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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:

Vasohibins encode tubulin detyrosinating activity
Joppe Nieuwenhuis, Athanassios Adamopoulos, Onno B. Bleijerveld, et al.
Science (2017) Vol. 358, Iss. 6369, pp. 1453-1456
Open Access | Times Cited: 234

Showing 1-25 of 234 citing articles:

The tubulin code and its role in controlling microtubule properties and functions
Carsten Janke, Maria M. Magiera
Nature Reviews Molecular Cell Biology (2020) Vol. 21, Iss. 6, pp. 307-326
Open Access | Times Cited: 689
Axonal transport: Driving synaptic function
Pedro Guedes-Dias, Erika L.F. Holzbaur
Science (2019) Vol. 366, Iss. 6462
Open Access | Times Cited: 286
The Tubulin Code in Microtubule Dynamics and Information Encoding
Antonina Roll‐Mecak
Developmental Cell (2020) Vol. 54, Iss. 1, pp. 7-20
Open Access | Times Cited: 220
RETRACTED ARTICLE: N6-methyladenosine induced miR-143-3p promotes the brain metastasis of lung cancer via regulation of VASH1
Hongsheng Wang, Qianqian Deng, Ziyan Lv, et al.
Molecular Cancer (2019) Vol. 18, Iss. 1
Open Access | Times Cited: 204
Advances in chemistry and bioactivity of parthenolide
Robert R. A. Freund, Philipp Gobrecht, Dietmar Fischer, et al.
Natural Product Reports (2019) Vol. 37, Iss. 4, pp. 541-565
Closed Access | Times Cited: 149
The phenotypic landscape of essential human genes
Luke Funk, Kuan-Chung Su, Jimmy Ly, et al.
Cell (2022) Vol. 185, Iss. 24, pp. 4634-4653.e22
Open Access | Times Cited: 114
The Tubulin Code, from Molecules to Health and Disease
Elizabeth D. McKenna, Stephanie L. Sarbanes, Steven W. Cummings, et al.
Annual Review of Cell and Developmental Biology (2023) Vol. 39, Iss. 1, pp. 331-361
Open Access | Times Cited: 45
Tubulin Posttranslational Modifications and Emerging Links to Human Disease
Maria M. Magiera, Puja Singh, Sudarshan Gadadhar, et al.
Cell (2018) Vol. 173, Iss. 6, pp. 1323-1327
Open Access | Times Cited: 153
Cardiac microtubules in health and heart disease
Matthew A. Caporizzo, Yingxian Chen, Benjamin L. Prosser
Experimental Biology and Medicine (2019) Vol. 244, Iss. 15, pp. 1255-1272
Open Access | Times Cited: 93
The Tubulin Detyrosination Cycle: Function and Enzymes
Joppe Nieuwenhuis, Thijn R. Brummelkamp
Trends in Cell Biology (2018) Vol. 29, Iss. 1, pp. 80-92
Closed Access | Times Cited: 92
Microtubules Increase Diastolic Stiffness in Failing Human Cardiomyocytes and Myocardium
Matthew A. Caporizzo, Yingxian Chen, Ken Bedi, et al.
Circulation (2020) Vol. 141, Iss. 11, pp. 902-915
Open Access | Times Cited: 83
The Mechanism of Tubulin Assembly into Microtubules: Insights from Structural Studies
M. Knossow, Valérie Campanacci, Liza Ammar Khodja, et al.
iScience (2020) Vol. 23, Iss. 9, pp. 101511-101511
Open Access | Times Cited: 78
MARK4 controls ischaemic heart failure through microtubule detyrosination
Xianjun Yu, Chen Xiao, Mamta Amrute‐Nayak, et al.
Nature (2021) Vol. 594, Iss. 7864, pp. 560-565
Open Access | Times Cited: 78
Proteomic and Functional Studies Reveal Detyrosinated Tubulin as Treatment Target in Sarcomere Mutation-Induced Hypertrophic Cardiomyopathy
Maike Schuldt, Jiayi Pei, Magdaléna Harakaľová, et al.
Circulation Heart Failure (2021) Vol. 14, Iss. 1
Open Access | Times Cited: 77
Time-resolved proteomics profiling of the ciliary Hedgehog response
Elena A. May, Marian Kalocsay, Inès Galtier D’Auriac, et al.
The Journal of Cell Biology (2021) Vol. 220, Iss. 5
Open Access | Times Cited: 74
α-tubulin tail modifications regulate microtubule stability through selective effector recruitment, not changes in intrinsic polymer dynamics
Jiayi Chen, Ekaterina G. Kholina, Agnieszka Szyk, et al.
Developmental Cell (2021) Vol. 56, Iss. 14, pp. 2016-2028.e4
Open Access | Times Cited: 73
Tubulin post‐translational modifications control neuronal development and functions
Marie‐Jo Moutin, Christophe Bosc, Leticia Peris, et al.
Developmental Neurobiology (2020) Vol. 81, Iss. 3, pp. 253-272
Open Access | Times Cited: 72
Post-translational Modifications of the Protein Termini
Li Chen, Anna Kashina
Frontiers in Cell and Developmental Biology (2021) Vol. 9
Open Access | Times Cited: 70
Posttranslational modification of microtubules by the MATCAP detyrosinase
Lisa Landskron, Jitske Bak, Athanassios Adamopoulos, et al.
Science (2022) Vol. 376, Iss. 6595
Open Access | Times Cited: 55
A live-cell marker to visualize the dynamics of stable microtubules throughout the cell cycle
Klara I. Jansen, Malina K. Iwanski, Mithila Burute, et al.
The Journal of Cell Biology (2023) Vol. 222, Iss. 5
Open Access | Times Cited: 25
Transfer RNA derived fragment, tRF-Glu-CTC, aggravates the development of neovascular age-related macular degeneration
Liang Yu, Lingjie Kong, Yuelu Zhang, et al.
Theranostics (2024) Vol. 14, Iss. 4, pp. 1500-1516
Open Access | Times Cited: 9
Detyrosinated microtubules spatially constrain lysosomes facilitating lysosome–autophagosome fusion
Nitin Mohan, Elena M. Sorokina, Ione Vilanova Verdeny, et al.
The Journal of Cell Biology (2018) Vol. 218, Iss. 2, pp. 632-643
Open Access | Times Cited: 72
Molecular basis of vasohibins-mediated detyrosination and its impact on spindle function and mitosis
Shanhui Liao, Girish Rajendraprasad, Na Wang, et al.
Cell Research (2019) Vol. 29, Iss. 7, pp. 533-547
Open Access | Times Cited: 70
Structural basis of tubulin detyrosination by vasohibins
Faxiang Li, Yingjie Hu, Shu‐Tao Qi, et al.
Nature Structural & Molecular Biology (2019) Vol. 26, Iss. 7, pp. 583-591
Open Access | Times Cited: 62
The Tubulin Code in Mitosis and Cancer
Danilo Lopes, Hélder Maiato
Cells (2020) Vol. 9, Iss. 11, pp. 2356-2356
Open Access | Times Cited: 59
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