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The formation of ordered nanoclusters controls cadherin anchoring to actin and cell-cell contact fluidity.

The Journal of cell biology

Strale PO, Duchesne L, Peyret G, Montel L, Nguyen T, Png E, Tampé R, Troyanovsky S, Hénon S, Ladoux B, Mège RM.
PMID: 26370504
J Cell Biol. 2015 Sep 14;210(6):1033. doi: 10.1083/jcb.20141011109022015c.

No abstract available.

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Strale PO, Duchesne L, Peyret G, et al. The formation of ordered nanoclusters controls cadherin anchoring to actin and cell-cell contact fluidity. J Cell Biol. 2015;210(6):1033doi: 10.1083/jcb.20141011109022015c.
Strale, P. O., Duchesne, L., Peyret, G., Montel, L., Nguyen, T., Png, E., Tampé, R., Troyanovsky, S., Hénon, S., Ladoux, B., & Mège, R. M. (2015). The formation of ordered nanoclusters controls cadherin anchoring to actin and cell-cell contact fluidity. The Journal of cell biology, 210(6), 1033. https://doi.org/10.1083/jcb.20141011109022015c
Strale, Pierre-Olivier, et al. "The formation of ordered nanoclusters controls cadherin anchoring to actin and cell-cell contact fluidity." The Journal of cell biology vol. 210,6 (2015): 1033. doi: https://doi.org/10.1083/jcb.20141011109022015c
Strale PO, Duchesne L, Peyret G, Montel L, Nguyen T, Png E, Tampé R, Troyanovsky S, Hénon S, Ladoux B, Mège RM. The formation of ordered nanoclusters controls cadherin anchoring to actin and cell-cell contact fluidity. J Cell Biol. 2015 Sep 14;210(6):1033. doi: 10.1083/jcb.20141011109022015c. PMID: 26370504; PMCID: PMC4576855.
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Rme-8 depletion perturbs Notch recycling and predisposes to pathogenic signaling.

The Journal of cell biology

Gomez-Lamarca M, Snowdon LA, Seib E, Klein T, Bray S.
PMID: 26240186
J Cell Biol. 2015 Aug 03;210(3):517. doi: 10.1083/jcb.20141100107172015c.

No abstract available.

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Gomez-Lamarca M, Snowdon LA, Seib E, et al. Rme-8 depletion perturbs Notch recycling and predisposes to pathogenic signaling. J Cell Biol. 2015;210(3):517doi: 10.1083/jcb.20141100107172015c.
Gomez-Lamarca, M., Snowdon, L. A., Seib, E., Klein, T., & Bray, S. (2015). Rme-8 depletion perturbs Notch recycling and predisposes to pathogenic signaling. The Journal of cell biology, 210(3), 517. https://doi.org/10.1083/jcb.20141100107172015c
Gomez-Lamarca, Maria, et al. "Rme-8 depletion perturbs Notch recycling and predisposes to pathogenic signaling." The Journal of cell biology vol. 210,3 (2015): 517. doi: https://doi.org/10.1083/jcb.20141100107172015c
Gomez-Lamarca M, Snowdon LA, Seib E, Klein T, Bray S. Rme-8 depletion perturbs Notch recycling and predisposes to pathogenic signaling. J Cell Biol. 2015 Aug 03;210(3):517. doi: 10.1083/jcb.20141100107172015c. PMID: 26240186; PMCID: PMC4523613.
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A network of assembly factors is involved in remodeling rRNA elements during preribosome maturation.

The Journal of cell biology

Baßler J, Paternoga H, Holdermann I, Thoms M, Granneman S, Barrio-Garcia C, Nyarko A, Lee W, Stier G, Clark SA, Schraivogel D, Kallas M, Beckmann R, Tollervey D, Barbar E, Sinning I, Hurt E.
PMID: 26150393
J Cell Biol. 2015 Jul 06;210(1):169-70. doi: 10.1083/jcb.20140811106112015c.

No abstract available.

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Baßler J, Paternoga H, Holdermann I, et al. A network of assembly factors is involved in remodeling rRNA elements during preribosome maturation. J Cell Biol. 2015;210(1):169-70doi: 10.1083/jcb.20140811106112015c.
Baßler, J., Paternoga, H., Holdermann, I., Thoms, M., Granneman, S., Barrio-Garcia, C., Nyarko, A., Lee, W., Stier, G., Clark, S. A., Schraivogel, D., Kallas, M., Beckmann, R., Tollervey, D., Barbar, E., Sinning, I., & Hurt, E. (2015). A network of assembly factors is involved in remodeling rRNA elements during preribosome maturation. The Journal of cell biology, 210(1), 169-70. https://doi.org/10.1083/jcb.20140811106112015c
Baßler, Jochen, et al. "A network of assembly factors is involved in remodeling rRNA elements during preribosome maturation." The Journal of cell biology vol. 210,1 (2015): 169-70. doi: https://doi.org/10.1083/jcb.20140811106112015c
Baßler J, Paternoga H, Holdermann I, Thoms M, Granneman S, Barrio-Garcia C, Nyarko A, Lee W, Stier G, Clark SA, Schraivogel D, Kallas M, Beckmann R, Tollervey D, Barbar E, Sinning I, Hurt E. A network of assembly factors is involved in remodeling rRNA elements during preribosome maturation. J Cell Biol. 2015 Jul 06;210(1):169-70. doi: 10.1083/jcb.20140811106112015c. PMID: 26150393; PMCID: PMC4494009.
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Prions Ex Vivo: What Cell Culture Models Tell Us about Infectious Proteins.

