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Showing 1 to 12 of 443 entries
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Actomyosin stress fiber mechanosensing in 2D and 3D.

F1000Research

Lee S, Kumar S.
PMID: 27635242
F1000Res. 2016 Sep 07;5. doi: 10.12688/f1000research.8800.1. eCollection 2016.

Mechanotransduction is the process through which cells survey the mechanical properties of their environment, convert these mechanical inputs into biochemical signals, and modulate their phenotype in response. These mechanical inputs, which may be encoded in the form of extracellular...

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Lee S, Kumar S. Actomyosin stress fiber mechanosensing in 2D and 3D. F1000Res. 2016;5doi: 10.12688/f1000research.8800.1.
Lee, S., & Kumar, S. (2016). Actomyosin stress fiber mechanosensing in 2D and 3D. F1000Research, 5. https://doi.org/10.12688/f1000research.8800.1
Lee, Stacey, and Kumar, Sanjay. "Actomyosin stress fiber mechanosensing in 2D and 3D." F1000Research vol. 5 (2016). doi: https://doi.org/10.12688/f1000research.8800.1
Lee S, Kumar S. Actomyosin stress fiber mechanosensing in 2D and 3D. F1000Res. 2016 Sep 07;5. doi: 10.12688/f1000research.8800.1. eCollection 2016. PMID: 27635242; PMCID: PMC5017290.
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Mitochondria-cytoskeleton associations in mammalian cytokinesis.

Cell division

Lawrence EJ, Boucher E, Mandato CA.
PMID: 27030796
Cell Div. 2016 Mar 18;11:3. doi: 10.1186/s13008-016-0015-4. eCollection 2016.

BACKGROUND: The role of the cytoskeleton in regulating mitochondrial distribution in dividing mammalian cells is poorly understood. We previously demonstrated that mitochondria are transported to the cleavage furrow during cytokinesis in a microtubule-dependent manner. However, the exact subset of...

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Lawrence EJ, Boucher E, Mandato CA. Mitochondria-cytoskeleton associations in mammalian cytokinesis. Cell Div. 2016;11:3doi: 10.1186/s13008-016-0015-4.
Lawrence, E. J., Boucher, E., & Mandato, C. A. (2016). Mitochondria-cytoskeleton associations in mammalian cytokinesis. Cell division, 113. https://doi.org/10.1186/s13008-016-0015-4
Lawrence, E J, et al. "Mitochondria-cytoskeleton associations in mammalian cytokinesis." Cell division vol. 11 (2016): 3. doi: https://doi.org/10.1186/s13008-016-0015-4
Lawrence EJ, Boucher E, Mandato CA. Mitochondria-cytoskeleton associations in mammalian cytokinesis. Cell Div. 2016 Mar 18;11:3. doi: 10.1186/s13008-016-0015-4. eCollection 2016. PMID: 27030796; PMCID: PMC4812650.
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Cdc42 and RhoA reveal different spatio-temporal dynamics upon local stimulation with Semaphorin-3A.

Frontiers in cellular neuroscience

Iseppon F, Napolitano LM, Torre V, Cojoc D.
PMID: 26379503
Front Cell Neurosci. 2015 Aug 26;9:333. doi: 10.3389/fncel.2015.00333. eCollection 2015.

Small RhoGTPases, such as Cdc42 and RhoA, are key players in integrating external cues and intracellular signaling pathways that regulate growth cone (GC) motility. Indeed, Cdc42 is involved in actin polymerization and filopodia formation, whereas RhoA induces GC collapse...

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Iseppon F, Napolitano LM, Torre V, et al. Cdc42 and RhoA reveal different spatio-temporal dynamics upon local stimulation with Semaphorin-3A. Front Cell Neurosci. 2015;9:333doi: 10.3389/fncel.2015.00333.
Iseppon, F., Napolitano, L. M., Torre, V., & Cojoc, D. (2015). Cdc42 and RhoA reveal different spatio-temporal dynamics upon local stimulation with Semaphorin-3A. Frontiers in cellular neuroscience, 9333. https://doi.org/10.3389/fncel.2015.00333
Iseppon, Federico, et al. "Cdc42 and RhoA reveal different spatio-temporal dynamics upon local stimulation with Semaphorin-3A." Frontiers in cellular neuroscience vol. 9 (2015): 333. doi: https://doi.org/10.3389/fncel.2015.00333
Iseppon F, Napolitano LM, Torre V, Cojoc D. Cdc42 and RhoA reveal different spatio-temporal dynamics upon local stimulation with Semaphorin-3A. Front Cell Neurosci. 2015 Aug 26;9:333. doi: 10.3389/fncel.2015.00333. eCollection 2015. PMID: 26379503; PMCID: PMC4549648.
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Analysis of Contractility and Invasion Potential of Two Canine Mammary Tumor Cell Lines.

