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Showing 1 to 12 of 82 entries
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Rac1 GTPase controls myelination and demyelination.

Bioarchitecture

Park HT, Feltri ML.
PMID: 21922040
Bioarchitecture. 2011 May;1(3):110-113. doi: 10.4161/bioa.1.3.16985.

After peripheral nerve injuries, Wallerian degeneration starts with a stereotypic fragmentation of myelin sheath into myelin ovoids, which occur near Schmidt-Lantermann incisures (SLI). This demyelination process requires a dramatic change in cytoskeletal structures in Schwann cells. We have recently...

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Park HT, Feltri ML. Rac1 GTPase controls myelination and demyelination. Bioarchitecture. 2011;1(3):110-113doi: 10.4161/bioa.1.3.16985.
Park, H. T., & Feltri, M. L. (2011). Rac1 GTPase controls myelination and demyelination. Bioarchitecture, 1(3), 110-113. https://doi.org/10.4161/bioa.1.3.16985
Park, Hwan Tae, and Feltri, M Laura. "Rac1 GTPase controls myelination and demyelination." Bioarchitecture vol. 1,3 (2011): 110-113. doi: https://doi.org/10.4161/bioa.1.3.16985
Park HT, Feltri ML. Rac1 GTPase controls myelination and demyelination. Bioarchitecture. 2011 May;1(3):110-113. doi: 10.4161/bioa.1.3.16985. PMID: 21922040; PMCID: PMC3173960.
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Control of cortical microtubule organization and desmosome stability by centrosomal proteins.

Bioarchitecture

Sumigray KD, Lechler T.
PMID: 22754612
Bioarchitecture. 2011 Sep 01;1(5):221-224. doi: 10.4161/bioa.18403.

In many tissues microtubules reorganize into non-centrosomal arrays in differentiated cells. In the epidermis, proliferative basal cells have a radial array of microtubules organized around a centrosome, while differentiated cells have cortical microtubules. The desmosomal protein desmoplakin is required...

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Sumigray KD, Lechler T. Control of cortical microtubule organization and desmosome stability by centrosomal proteins. Bioarchitecture. 2011;1(5):221-224doi: 10.4161/bioa.18403.
Sumigray, K. D., & Lechler, T. (2011). Control of cortical microtubule organization and desmosome stability by centrosomal proteins. Bioarchitecture, 1(5), 221-224. https://doi.org/10.4161/bioa.18403
Sumigray, Kaelyn D, and Lechler, Terry. "Control of cortical microtubule organization and desmosome stability by centrosomal proteins." Bioarchitecture vol. 1,5 (2011): 221-224. doi: https://doi.org/10.4161/bioa.18403
Sumigray KD, Lechler T. Control of cortical microtubule organization and desmosome stability by centrosomal proteins. Bioarchitecture. 2011 Sep 01;1(5):221-224. doi: 10.4161/bioa.18403. PMID: 22754612; PMCID: PMC3384573.
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Structural implications of conserved aspartate residues located in tropomyosin's coiled-coil core.

Bioarchitecture

Moore JR, Li X, Nirody J, Fischer S, Lehman W.
PMID: 22754618
Bioarchitecture. 2011 Sep 01;1(5):250-255. doi: 10.4161/bioa.18117.

Polar residues lying between adjacent α-helical chains of coiled-coils often contribute to coiled-coil curvature and flexibility, while more typical core hydrophobic residues anneal the chains together. In tropomyosins, ranging from smooth and skeletal muscle to cytoplasmic isoforms, a highly...

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Moore JR, Li X, Nirody J, et al. Structural implications of conserved aspartate residues located in tropomyosin's coiled-coil core. Bioarchitecture. 2011;1(5):250-255doi: 10.4161/bioa.18117.
Moore, J. R., Li, X., Nirody, J., Fischer, S., & Lehman, W. (2011). Structural implications of conserved aspartate residues located in tropomyosin's coiled-coil core. Bioarchitecture, 1(5), 250-255. https://doi.org/10.4161/bioa.18117
Moore, Jeffrey R, et al. "Structural implications of conserved aspartate residues located in tropomyosin's coiled-coil core." Bioarchitecture vol. 1,5 (2011): 250-255. doi: https://doi.org/10.4161/bioa.18117
Moore JR, Li X, Nirody J, Fischer S, Lehman W. Structural implications of conserved aspartate residues located in tropomyosin's coiled-coil core. Bioarchitecture. 2011 Sep 01;1(5):250-255. doi: 10.4161/bioa.18117. PMID: 22754618; PMCID: PMC3384579.
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Nucleosome assembly and genome integrity: The fork is the link.

