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Microscopic Temperature Control Reveals Cooperative Regulation of Actin-Myosin Interaction by Drebrin E.

Nano letters

Kubota H, Ogawa H, Miyazaki M, Ishii S, Oyama K, Kawamura Y, Ishiwata S, Suzuki M.
PMID: 34751025
Nano Lett. 2021 Nov 24;21(22):9526-9533. doi: 10.1021/acs.nanolett.1c02955. Epub 2021 Nov 09.

Drebrin E is a regulatory protein of intracellular force produced by actomyosin complexes, that is, myosin molecular motors interacting with actin filaments. The expression level of drebrin E in nerve cells decreases as the animal grows, suggesting its pivotal...

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Kubota H, Ogawa H, Miyazaki M, et al. Microscopic Temperature Control Reveals Cooperative Regulation of Actin-Myosin Interaction by Drebrin E. Nano Lett. 2021;21(22):9526-9533doi: 10.1021/acs.nanolett.1c02955.
Kubota, H., Ogawa, H., Miyazaki, M., Ishii, S., Oyama, K., Kawamura, Y., Ishiwata, S., & Suzuki, M. (2021). Microscopic Temperature Control Reveals Cooperative Regulation of Actin-Myosin Interaction by Drebrin E. Nano letters, 21(22), 9526-9533. https://doi.org/10.1021/acs.nanolett.1c02955
Kubota, Hiroaki, et al. "Microscopic Temperature Control Reveals Cooperative Regulation of Actin-Myosin Interaction by Drebrin E." Nano letters vol. 21,22 (2021): 9526-9533. doi: https://doi.org/10.1021/acs.nanolett.1c02955
Kubota H, Ogawa H, Miyazaki M, Ishii S, Oyama K, Kawamura Y, Ishiwata S, Suzuki M. Microscopic Temperature Control Reveals Cooperative Regulation of Actin-Myosin Interaction by Drebrin E. Nano Lett. 2021 Nov 24;21(22):9526-9533. doi: 10.1021/acs.nanolett.1c02955. Epub 2021 Nov 09. PMID: 34751025.
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High-resolution structures of the actomyosin-V complex in three nucleotide states provide insights into the force generation mechanism.

eLife

Pospich S, Sweeney HL, Houdusse A, Raunser S.
PMID: 34812732
Elife. 2021 Nov 23;10. doi: 10.7554/eLife.73724.

The molecular motor myosin undergoes a series of major structural transitions during its force-producing motor cycle. The underlying mechanism and its coupling to ATP hydrolysis and actin binding are only partially understood, mostly due to sparse structural data on...

Cite
Pospich S, Sweeney HL, Houdusse A, et al. High-resolution structures of the actomyosin-V complex in three nucleotide states provide insights into the force generation mechanism. Elife. 2021;10doi: 10.7554/eLife.73724.
Pospich, S., Sweeney, H. L., Houdusse, A., & Raunser, S. (2021). High-resolution structures of the actomyosin-V complex in three nucleotide states provide insights into the force generation mechanism. eLife, 10. https://doi.org/10.7554/eLife.73724
Pospich, Sabrina, et al. "High-resolution structures of the actomyosin-V complex in three nucleotide states provide insights into the force generation mechanism." eLife vol. 10 (2021). doi: https://doi.org/10.7554/eLife.73724
Pospich S, Sweeney HL, Houdusse A, Raunser S. High-resolution structures of the actomyosin-V complex in three nucleotide states provide insights into the force generation mechanism. Elife. 2021 Nov 23;10. doi: 10.7554/eLife.73724. PMID: 34812732.
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Nonmuscle Myosin II in cancer cell migration and mechanotransduction.

The international journal of biochemistry & cell biology

Halder D, Mallick D, Chatterjee A, Jana SS.
PMID: 34400319
Int J Biochem Cell Biol. 2021 Oct;139:106058. doi: 10.1016/j.biocel.2021.106058. Epub 2021 Aug 13.

