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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:

Imaging and manipulating proteins in live cells through covalent labeling
Lin Xue, Julie Karpenko, Julien Hiblot, et al.
Nature Chemical Biology (2015) Vol. 11, Iss. 12, pp. 917-923
Closed Access | Times Cited: 210

Showing 1-25 of 210 citing articles:

Inverse electron demand Diels–Alder reactions in chemical biology
Bruno L. Oliveira, Zijian Guo, Gonçalo J. L. Bernardes
Chemical Society Reviews (2017) Vol. 46, Iss. 16, pp. 4895-4950
Open Access | Times Cited: 897
A general method to fine-tune fluorophores for live-cell and in vivo imaging
Jonathan B. Grimm, Anand K. Muthusamy, Yajie Liang, et al.
Nature Methods (2017) Vol. 14, Iss. 10, pp. 987-994
Open Access | Times Cited: 602
Genetically Encoded Fluorescent Biosensors Illuminate the Spatiotemporal Regulation of Signaling Networks
Eric C. Greenwald, Sohum Mehta, Jin Zhang
Chemical Reviews (2018) Vol. 118, Iss. 24, pp. 11707-11794
Open Access | Times Cited: 445
Small-Molecule Fluorescent Probes for Live-Cell Super-Resolution Microscopy
Lu Wang, Michelle S. Frei, Aleksandar Salim, et al.
Journal of the American Chemical Society (2018) Vol. 141, Iss. 7, pp. 2770-2781
Closed Access | Times Cited: 439
Bright photoactivatable fluorophores for single-molecule imaging
Jonathan B. Grimm, Brian P. English, Heejun Choi, et al.
Nature Methods (2016) Vol. 13, Iss. 12, pp. 985-988
Open Access | Times Cited: 379
Targeting the N terminus for site-selective protein modification
Christian Rosén, Matthew B. Francis
Nature Chemical Biology (2017) Vol. 13, Iss. 7, pp. 697-705
Closed Access | Times Cited: 326
A general strategy to develop cell permeable and fluorogenic probes for multicolour nanoscopy
Lu Wang, Mai Tran, Elisa D’Este, et al.
Nature Chemistry (2019) Vol. 12, Iss. 2, pp. 165-172
Open Access | Times Cited: 320
Chemistry for Covalent Modification of Endogenous/Native Proteins: From Test Tubes to Complex Biological Systems
Tomonori Tamura, Itaru Hamachi
Journal of the American Chemical Society (2018) Vol. 141, Iss. 7, pp. 2782-2799
Open Access | Times Cited: 298
Glyoxal as an alternative fixative to formaldehyde in immunostaining and super‐resolution microscopy
Katharina N. Richter, Natalia H. Revelo, Katharina J. Seitz, et al.
The EMBO Journal (2017) Vol. 37, Iss. 1, pp. 139-159
Open Access | Times Cited: 279
Chemo- and Regioselective Lysine Modification on Native Proteins
María João Matos, Bruno L. Oliveira, Nuria Martínez‐Sáez, et al.
Journal of the American Chemical Society (2018) Vol. 140, Iss. 11, pp. 4004-4017
Open Access | Times Cited: 259
EzColocalization: An ImageJ plugin for visualizing and measuring colocalization in cells and organisms
Weston Stauffer, Huanjie Sheng, Han N. Lim
Scientific Reports (2018) Vol. 8, Iss. 1
Open Access | Times Cited: 255
Arylation Chemistry for Bioconjugation
Chi Zhang, Ekaterina V. Vinogradova, Alexander M. Spokoyny, et al.
Angewandte Chemie International Edition (2018) Vol. 58, Iss. 15, pp. 4810-4839
Open Access | Times Cited: 233
Teaching Old Dyes New Tricks: Biological Probes Built from Fluoresceins and Rhodamines
Luke D. Lavis
Annual Review of Biochemistry (2017) Vol. 86, Iss. 1, pp. 825-843
Open Access | Times Cited: 231
Mass Spectrometry-Based Protein Footprinting for Higher-Order Structure Analysis: Fundamentals and Applications
Xiaoran Roger Liu, Mengru Zhang, Michael L. Gross
Chemical Reviews (2020) Vol. 120, Iss. 10, pp. 4355-4454
Open Access | Times Cited: 219
Systematic Tuning of Rhodamine Spirocyclization for Super-resolution Microscopy
Nicolas Lardon, Lu Wang, Aline Tschanz, et al.
Journal of the American Chemical Society (2021) Vol. 143, Iss. 36, pp. 14592-14600
Open Access | Times Cited: 127
Kinetic and Structural Characterization of the Self-Labeling Protein Tags HaloTag7, SNAP-tag, and CLIP-tag
Jonas Wilhelm, Stefanie F. Kühn, Mirosław Tarnawski, et al.
Biochemistry (2021) Vol. 60, Iss. 33, pp. 2560-2575
Open Access | Times Cited: 119
General Design Strategy to Precisely Control the Emission of Fluorophores via a Twisted Intramolecular Charge Transfer (TICT) Process
Kenjiro Hanaoka, Shimpei Iwaki, Kiyoshi Yagi, et al.
Journal of the American Chemical Society (2022) Vol. 144, Iss. 43, pp. 19778-19790
Closed Access | Times Cited: 93
A general design of caging-group-free photoactivatable fluorophores for live-cell nanoscopy
Richard Lincoln, Mariano L. Bossi, Michael Remmel, et al.
Nature Chemistry (2022) Vol. 14, Iss. 9, pp. 1013-1020
Open Access | Times Cited: 76
A general method for the development of multicolor biosensors with large dynamic ranges
Lars Hellweg, Anna Edenhofer, Lucas Barck, et al.
Nature Chemical Biology (2023) Vol. 19, Iss. 9, pp. 1147-1157
Open Access | Times Cited: 49
Optimized Red-Absorbing Dyes for Imaging and Sensing
Jonathan B. Grimm, Ariana N. Tkachuk, Ronak Patel, et al.
Journal of the American Chemical Society (2023) Vol. 145, Iss. 42, pp. 23000-23013
Open Access | Times Cited: 43
Chemically engineering cells for precision medicine
Yixin Wang, Zhaoting Li, Fanyi Mo, et al.
Chemical Society Reviews (2023) Vol. 52, Iss. 3, pp. 1068-1102
Closed Access | Times Cited: 41
Engineering paralog-specific PSD-95 recombinant binders as minimally interfering multimodal probes for advanced imaging techniques
Charlotte Rimbault, Christelle Breillat, Benjamin Compans, et al.
eLife (2024) Vol. 13
Open Access | Times Cited: 20
Bioorthogonal chemical labeling of endogenous neurotransmitter receptors in living mouse brains
Hiroshi Nonaka, Seiji Sakamoto, Kazuki Shiraiwa, et al.
Proceedings of the National Academy of Sciences (2024) Vol. 121, Iss. 6
Open Access | Times Cited: 17
Stoichiometric and irreversible cysteine-selective protein modification using carbonylacrylic reagents
Barbara Bernardim, Pedro M. S. D. Cal, María João Matos, et al.
Nature Communications (2016) Vol. 7, Iss. 1
Open Access | Times Cited: 165
Mapping the dynamics and nanoscale organization of synaptic adhesion proteins using monomeric streptavidin
Ingrid Chamma, Mathieu Letellier, Corey Butler, et al.
Nature Communications (2016) Vol. 7, Iss. 1
Open Access | Times Cited: 148
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