Frontiers in veterinary science

Rajakylä K, Krishnan R, Tojkander S.
PMID: 28955712
Front Vet Sci. 2017 Sep 12;4:149. doi: 10.3389/fvets.2017.00149. eCollection 2017.

Cancer cells are surrounded by a mechanically and biochemically distinct microenvironment that undergoes dynamic changes throughout the neoplastic progression. During this progression, some cancer cells acquire abnormal characteristics that potentiate their escape from the primary tumor site, to establish...

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Rajakylä K, Krishnan R, Tojkander S. Analysis of Contractility and Invasion Potential of Two Canine Mammary Tumor Cell Lines. Front Vet Sci. 2017;4:149doi: 10.3389/fvets.2017.00149.
Rajakylä, K., Krishnan, R., & Tojkander, S. (2017). Analysis of Contractility and Invasion Potential of Two Canine Mammary Tumor Cell Lines. Frontiers in veterinary science, 4149. https://doi.org/10.3389/fvets.2017.00149
Rajakylä, Kaisa, et al. "Analysis of Contractility and Invasion Potential of Two Canine Mammary Tumor Cell Lines." Frontiers in veterinary science vol. 4 (2017): 149. doi: https://doi.org/10.3389/fvets.2017.00149
Rajakylä K, Krishnan R, Tojkander S. Analysis of Contractility and Invasion Potential of Two Canine Mammary Tumor Cell Lines. Front Vet Sci. 2017 Sep 12;4:149. doi: 10.3389/fvets.2017.00149. eCollection 2017. PMID: 28955712; PMCID: PMC5600937.
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Heavy-meromyosin-decoration of microfilaments from Mougeotia protoplasts.

Planta

Klein K, Wagner G, Blatt MR.
PMID: 24306883
Planta. 1980 Dec;150(5):354-6. doi: 10.1007/BF00390169.

The cell wall of the green alga Mougeotia was enzymatically digested by macerase and cellulysin. Released protoplasts were spread on poly-L-ornithine, formvar-carbon-coated grids, and cell fragments were collected for structural characterization. Large numbers of 5-7 nm filaments are seen...

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Klein K, Wagner G, Blatt MR. Heavy-meromyosin-decoration of microfilaments from Mougeotia protoplasts. Planta. 1980;150(5):354-6doi: 10.1007/BF00390169.
Klein, K., Wagner, G., & Blatt, M. R. (1980). Heavy-meromyosin-decoration of microfilaments from Mougeotia protoplasts. Planta, 150(5), 354-6. https://doi.org/10.1007/BF00390169
Klein, K, et al. "Heavy-meromyosin-decoration of microfilaments from Mougeotia protoplasts." Planta vol. 150,5 (1980): 354-6. doi: https://doi.org/10.1007/BF00390169
Klein K, Wagner G, Blatt MR. Heavy-meromyosin-decoration of microfilaments from Mougeotia protoplasts. Planta. 1980 Dec;150(5):354-6. doi: 10.1007/BF00390169. PMID: 24306883.
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Protein Bodies in Leaves Exchange Contents through the Endoplasmic Reticulum.

Frontiers in plant science

Saberianfar R, Sattarzadeh A, Joensuu JJ, Kohalmi SE, Menassa R.
PMID: 27242885
Front Plant Sci. 2016 May 23;7:693. doi: 10.3389/fpls.2016.00693. eCollection 2016.

Protein bodies (PBs) are organelles found in seeds whose main function is the storage of proteins that are used during germination for sustaining growth. PBs can also be induced to form in leaves when foreign proteins are produced at...

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Saberianfar R, Sattarzadeh A, Joensuu JJ, et al. Protein Bodies in Leaves Exchange Contents through the Endoplasmic Reticulum. Front Plant Sci. 2016;7:693doi: 10.3389/fpls.2016.00693.
Saberianfar, R., Sattarzadeh, A., Joensuu, J. J., Kohalmi, S. E., & Menassa, R. (2016). Protein Bodies in Leaves Exchange Contents through the Endoplasmic Reticulum. Frontiers in plant science, 7693. https://doi.org/10.3389/fpls.2016.00693
Saberianfar, Reza, et al. "Protein Bodies in Leaves Exchange Contents through the Endoplasmic Reticulum." Frontiers in plant science vol. 7 (2016): 693. doi: https://doi.org/10.3389/fpls.2016.00693
Saberianfar R, Sattarzadeh A, Joensuu JJ, Kohalmi SE, Menassa R. Protein Bodies in Leaves Exchange Contents through the Endoplasmic Reticulum. Front Plant Sci. 2016 May 23;7:693. doi: 10.3389/fpls.2016.00693. eCollection 2016. PMID: 27242885; PMCID: PMC4876836.
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Mechanics of Relaxation of the Human Heart.