Cell migration is a key step of cancer metastasis, immune-cell navigation, homing of stem cells and development. What adds complexity to it is the heterogeneity of the tissue environment that gives rise to a vast diversity of migratory mechanisms...

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Halder D, Mallick D, Chatterjee A, et al. Nonmuscle Myosin II in cancer cell migration and mechanotransduction. Int J Biochem Cell Biol. 2021;139:106058doi: 10.1016/j.biocel.2021.106058.
Halder, D., Mallick, D., Chatterjee, A., & Jana, S. S. (2021). Nonmuscle Myosin II in cancer cell migration and mechanotransduction. The international journal of biochemistry & cell biology, 139106058. https://doi.org/10.1016/j.biocel.2021.106058
Halder, Debdatta, et al. "Nonmuscle Myosin II in cancer cell migration and mechanotransduction." The international journal of biochemistry & cell biology vol. 139 (2021): 106058. doi: https://doi.org/10.1016/j.biocel.2021.106058
Halder D, Mallick D, Chatterjee A, Jana SS. Nonmuscle Myosin II in cancer cell migration and mechanotransduction. Int J Biochem Cell Biol. 2021 Oct;139:106058. doi: 10.1016/j.biocel.2021.106058. Epub 2021 Aug 13. PMID: 34400319.
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Aurora-B phosphorylates the myosin II heavy chain to promote cytokinesis.

The Journal of biological chemistry

Babkoff A, Cohen-Kfir E, Aharon H, Ravid S.
PMID: 34343568
J Biol Chem. 2021 Sep;297(3):101024. doi: 10.1016/j.jbc.2021.101024. Epub 2021 Jul 31.

Cytokinesis, the final step of mitosis, is mediated by an actomyosin contractile ring, the formation of which is temporally and spatially regulated following anaphase onset. Aurora-B is a member of the chromosomal passenger complex, which regulates various processes during...

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Babkoff A, Cohen-Kfir E, Aharon H, et al. Aurora-B phosphorylates the myosin II heavy chain to promote cytokinesis. J Biol Chem. 2021;297(3):101024doi: 10.1016/j.jbc.2021.101024.
Babkoff, A., Cohen-Kfir, E., Aharon, H., & Ravid, S. (2021). Aurora-B phosphorylates the myosin II heavy chain to promote cytokinesis. The Journal of biological chemistry, 297(3), 101024. https://doi.org/10.1016/j.jbc.2021.101024
Babkoff, Aryeh, et al. "Aurora-B phosphorylates the myosin II heavy chain to promote cytokinesis." The Journal of biological chemistry vol. 297,3 (2021): 101024. doi: https://doi.org/10.1016/j.jbc.2021.101024
Babkoff A, Cohen-Kfir E, Aharon H, Ravid S. Aurora-B phosphorylates the myosin II heavy chain to promote cytokinesis. J Biol Chem. 2021 Sep;297(3):101024. doi: 10.1016/j.jbc.2021.101024. Epub 2021 Jul 31. PMID: 34343568; PMCID: PMC8385403.
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How adherens junctions move cells during collective migration.

Faculty reviews

Gupta S, Yap AS.
PMID: 34308422
Fac Rev. 2021 Jun 15;10:56. doi: 10.12703/r/10-56. eCollection 2021.

In this review, we consider how the association between adherens junctions and the actomyosin cytoskeleton influences collective cell movement. We focus on recent findings which reveal different ways for adherens junctions to promote the locomotion of cells within tissues:...

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Gupta S, Yap AS. How adherens junctions move cells during collective migration. Fac Rev. 2021;10:56doi: 10.12703/r/10-56.
Gupta, S., & Yap, A. S. (2021). How adherens junctions move cells during collective migration. Faculty reviews, 1056. https://doi.org/10.12703/r/10-56
Gupta, Shafali, and Yap, Alpha S. "How adherens junctions move cells during collective migration." Faculty reviews vol. 10 (2021): 56. doi: https://doi.org/10.12703/r/10-56
Gupta S, Yap AS. How adherens junctions move cells during collective migration. Fac Rev. 2021 Jun 15;10:56. doi: 10.12703/r/10-56. eCollection 2021. PMID: 34308422; PMCID: PMC8265563.
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Actomyosin dynamics modulate microtubule deformation and growth during T-cell activation.