Bioarchitecture

Prado F, Clemente-Ruiz M.
PMID: 22754621
Bioarchitecture. 2012 Jan 01;2(1):6-10. doi: 10.4161/bioa.19737.

Maintaining the stability of the replication forks is one of the main tasks of the DNA damage response. Specifically, checkpoint mechanisms detect stressed forks and prevent their collapse. In the published report reviewed here we have shown that defective...

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Prado F, Clemente-Ruiz M. Nucleosome assembly and genome integrity: The fork is the link. Bioarchitecture. 2012;2(1):6-10doi: 10.4161/bioa.19737.
Prado, F., & Clemente-Ruiz, M. (2012). Nucleosome assembly and genome integrity: The fork is the link. Bioarchitecture, 2(1), 6-10. https://doi.org/10.4161/bioa.19737
Prado, Félix, and Clemente-Ruiz, Marta. "Nucleosome assembly and genome integrity: The fork is the link." Bioarchitecture vol. 2,1 (2012): 6-10. doi: https://doi.org/10.4161/bioa.19737
Prado F, Clemente-Ruiz M. Nucleosome assembly and genome integrity: The fork is the link. Bioarchitecture. 2012 Jan 01;2(1):6-10. doi: 10.4161/bioa.19737. PMID: 22754621; PMCID: PMC3383716.
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A new role of multi scaffold protein Liprin-α: Liprin-α suppresses Rho-mDia mediated stress fiber formation.

Bioarchitecture

Sakamoto S, Narumiya S, Ishizaki T.
PMID: 22754629
Bioarchitecture. 2012 Feb 01;2(2):43-49. doi: 10.4161/bioa.20442.

Regulation of the actin cytoskeleton is crucial for cell morphology and migration. One of the key molecules that regulates actin remodeling is the small GTPase Rho. Rho shuttles between the inactive GDP-bound form and the active GTP-bound form, and...

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Sakamoto S, Narumiya S, Ishizaki T. A new role of multi scaffold protein Liprin-α: Liprin-α suppresses Rho-mDia mediated stress fiber formation. Bioarchitecture. 2012;2(2):43-49doi: 10.4161/bioa.20442.
Sakamoto, S., Narumiya, S., & Ishizaki, T. (2012). A new role of multi scaffold protein Liprin-α: Liprin-α suppresses Rho-mDia mediated stress fiber formation. Bioarchitecture, 2(2), 43-49. https://doi.org/10.4161/bioa.20442
Sakamoto, Satoko, et al. "A new role of multi scaffold protein Liprin-α: Liprin-α suppresses Rho-mDia mediated stress fiber formation." Bioarchitecture vol. 2,2 (2012): 43-49. doi: https://doi.org/10.4161/bioa.20442
Sakamoto S, Narumiya S, Ishizaki T. A new role of multi scaffold protein Liprin-α: Liprin-α suppresses Rho-mDia mediated stress fiber formation. Bioarchitecture. 2012 Feb 01;2(2):43-49. doi: 10.4161/bioa.20442. PMID: 22754629; PMCID: PMC3383721.
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Cortical actin dynamics: Generating randomness by formin(g) and moving.

Bioarchitecture

Yu H, Wedlich-Söldner R.
PMID: 22069508
Bioarchitecture. 2011 Jul;1(4):165-168. doi: 10.4161/bioa.1.4.17314. Epub 2011 Jul 01.

The actin cytoskeleton plays essential roles in cell polarization and cell morphogenesis of the budding yeast Saccharomyces cerevisiae. Yeast cells utilize formin-generated actin cables as tracks for polarized transport, which forms the basis for a positive feedback loop driving...

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Yu H, Wedlich-Söldner R. Cortical actin dynamics: Generating randomness by formin(g) and moving. Bioarchitecture. 2011;1(4):165-168doi: 10.4161/bioa.1.4.17314.
Yu, H., & Wedlich-Söldner, R. (2011). Cortical actin dynamics: Generating randomness by formin(g) and moving. Bioarchitecture, 1(4), 165-168. https://doi.org/10.4161/bioa.1.4.17314
Yu, Haochen, and Wedlich-Söldner, Roland. "Cortical actin dynamics: Generating randomness by formin(g) and moving." Bioarchitecture vol. 1,4 (2011): 165-168. doi: https://doi.org/10.4161/bioa.1.4.17314
Yu H, Wedlich-Söldner R. Cortical actin dynamics: Generating randomness by formin(g) and moving. Bioarchitecture. 2011 Jul;1(4):165-168. doi: 10.4161/bioa.1.4.17314. Epub 2011 Jul 01. PMID: 22069508; PMCID: PMC3210520.
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Lymphocyte polarity, the immunological synapse and the scope of biological analogy.

