A single structurally conserved SUMOylation site in CRMP2 controls NaV1.7 function
Article Properties
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LanguageEnglish
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DOI (url)
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Publication Date2017/02/28
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Journal
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Indian UGC (journal)
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Refrences54
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Citations30
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Erik Thomas Dustrude Department of Pharmacology, College of Medicine, University of Arizona, Tucson, AZ, USA ORCID (unauthenticated)
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Samantha Perez-Miller Department of Pharmacology, College of Medicine, University of Arizona, Tucson, AZ, USA ORCID (unauthenticated)
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Liberty François-Moutal Department of Pharmacology, College of Medicine, University of Arizona, Tucson, AZ, USA ORCID (unauthenticated)
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Aubin Moutal Department of Pharmacology, College of Medicine, University of Arizona, Tucson, AZ, USA ORCID (unauthenticated)
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May Khanna Department of Pharmacology, College of Medicine, University of Arizona, Tucson, AZ, USA ORCID (unauthenticated)
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Rajesh Khanna Department of Pharmacology, College of Medicine, University of Arizona, Tucson, AZ, USADepartment of Anesthesiology, College of Medicine, University of Arizona, Tucson, AZ, USANeuroscience Graduate Interdisciplinary Program, College of Medicine, University of Arizona, Tucson, AZ, USA ORCID (unauthenticated)
Cite
Dustrude, Erik Thomas, et al. “A Single Structurally Conserved SUMOylation Site in CRMP2 Controls NaV1.7 Function”. Channels, vol. 11, no. 4, 2017, pp. 316-28, https://doi.org/10.1080/19336950.2017.1299838.
Dustrude, E. T., Perez-Miller, S., François-Moutal, L., Moutal, A., Khanna, M., & Khanna, R. (2017). A single structurally conserved SUMOylation site in CRMP2 controls NaV1.7 function. Channels, 11(4), 316-328. https://doi.org/10.1080/19336950.2017.1299838
Dustrude ET, Perez-Miller S, François-Moutal L, Moutal A, Khanna M, Khanna R. A single structurally conserved SUMOylation site in CRMP2 controls NaV1.7 function. Channels. 2017;11(4):316-28.
Journal Categories
Medicine
Therapeutics
Pharmacology
Science
Biology (General)
Science
Biology (General)
Genetics
Science
Physiology
Refrences
| Title | Journal | Journal Categories | Citations | Publication Date |
|---|---|---|---|---|
| CRMP-2 binds to tubulin heterodimers to promote microtubule assembly | Nature Cell Biology |
| 573 | 2002 |
| Interactive Tree Of Life v2: online annotation and display of phylogenetic trees made easy | Nucleic Acids Research |
| 1,118 | 2011 |
| Regulation of CREB signaling through L-type Ca2+channels by Nipsnap-2 | Channels |
| 17 | 2012 |
| 10.1107/S0907444909052925 | ||||
| 10.1107/S0907444910007493 |
Citations
| Title | Journal | Journal Categories | Citations | Publication Date |
|---|---|---|---|---|
| Correlative increasing expressions of KIF5b and Nav1.7 in DRG neurons of rats under neuropathic pain conditions | Physiology & Behavior |
| 1 | 2023 |
Identification and targeting of a unique Na
V
1.7 domain driving chronic pain | Proceedings of the National Academy of Sciences |
| 3 | 2023 |
A peptidomimetic modulator of the Ca
V
2.2 N-type calcium channel for chronic pain | Proceedings of the National Academy of Sciences |
| 2023 | |
Intranasal CRMP2-Ubc9 inhibitor regulates NaV1.7 to alleviate trigeminal neuropathic pain | Pain |
| 2023 | |
Contribution of the dihydropyrimidinase-like proteins family in synaptic physiology and in neurodevelopmental disorders | Frontiers in Neuroscience |
| 5 | 2023 |
Citations Analysis
The category
Medicine: Internal medicine: Neurosciences. Biological psychiatry. Neuropsychiatry 15
is the most commonly referenced area in studies that cite this article. The first research to cite this article was titled Dissecting the role of the CRMP2–neurofibromin complex on pain behaviors and was published in 2017. The most recent citation comes from a 2023 study titled A peptidomimetic modulator of the Ca
V
2.2 N-type calcium channel for chronic pain. This article reached its peak citation in 2019, with 8 citations. It has been cited in 18 different journals, 33% of which are open access. Among related journals, the Channels cited this research the most, with 5 citations. The chart below illustrates the annual citation trends for this article.