Molecular biology of the cell

Rey-Suarez I, Rogers N, Kerr S, Shroff H, Upadhyaya A.
PMID: 33826369
Mol Biol Cell. 2021 Aug 19;32(18):1641-1653. doi: 10.1091/mbc.E20-10-0685. Epub 2021 Apr 07.

Activation of T-cells leads to the formation of immune synapses (ISs) with antigen-presenting cells. This requires T-cell polarization and coordination between the actomyosin and microtubule cytoskeletons. The interactions between these two cytoskeletal components during T-cell activation are not well...

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Rey-Suarez I, Rogers N, Kerr S, et al. Actomyosin dynamics modulate microtubule deformation and growth during T-cell activation. Mol Biol Cell. 2021;32(18):1641-1653doi: 10.1091/mbc.E20-10-0685.
Rey-Suarez, I., Rogers, N., Kerr, S., Shroff, H., & Upadhyaya, A. (2021). Actomyosin dynamics modulate microtubule deformation and growth during T-cell activation. Molecular biology of the cell, 32(18), 1641-1653. https://doi.org/10.1091/mbc.E20-10-0685
Rey-Suarez, Ivan, et al. "Actomyosin dynamics modulate microtubule deformation and growth during T-cell activation." Molecular biology of the cell vol. 32,18 (2021): 1641-1653. doi: https://doi.org/10.1091/mbc.E20-10-0685
Rey-Suarez I, Rogers N, Kerr S, Shroff H, Upadhyaya A. Actomyosin dynamics modulate microtubule deformation and growth during T-cell activation. Mol Biol Cell. 2021 Aug 19;32(18):1641-1653. doi: 10.1091/mbc.E20-10-0685. Epub 2021 Apr 07. PMID: 33826369; PMCID: PMC8684730.
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Spatial and temporal dynamics of RhoA activities of single breast tumor cells in a 3D environment revealed by a machine learning-assisted FRET technique.

Experimental cell research

Cheung BCH, Hodgson L, Segall JE, Wu M.
PMID: 34813733
Exp Cell Res. 2021 Nov 20;410(2):112939. doi: 10.1016/j.yexcr.2021.112939. Epub 2021 Nov 20.

One of the hallmarks of cancer cells is their exceptional ability to migrate within the extracellular matrix (ECM) for gaining access to the circulatory system, a critical step of cancer metastasis. RhoA, a small GTPase, is known to be...

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Cheung BCH, Hodgson L, Segall JE, et al. Spatial and temporal dynamics of RhoA activities of single breast tumor cells in a 3D environment revealed by a machine learning-assisted FRET technique. Exp Cell Res. 2021;410(2):112939doi: 10.1016/j.yexcr.2021.112939.
Cheung, B. C. H., Hodgson, L., Segall, J. E., & Wu, M. (2021). Spatial and temporal dynamics of RhoA activities of single breast tumor cells in a 3D environment revealed by a machine learning-assisted FRET technique. Experimental cell research, 410(2), 112939. https://doi.org/10.1016/j.yexcr.2021.112939
Cheung, Brian C H, et al. "Spatial and temporal dynamics of RhoA activities of single breast tumor cells in a 3D environment revealed by a machine learning-assisted FRET technique." Experimental cell research vol. 410,2 (2021): 112939. doi: https://doi.org/10.1016/j.yexcr.2021.112939
Cheung BCH, Hodgson L, Segall JE, Wu M. Spatial and temporal dynamics of RhoA activities of single breast tumor cells in a 3D environment revealed by a machine learning-assisted FRET technique. Exp Cell Res. 2021 Nov 20;410(2):112939. doi: 10.1016/j.yexcr.2021.112939. Epub 2021 Nov 20. PMID: 34813733.
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In-frame deletion of SPECC1L microtubule association domain results in gain-of-function phenotypes affecting embryonic tissue movement and fusion events.