News in physiological sciences : an international journal of physiology produced jointly by the International Union of Physiological Sciences and the American Physiological Society

Chemla D, Coirault C, Hébert JL, Lecarpentier Y.
PMID: 11390883
News Physiol Sci. 2000 Apr;15:78-83. doi: 10.1152/physiologyonline.2000.15.2.78.

Rapid and complete relaxation is a prerequisite for cardiac output adaptation to changes in loading conditions, inotropic stimulation, and heart rate. In the healthy human heart, the rate and extent of relaxation depend mainly on actomyosin cross bridge dissociation...

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Chemla D, Coirault C, Hébert JL, et al. Mechanics of Relaxation of the Human Heart. News Physiol Sci. 2000;15:78-83doi: 10.1152/physiologyonline.2000.15.2.78.
Chemla, D., Coirault, C., Hébert, J. L., & Lecarpentier, Y. (2000). Mechanics of Relaxation of the Human Heart. News in physiological sciences : an international journal of physiology produced jointly by the International Union of Physiological Sciences and the American Physiological Society, 1578-83. https://doi.org/10.1152/physiologyonline.2000.15.2.78
Chemla, Denis, et al. "Mechanics of Relaxation of the Human Heart." News in physiological sciences : an international journal of physiology produced jointly by the International Union of Physiological Sciences and the American Physiological Society vol. 15 (2000): 78-83. doi: https://doi.org/10.1152/physiologyonline.2000.15.2.78
Chemla D, Coirault C, Hébert JL, Lecarpentier Y. Mechanics of Relaxation of the Human Heart. News Physiol Sci. 2000 Apr;15:78-83. doi: 10.1152/physiologyonline.2000.15.2.78. PMID: 11390883.
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Actomyosin-mediated statolith positioning and sedimentation in gravisensing plant cells studied in microgravity.

Journal of gravitational physiology : a journal of the International Society for Gravitational Physiology

Braun M.
PMID: 15002553
J Gravit Physiol. 2002 Jul;9(1):P215-6.

Graviresponding and tip-growing characean rhizoids and protonemata possess a highly efficient actin-based system to control and correct the position of their statoliths, a prerequisite for gravisensing. Acropetally and basipetally acting actomyosin forces and gravity are the components of the...

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Braun M. Actomyosin-mediated statolith positioning and sedimentation in gravisensing plant cells studied in microgravity. J Gravit Physiol. 2002;9(1):P215-6
Braun, M. (2002). Actomyosin-mediated statolith positioning and sedimentation in gravisensing plant cells studied in microgravity. Journal of gravitational physiology : a journal of the International Society for Gravitational Physiology, 9(1), P215-6.
Braun, Markus. "Actomyosin-mediated statolith positioning and sedimentation in gravisensing plant cells studied in microgravity." Journal of gravitational physiology : a journal of the International Society for Gravitational Physiology vol. 9,1 (2002): P215-6.
Braun M. Actomyosin-mediated statolith positioning and sedimentation in gravisensing plant cells studied in microgravity. J Gravit Physiol. 2002 Jul;9(1):P215-6. PMID: 15002553.
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Purification and characterization of actin from maize pollen.

Plant physiology

Liu X, Yen LF.
PMID: 16668982
Plant Physiol. 1992 Jul;99(3):1151-5. doi: 10.1104/pp.99.3.1151.

Pollen is an excellent source of actin for biochemical and physiological studies of the actomyosin system in higher plants. We have developed an efficient method to prepare relatively high levels of actin from the pollen of maize (Zea mays...