Bioarchitecture

Huse M.
PMID: 22069511
Bioarchitecture. 2011 Jul;1(4):180-185. doi: 10.4161/bioa.1.4.17594. Epub 2011 Jul 01.

Lymphocytes such as T cells, B cells and natural killer (NK) cells form specialized contacts, called immunological synapses, with other cells in order to engage in specific intercellular communication and killing. Synapse formation is associated with the polarization of...

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Huse M. Lymphocyte polarity, the immunological synapse and the scope of biological analogy. Bioarchitecture. 2011;1(4):180-185doi: 10.4161/bioa.1.4.17594.
Huse, M. (2011). Lymphocyte polarity, the immunological synapse and the scope of biological analogy. Bioarchitecture, 1(4), 180-185. https://doi.org/10.4161/bioa.1.4.17594
Huse, Morgan. "Lymphocyte polarity, the immunological synapse and the scope of biological analogy." Bioarchitecture vol. 1,4 (2011): 180-185. doi: https://doi.org/10.4161/bioa.1.4.17594
Huse M. Lymphocyte polarity, the immunological synapse and the scope of biological analogy. Bioarchitecture. 2011 Jul;1(4):180-185. doi: 10.4161/bioa.1.4.17594. Epub 2011 Jul 01. PMID: 22069511; PMCID: PMC3210514.
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Nuclear actin-related proteins take shape.

Bioarchitecture

Fenn S, Gerhold CB, Hopfner KP.
PMID: 22069513
Bioarchitecture. 2011 Jul;1(4):192-195. doi: 10.4161/bioa.1.4.17643. Epub 2011 Jul 01.

The function of nuclear actin is poorly understood. It is known to be a discrete component of several chromatin-modifying complexes. Nevertheless, filamentous forms of actin are important for various nuclear processes as well. Nuclear actin is often associated with...

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Fenn S, Gerhold CB, Hopfner KP. Nuclear actin-related proteins take shape. Bioarchitecture. 2011;1(4):192-195doi: 10.4161/bioa.1.4.17643.
Fenn, S., Gerhold, C. B., & Hopfner, K. P. (2011). Nuclear actin-related proteins take shape. Bioarchitecture, 1(4), 192-195. https://doi.org/10.4161/bioa.1.4.17643
Fenn, Sebastian, et al. "Nuclear actin-related proteins take shape." Bioarchitecture vol. 1,4 (2011): 192-195. doi: https://doi.org/10.4161/bioa.1.4.17643
Fenn S, Gerhold CB, Hopfner KP. Nuclear actin-related proteins take shape. Bioarchitecture. 2011 Jul;1(4):192-195. doi: 10.4161/bioa.1.4.17643. Epub 2011 Jul 01. PMID: 22069513; PMCID: PMC3210522.
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Further insights into cortactin conformational regulation.

Bioarchitecture

Evans JV, Kelley LC, Hayes KE, Ammer AG, Martin KH, Weed SA.
PMID: 21866257
Bioarchitecture. 2011 Jan;1(1):21-23. doi: 10.4161/bioa.1.1.14631.

The actin regulatory protein cortactin is involved in multiple signaling pathways impinging on the cortical actin cytoskeleton. Cortactin is phosphorylated by ERK1/2 and Src family tyrosine kinases, resulting in neuronal Wiskott Aldrich Syndrome protein (N-WASp) activation and enhanced actin...

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Evans JV, Kelley LC, Hayes KE, et al. Further insights into cortactin conformational regulation. Bioarchitecture. 2011;1(1):21-23doi: 10.4161/bioa.1.1.14631.
Evans, J. V., Kelley, L. C., Hayes, K. E., Ammer, A. G., Martin, K. H., & Weed, S. A. (2011). Further insights into cortactin conformational regulation. Bioarchitecture, 1(1), 21-23. https://doi.org/10.4161/bioa.1.1.14631
Evans, Jason V, et al. "Further insights into cortactin conformational regulation." Bioarchitecture vol. 1,1 (2011): 21-23. doi: https://doi.org/10.4161/bioa.1.1.14631
Evans JV, Kelley LC, Hayes KE, Ammer AG, Martin KH, Weed SA. Further insights into cortactin conformational regulation. Bioarchitecture. 2011 Jan;1(1):21-23. doi: 10.4161/bioa.1.1.14631. PMID: 21866257; PMCID: PMC3158636.
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Nanoscopy of cell architecture: The actin-membrane interface.