Human molecular genetics

Goering JP, Wenger LW, Stetsiv M, Moedritzer M, Hall EG, Isai DG, Jack BM, Umar Z, Rickabaugh MK, Czirok A, Saadi I.
PMID: 34302166
Hum Mol Genet. 2021 Dec 17;31(1):18-31. doi: 10.1093/hmg/ddab211.

Patients with autosomal dominant SPECC1L variants show syndromic malformations, including hypertelorism, cleft palate and omphalocele. These SPECC1L variants largely cluster in the second coiled-coil domain (CCD2), which facilitates association with microtubules. To study SPECC1L function in mice, we first...

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Goering JP, Wenger LW, Stetsiv M, et al. In-frame deletion of SPECC1L microtubule association domain results in gain-of-function phenotypes affecting embryonic tissue movement and fusion events. Hum Mol Genet. 2021;31(1):18-31doi: 10.1093/hmg/ddab211.
Goering, J. P., Wenger, L. W., Stetsiv, M., Moedritzer, M., Hall, E. G., Isai, D. G., Jack, B. M., Umar, Z., Rickabaugh, M. K., Czirok, A., & Saadi, I. (2021). In-frame deletion of SPECC1L microtubule association domain results in gain-of-function phenotypes affecting embryonic tissue movement and fusion events. Human molecular genetics, 31(1), 18-31. https://doi.org/10.1093/hmg/ddab211
Goering, Jeremy P, et al. "In-frame deletion of SPECC1L microtubule association domain results in gain-of-function phenotypes affecting embryonic tissue movement and fusion events." Human molecular genetics vol. 31,1 (2021): 18-31. doi: https://doi.org/10.1093/hmg/ddab211
Goering JP, Wenger LW, Stetsiv M, Moedritzer M, Hall EG, Isai DG, Jack BM, Umar Z, Rickabaugh MK, Czirok A, Saadi I. In-frame deletion of SPECC1L microtubule association domain results in gain-of-function phenotypes affecting embryonic tissue movement and fusion events. Hum Mol Genet. 2021 Dec 17;31(1):18-31. doi: 10.1093/hmg/ddab211. PMID: 34302166; PMCID: PMC8682745.
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Precision Surface Microtopography Regulates Cell Fate via Changes to Actomyosin Contractility and Nuclear Architecture.

Advanced science (Weinheim, Baden-Wurttemberg, Germany)

Carthew J, Abdelmaksoud HH, Hodgson-Garms M, Aslanoglou S, Ghavamian S, Elnathan R, Spatz JP, Brugger J, Thissen H, Voelcker NH, Cadarso VJ, Frith JE.
PMID: 33747730
Adv Sci (Weinh). 2021 Jan 29;8(6):2003186. doi: 10.1002/advs.202003186. eCollection 2021 Mar.

Cells are able to perceive complex mechanical cues from their microenvironment, which in turn influences their development. Although the understanding of these intricate mechanotransductive signals is evolving, the precise roles of substrate microtopography in directing cell fate is still...

