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1967 3
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2007 814
2008 825
2009 905
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2014 1075
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25,008 results

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Page 1
Regulation of end-binding protein EB1 in the control of microtubule dynamics.
Nehlig A, Molina A, Rodrigues-Ferreira S, Honoré S, Nahmias C. Nehlig A, et al. Cell Mol Life Sci. 2017 Jul;74(13):2381-2393. doi: 10.1007/s00018-017-2476-2. Epub 2017 Feb 15. Cell Mol Life Sci. 2017. PMID: 28204846 Free PMC article. Review.
End-binding protein 1 (EB1) is a plus-end-tracking protein (+TIP) that accumulates at growing microtubule ends and plays a pivotal role in the regulation of microtubule dynamics. EB1 autonomously binds an extended tubulin-GTP/GDP-Pi structure at growin …
End-binding protein 1 (EB1) is a plus-end-tracking protein (+TIP) that accumulates at growing microtubule ends and plays a piv …
Partial mimicry of the microtubule binding of tau by its membrane binding.
MacAinsh M, Zhou HX. MacAinsh M, et al. Protein Sci. 2023 Mar;32(3):e4581. doi: 10.1002/pro.4581. Protein Sci. 2023. PMID: 36710643 Free PMC article.
Tau, as typical of intrinsically disordered proteins (IDPs), binds to multiple targets including microtubules and acidic membranes. The latter two surfaces are both highly negatively charged, raising the prospect of mimicry in their binding by tau. The tau- …
Tau, as typical of intrinsically disordered proteins (IDPs), binds to multiple targets including microtubules and acidic membr …
The microtubule end-binding affinity of EB1 is enhanced by a dimeric organization that is susceptible to phosphorylation.
Song Y, Zhang Y, Pan Y, He J, Wang Y, Chen W, Guo J, Deng H, Xue Y, Fang X, Liang X. Song Y, et al. J Cell Sci. 2020 May 14;133(9):jcs241216. doi: 10.1242/jcs.241216. J Cell Sci. 2020. PMID: 32152183
In cells, microtubule dynamics are regulated by plus-end tracking proteins (+TIPs). End-binding protein 1 (EB1, also known as MAPRE1) acts as a master regulator of +TIP networks by targeting the growing ends of microtubules and recruiting other factors. Howev …
In cells, microtubule dynamics are regulated by plus-end tracking proteins (+TIPs). End-binding protein 1 (EB1, also known as …
Adenomatous Polyposis Coli as a Scaffold for Microtubule End-Binding Proteins.
Serre L, Stoppin-Mellet V, Arnal I. Serre L, et al. J Mol Biol. 2019 May 3;431(10):1993-2005. doi: 10.1016/j.jmb.2019.03.028. Epub 2019 Apr 6. J Mol Biol. 2019. PMID: 30959051
Our results show that APC-C binds along the microtubule wall but does not accumulate at microtubule tips, even when EB proteins are present. APC-C was also found to enhance EB binding at the extremity of growing microtubules and on the microt
Our results show that APC-C binds along the microtubule wall but does not accumulate at microtubule tips, even when EB …
Microtubule bundling by MAP65-1 protects against severing by inhibiting the binding of katanin.
Burkart GM, Dixit R. Burkart GM, et al. Mol Biol Cell. 2019 Jun 15;30(13):1587-1597. doi: 10.1091/mbc.E18-12-0776. Epub 2019 Apr 24. Mol Biol Cell. 2019. PMID: 31017848 Free PMC article.
Using various MAP65-1 mutant proteins, we demonstrate that efficient cross-linking of microtubules is crucial for this protective effect and that microtubule binding alone is not sufficient. Reduced severing due to microtubule bundling by MAP65-1 corre …
Using various MAP65-1 mutant proteins, we demonstrate that efficient cross-linking of microtubules is crucial for this protective eff …
Seeded microtubule growth for cryoelectron microscopy of end-binding proteins.
Maurer SP, Fourniol FJ, Hoenger A, Surrey T. Maurer SP, et al. Methods Mol Biol. 2014;1136:247-60. doi: 10.1007/978-1-4939-0329-0_11. Methods Mol Biol. 2014. PMID: 24633800
End-binding proteins (EBs) have the ability to autonomously track the ends of growing microtubules, where they recruit several proteins that control various aspects of microtubule cytoskeleton organization and function. ...In combination with single-particle …
End-binding proteins (EBs) have the ability to autonomously track the ends of growing microtubules, where they recruit several …
Structure of the ciliary tip central pair reveals the unique role of the microtubule-seam binding protein SPEF1.
Legal T, Joachimiak E, Parra M, Peng W, Tam A, Black C, Guha M, Nguyen CA, Ghanaeian A, Valente-Paterno M, Brouhard G, Gaertig J, Wloga D, Bui KH. Legal T, et al. Curr Biol. 2025 Jul 21;35(14):3404-3417.e6. doi: 10.1016/j.cub.2025.06.020. Epub 2025 Jul 11. Curr Biol. 2025. PMID: 40651469 Free PMC article.
Moreover, we found that the conserved protein SPEF1 binds to both microtubule seams and crosslinked the two microtubules. In vitro, human SPEF1 binds to the microtubule seam as visualized by cryoelectron tomography and subtomogram averaging. Sin …
Moreover, we found that the conserved protein SPEF1 binds to both microtubule seams and crosslinked the two microtubules
The binding of Borealin to microtubules underlies a tension independent kinetochore-microtubule error correction pathway.
Trivedi P, Zaytsev AV, Godzi M, Ataullakhanov FI, Grishchuk EL, Stukenberg PT. Trivedi P, et al. Nat Commun. 2019 Feb 8;10(1):682. doi: 10.1038/s41467-019-08418-4. Nat Commun. 2019. PMID: 30737408 Free PMC article.
Here we find these microtubules control kinetochore phosphorylation by the CPC in a tension independent manner via a microtubule-binding site on the Borealin subunit. ...Experimental and modeling evidence suggests that kinetochore phosphorylation is greatly s …
Here we find these microtubules control kinetochore phosphorylation by the CPC in a tension independent manner via a microtubule
Cep120 promotes microtubule formation through a unique tubulin binding C2 domain.
Sharma A, Gerard SF, Olieric N, Steinmetz MO. Sharma A, et al. J Struct Biol. 2018 Jul;203(1):62-70. doi: 10.1016/j.jsb.2018.01.009. Epub 2018 Feb 1. J Struct Biol. 2018. PMID: 29398280
Surprisingly, unlike the classical C2 domains, all three Cep120 C2 domains lack calcium- and phospholipid-binding activities. However, biophysical and biochemical assays revealed that the N-terminal Cep120 C2 domain (C2A) binds to both tubulin and microtubules
Surprisingly, unlike the classical C2 domains, all three Cep120 C2 domains lack calcium- and phospholipid-binding activities. However …
Rapid binding to protofilament edge sites facilitates tip tracking of EB1 at growing microtubule plus-ends.
Gonzalez SJ, Heckel JM, Goldblum RR, Reid TA, McClellan M, Gardner MK. Gonzalez SJ, et al. Elife. 2024 Feb 22;13:e91719. doi: 10.7554/eLife.91719. Elife. 2024. PMID: 38385657 Free PMC article.
It is widely accepted that EB1 binds with higher affinity to GTP-tubulin subunits at the growing microtubule tip, relative to GDP-tubulin along the microtubule length. ...We found that DARPin blocked EB1 protofilament-edge binding, which led to a decre …
It is widely accepted that EB1 binds with higher affinity to GTP-tubulin subunits at the growing microtubule tip, relative to …
25,008 results
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