Bioarchitecture

Ahmed S.
PMID: 21866260
Bioarchitecture. 2011 Jan;1(1):32-38. doi: 10.4161/bioa.1.1.14799.

It was light microscopy that first revealed the hidden world of bacteria and the unit of life the "cell." From these first observations, made in the late 1600s, it has been clear that seeing is an important tool in...

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Ahmed S. Nanoscopy of cell architecture: The actin-membrane interface. Bioarchitecture. 2011;1(1):32-38doi: 10.4161/bioa.1.1.14799.
Ahmed, S. (2011). Nanoscopy of cell architecture: The actin-membrane interface. Bioarchitecture, 1(1), 32-38. https://doi.org/10.4161/bioa.1.1.14799
Ahmed, Sohail. "Nanoscopy of cell architecture: The actin-membrane interface." Bioarchitecture vol. 1,1 (2011): 32-38. doi: https://doi.org/10.4161/bioa.1.1.14799
Ahmed S. Nanoscopy of cell architecture: The actin-membrane interface. Bioarchitecture. 2011 Jan;1(1):32-38. doi: 10.4161/bioa.1.1.14799. PMID: 21866260; PMCID: PMC3158633.
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ESCRT proteins: Double-edged regulators of cellular signaling.

Bioarchitecture

Tu C, Ahmad G, Mohapatra B, Bhattacharyya S, Ortega-Cava CF, Chung BM, Wagner KU, Raja SM, Naramura M, Band V, Band H.
PMID: 21866262
Bioarchitecture. 2011 Jan;1(1):45-48. doi: 10.4161/bioa.1.1.15173.

ESCRT pathway proteins play a key role in sorting ubiquitinated membrane receptors towards lysosomes providing an important mechanism for attenuating cell surface receptor signaling. However, recent studies point to a positive role of ESCRT proteins in signal transduction in...

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Tu C, Ahmad G, Mohapatra B, et al. ESCRT proteins: Double-edged regulators of cellular signaling. Bioarchitecture. 2011;1(1):45-48doi: 10.4161/bioa.1.1.15173.
Tu, C., Ahmad, G., Mohapatra, B., Bhattacharyya, S., Ortega-Cava, C. F., Chung, B. M., Wagner, K. U., Raja, S. M., Naramura, M., Band, V., & Band, H. (2011). ESCRT proteins: Double-edged regulators of cellular signaling. Bioarchitecture, 1(1), 45-48. https://doi.org/10.4161/bioa.1.1.15173
Tu, Chun, et al. "ESCRT proteins: Double-edged regulators of cellular signaling." Bioarchitecture vol. 1,1 (2011): 45-48. doi: https://doi.org/10.4161/bioa.1.1.15173
Tu C, Ahmad G, Mohapatra B, Bhattacharyya S, Ortega-Cava CF, Chung BM, Wagner KU, Raja SM, Naramura M, Band V, Band H. ESCRT proteins: Double-edged regulators of cellular signaling. Bioarchitecture. 2011 Jan;1(1):45-48. doi: 10.4161/bioa.1.1.15173. PMID: 21866262; PMCID: PMC3158637.
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Pulling it together: The mitotic function of TACC3.

Bioarchitecture

Hood FE, Royle SJ.
PMID: 21922039
Bioarchitecture. 2011 May;1(3):105-109. doi: 10.4161/bioa.1.3.16518.

Transforming acidic coiled coil 3 (TACC3) is a non-motor microtubule-associated protein (MAP) that is important for mitotic spindle stability and organization. The exact mechanism by which TACC3 acts at microtubules to stabilize the spindle has been unclear. However, several...

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Hood FE, Royle SJ. Pulling it together: The mitotic function of TACC3. Bioarchitecture. 2011;1(3):105-109doi: 10.4161/bioa.1.3.16518.
Hood, F. E., & Royle, S. J. (2011). Pulling it together: The mitotic function of TACC3. Bioarchitecture, 1(3), 105-109. https://doi.org/10.4161/bioa.1.3.16518
Hood, Fiona E, and Royle, Stephen J. "Pulling it together: The mitotic function of TACC3." Bioarchitecture vol. 1,3 (2011): 105-109. doi: https://doi.org/10.4161/bioa.1.3.16518
Hood FE, Royle SJ. Pulling it together: The mitotic function of TACC3. Bioarchitecture. 2011 May;1(3):105-109. doi: 10.4161/bioa.1.3.16518. PMID: 21922039; PMCID: PMC3173962.
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Showing 1 to 12 of 82 entries