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Carthew J, Abdelmaksoud HH, Hodgson-Garms M, et al. Precision Surface Microtopography Regulates Cell Fate via Changes to Actomyosin Contractility and Nuclear Architecture. Adv Sci (Weinh). 2021;8(6):2003186doi: 10.1002/advs.202003186.
Carthew, J., Abdelmaksoud, H. H., Hodgson-Garms, M., Aslanoglou, S., Ghavamian, S., Elnathan, R., Spatz, J. P., Brugger, J., Thissen, H., Voelcker, N. H., Cadarso, V. J., & Frith, J. E. (2021). Precision Surface Microtopography Regulates Cell Fate via Changes to Actomyosin Contractility and Nuclear Architecture. Advanced science (Weinheim, Baden-Wurttemberg, Germany), 8(6), 2003186. https://doi.org/10.1002/advs.202003186
Carthew, James, et al. "Precision Surface Microtopography Regulates Cell Fate via Changes to Actomyosin Contractility and Nuclear Architecture." Advanced science (Weinheim, Baden-Wurttemberg, Germany) vol. 8,6 (2021): 2003186. doi: https://doi.org/10.1002/advs.202003186
Carthew J, Abdelmaksoud HH, Hodgson-Garms M, Aslanoglou S, Ghavamian S, Elnathan R, Spatz JP, Brugger J, Thissen H, Voelcker NH, Cadarso VJ, Frith JE. Precision Surface Microtopography Regulates Cell Fate via Changes to Actomyosin Contractility and Nuclear Architecture. Adv Sci (Weinh). 2021 Jan 29;8(6):2003186. doi: 10.1002/advs.202003186. eCollection 2021 Mar. PMID: 33747730; PMCID: PMC7967085.
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High-resolution structures of the actomyosin-V complex in three nucleotide states provide insights into the force generation mechanism.

eLife

Pospich S, Sweeney HL, Houdusse A, Raunser S.
PMID: 34812732
Elife. 2021 Nov 23;10. doi: 10.7554/eLife.73724.

The molecular motor myosin undergoes a series of major structural transitions during its force-producing motor cycle. The underlying mechanism and its coupling to ATP hydrolysis and actin binding are only partially understood, mostly due to sparse structural data on...

Cite
Pospich S, Sweeney HL, Houdusse A, et al. High-resolution structures of the actomyosin-V complex in three nucleotide states provide insights into the force generation mechanism. Elife. 2021;10doi: 10.7554/eLife.73724.
Pospich, S., Sweeney, H. L., Houdusse, A., & Raunser, S. (2021). High-resolution structures of the actomyosin-V complex in three nucleotide states provide insights into the force generation mechanism. eLife, 10. https://doi.org/10.7554/eLife.73724
Pospich, Sabrina, et al. "High-resolution structures of the actomyosin-V complex in three nucleotide states provide insights into the force generation mechanism." eLife vol. 10 (2021). doi: https://doi.org/10.7554/eLife.73724
Pospich S, Sweeney HL, Houdusse A, Raunser S. High-resolution structures of the actomyosin-V complex in three nucleotide states provide insights into the force generation mechanism. Elife. 2021 Nov 23;10. doi: 10.7554/eLife.73724. PMID: 34812732; PMCID: PMC8735999.
Copy Download .nbib Format: NLM
High-resolution structures of the actomyosin-V complex in three nucleotide states provide insights into the force generation mechanism.

eLife

Pospich S, Sweeney HL, Houdusse A, Raunser S.
PMID: 34812732
Elife. 2021 Nov 23;10. doi: 10.7554/eLife.73724.

The molecular motor myosin undergoes a series of major structural transitions during its force-producing motor cycle. The underlying mechanism and its coupling to ATP hydrolysis and actin binding are only partially understood, mostly due to sparse structural data on...

Cite
Pospich S, Sweeney HL, Houdusse A, et al. High-resolution structures of the actomyosin-V complex in three nucleotide states provide insights into the force generation mechanism. Elife. 2021;10doi: 10.7554/eLife.73724.
Pospich, S., Sweeney, H. L., Houdusse, A., & Raunser, S. (2021). High-resolution structures of the actomyosin-V complex in three nucleotide states provide insights into the force generation mechanism. eLife, 10. https://doi.org/10.7554/eLife.73724
Pospich, Sabrina, et al. "High-resolution structures of the actomyosin-V complex in three nucleotide states provide insights into the force generation mechanism." eLife vol. 10 (2021). doi: https://doi.org/10.7554/eLife.73724
Pospich S, Sweeney HL, Houdusse A, Raunser S. High-resolution structures of the actomyosin-V complex in three nucleotide states provide insights into the force generation mechanism. Elife. 2021 Nov 23;10. doi: 10.7554/eLife.73724. PMID: 34812732; PMCID: PMC8735999.
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Showing 433 to 443 of 443 entries