tianyang Yan, Heta S. Desai, Lisa M. Boatner, et al.
ChemBioChem (2021) Vol. 22, Iss. 10, pp. 1841-1851
Open Access | Times Cited: 64
An Overview of Cell-Based Assay Platforms for the Solute Carrier Family of Transporters
Vojtech Dvorak, Tabea Wiedmer, Álvaro Inglés‐Prieto, et al.
Frontiers in Pharmacology (2021) Vol. 12
Open Access | Times Cited: 57
Vojtech Dvorak, Tabea Wiedmer, Álvaro Inglés‐Prieto, et al.
Frontiers in Pharmacology (2021) Vol. 12
Open Access | Times Cited: 57
An Expanding Repertoire of Protein Acylations
Yuxuan Xu, Zhenyu Shi, Li Bao
Molecular & Cellular Proteomics (2022) Vol. 21, Iss. 3, pp. 100193-100193
Open Access | Times Cited: 52
Yuxuan Xu, Zhenyu Shi, Li Bao
Molecular & Cellular Proteomics (2022) Vol. 21, Iss. 3, pp. 100193-100193
Open Access | Times Cited: 52
In situ identification of cellular drug targets in mammalian tissue
Zhengyuan Pang, Michael A. Schafroth, Daisuke Ogasawara, et al.
Cell (2022) Vol. 185, Iss. 10, pp. 1793-1805.e17
Open Access | Times Cited: 51
Zhengyuan Pang, Michael A. Schafroth, Daisuke Ogasawara, et al.
Cell (2022) Vol. 185, Iss. 10, pp. 1793-1805.e17
Open Access | Times Cited: 51
Click chemistry and drug delivery: A bird's-eye view
Shameer M. Kondengadan, Shubham Bansal, Ce Yang, et al.
Acta Pharmaceutica Sinica B (2022) Vol. 13, Iss. 5, pp. 1990-2016
Open Access | Times Cited: 49
Shameer M. Kondengadan, Shubham Bansal, Ce Yang, et al.
Acta Pharmaceutica Sinica B (2022) Vol. 13, Iss. 5, pp. 1990-2016
Open Access | Times Cited: 49
Tools for mammalian glycoscience research
Matthew E. Griffin, Linda C. Hsieh‐Wilson
Cell (2022) Vol. 185, Iss. 15, pp. 2657-2677
Open Access | Times Cited: 43
Matthew E. Griffin, Linda C. Hsieh‐Wilson
Cell (2022) Vol. 185, Iss. 15, pp. 2657-2677
Open Access | Times Cited: 43
Advances in enrichment methods for mass spectrometry-based proteomics analysis of post-translational modifications
Jessica Brandi, Roberta Noberini, Tiziana Bonaldi, et al.
Journal of Chromatography A (2022) Vol. 1678, pp. 463352-463352
Closed Access | Times Cited: 41
Jessica Brandi, Roberta Noberini, Tiziana Bonaldi, et al.
Journal of Chromatography A (2022) Vol. 1678, pp. 463352-463352
Closed Access | Times Cited: 41