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Liu X, Yen LF. Purification and characterization of actin from maize pollen. Plant Physiol. 1992;99(3):1151-5doi: 10.1104/pp.99.3.1151.
Liu, X., & Yen, L. F. (1992). Purification and characterization of actin from maize pollen. Plant physiology, 99(3), 1151-5. https://doi.org/10.1104/pp.99.3.1151
Liu, X, and Yen, L F. "Purification and characterization of actin from maize pollen." Plant physiology vol. 99,3 (1992): 1151-5. doi: https://doi.org/10.1104/pp.99.3.1151
Liu X, Yen LF. Purification and characterization of actin from maize pollen. Plant Physiol. 1992 Jul;99(3):1151-5. doi: 10.1104/pp.99.3.1151. PMID: 16668982; PMCID: PMC1080596.
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Cell signalling and motility in Entamoeba histolytica.

Parasitology today (Personal ed.)

Guillén N.
PMID: 15463670
Parasitol Today. 1993 Oct;9(10):364-9. doi: 10.1016/0169-4758(93)90084-s.

Entamoeba histolytica crawls as a polarized cell following external stimuli, with the translocation of signals modifying extracellular matrix interactions and the amoeba cytoskeleton. Nancy Guillén here describes how the gliding of E. histolytica cells requires the activity of the...

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Guillén N. Cell signalling and motility in Entamoeba histolytica. Parasitol Today. 1993;9(10):364-9doi: 10.1016/0169-4758(93)90084-s.
Guillén, N. (1993). Cell signalling and motility in Entamoeba histolytica. Parasitology today (Personal ed.), 9(10), 364-9. https://doi.org/10.1016/0169-4758(93)90084-s
Guillén, N. "Cell signalling and motility in Entamoeba histolytica." Parasitology today (Personal ed.) vol. 9,10 (1993): 364-9. doi: https://doi.org/10.1016/0169-4758(93)90084-s
Guillén N. Cell signalling and motility in Entamoeba histolytica. Parasitol Today. 1993 Oct;9(10):364-9. doi: 10.1016/0169-4758(93)90084-s. PMID: 15463670.
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Properties of Mitochondrial Contractile Protein and Actomyosin of Heart Muscle.

Science (New York, N.Y.)

Blair PV, Perdue JF, Green DE.
PMID: 17836364
Science. 1964 May 01;144(3618):560. doi: 10.1126/science.144.3618.560.

No abstract available.

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Blair PV, Perdue JF, Green DE. Properties of Mitochondrial Contractile Protein and Actomyosin of Heart Muscle. Science. 1964;144(3618):560doi: 10.1126/science.144.3618.560.
Blair, P. V., Perdue, J. F., & Green, D. E. (1964). Properties of Mitochondrial Contractile Protein and Actomyosin of Heart Muscle. Science (New York, N.Y.), 144(3618), 560. https://doi.org/10.1126/science.144.3618.560
Blair, P V, et al. "Properties of Mitochondrial Contractile Protein and Actomyosin of Heart Muscle." Science (New York, N.Y.) vol. 144,3618 (1964): 560. doi: https://doi.org/10.1126/science.144.3618.560
Blair PV, Perdue JF, Green DE. Properties of Mitochondrial Contractile Protein and Actomyosin of Heart Muscle. Science. 1964 May 01;144(3618):560. doi: 10.1126/science.144.3618.560. PMID: 17836364.
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Eye muscles of the pike (Esox lucius) fiber types and their actomyosin ATPase and SDH activity.

Tissue & cell

Zawadowska B.
PMID: 18621180
Tissue Cell. 1991;23(5):657-64. doi: 10.1016/0040-8166(91)90021-k.

The eye muscles of the pike are organized in two distinct populations of fibers arranged in semicircular layers. The distal layer, consisting of small diameter muscle fibers, is mainly made up of type I and tonic (slow) fibers. The...

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Zawadowska B. Eye muscles of the pike (Esox lucius) fiber types and their actomyosin ATPase and SDH activity. Tissue Cell. 1991;23(5):657-64doi: 10.1016/0040-8166(91)90021-k.
Zawadowska, B. (1991). Eye muscles of the pike (Esox lucius) fiber types and their actomyosin ATPase and SDH activity. Tissue & cell, 23(5), 657-64. https://doi.org/10.1016/0040-8166(91)90021-k
Zawadowska, B. "Eye muscles of the pike (Esox lucius) fiber types and their actomyosin ATPase and SDH activity." Tissue & cell vol. 23,5 (1991): 657-64. doi: https://doi.org/10.1016/0040-8166(91)90021-k
Zawadowska B. Eye muscles of the pike (Esox lucius) fiber types and their actomyosin ATPase and SDH activity. Tissue Cell. 1991;23(5):657-64. doi: 10.1016/0040-8166(91)90021-k. PMID: 18621180.
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Showing 1 to 12 of 443 entries