International journal of cell biology

Krauss S, Vorberg I.
PMID: 24282413
Int J Cell Biol. 2013;2013:704546. doi: 10.1155/2013/704546. Epub 2013 Oct 26.

Prions are unconventional infectious agents that are composed of misfolded aggregated prion protein. Prions replicate their conformation by template-assisted conversion of the endogenous prion protein PrP. Templated conversion of soluble proteins into protein aggregates is also a hallmark of...

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Krauss S, Vorberg I. Prions Ex Vivo: What Cell Culture Models Tell Us about Infectious Proteins. Int J Cell Biol. 2013;2013:704546doi: 10.1155/2013/704546.
Krauss, S., & Vorberg, I. (2013). Prions Ex Vivo: What Cell Culture Models Tell Us about Infectious Proteins. International journal of cell biology, 2013704546. https://doi.org/10.1155/2013/704546
Krauss, Sybille, and Vorberg, Ina. "Prions Ex Vivo: What Cell Culture Models Tell Us about Infectious Proteins." International journal of cell biology vol. 2013 (2013): 704546. doi: https://doi.org/10.1155/2013/704546
Krauss S, Vorberg I. Prions Ex Vivo: What Cell Culture Models Tell Us about Infectious Proteins. Int J Cell Biol. 2013;2013:704546. doi: 10.1155/2013/704546. Epub 2013 Oct 26. PMID: 24282413; PMCID: PMC3825132.
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Changes in the Distribution of the α 3 Na(+)/K(+) ATPase Subunit in Heterozygous Lurcher Purkinje Cells as a Genetic Model of Chronic Depolarization during Development.

International journal of cell biology

McFarland R, Zanjani HS, Mariani J, Vogel MW.
PMID: 24719618
Int J Cell Biol. 2014;2014:152645. doi: 10.1155/2014/152645. Epub 2014 Feb 27.

A common assumption of excitotoxic mechanisms in the nervous system is that the ionic imbalance resulting from overstimulation of glutamate receptors and increased Na(+) and Ca(++) influx overwhelms cellular energy metabolic systems leading to cell death. The goal of...

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McFarland R, Zanjani HS, Mariani J, et al. Changes in the Distribution of the α 3 Na(+)/K(+) ATPase Subunit in Heterozygous Lurcher Purkinje Cells as a Genetic Model of Chronic Depolarization during Development. Int J Cell Biol. 2014;2014:152645doi: 10.1155/2014/152645.
McFarland, R., Zanjani, H. S., Mariani, J., & Vogel, M. W. (2014). Changes in the Distribution of the α 3 Na(+)/K(+) ATPase Subunit in Heterozygous Lurcher Purkinje Cells as a Genetic Model of Chronic Depolarization during Development. International journal of cell biology, 2014152645. https://doi.org/10.1155/2014/152645
McFarland, Rebecca, et al. "Changes in the Distribution of the α 3 Na(+)/K(+) ATPase Subunit in Heterozygous Lurcher Purkinje Cells as a Genetic Model of Chronic Depolarization during Development." International journal of cell biology vol. 2014 (2014): 152645. doi: https://doi.org/10.1155/2014/152645
McFarland R, Zanjani HS, Mariani J, Vogel MW. Changes in the Distribution of the α 3 Na(+)/K(+) ATPase Subunit in Heterozygous Lurcher Purkinje Cells as a Genetic Model of Chronic Depolarization during Development. Int J Cell Biol. 2014;2014:152645. doi: 10.1155/2014/152645. Epub 2014 Feb 27. PMID: 24719618; PMCID: PMC3955620.
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Quantifying Changes in the Cellular Thiol-Disulfide Status during Differentiation of B Cells into Antibody-Secreting Plasma Cells.

International journal of cell biology

Hansen RE, Otsu M, Braakman I, Winther JR.
PMID: 24223594
Int J Cell Biol. 2013;2013:898563. doi: 10.1155/2013/898563. Epub 2013 Sep 24.

Plasma cells produce and secrete massive amounts of disulfide-containing antibodies. To accommodate this load on the secretory machinery, the differentiation of resting B cells into antibody-secreting plasma cells is accompanied by a preferential expansion of the secretory compartments of...

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Hansen RE, Otsu M, Braakman I, et al. Quantifying Changes in the Cellular Thiol-Disulfide Status during Differentiation of B Cells into Antibody-Secreting Plasma Cells. Int J Cell Biol. 2013;2013:898563doi: 10.1155/2013/898563.
Hansen, R. E., Otsu, M., Braakman, I., & Winther, J. R. (2013). Quantifying Changes in the Cellular Thiol-Disulfide Status during Differentiation of B Cells into Antibody-Secreting Plasma Cells. International journal of cell biology, 2013898563. https://doi.org/10.1155/2013/898563
Hansen, Rosa E, et al. "Quantifying Changes in the Cellular Thiol-Disulfide Status during Differentiation of B Cells into Antibody-Secreting Plasma Cells." International journal of cell biology vol. 2013 (2013): 898563. doi: https://doi.org/10.1155/2013/898563
Hansen RE, Otsu M, Braakman I, Winther JR. Quantifying Changes in the Cellular Thiol-Disulfide Status during Differentiation of B Cells into Antibody-Secreting Plasma Cells. Int J Cell Biol. 2013;2013:898563. doi: 10.1155/2013/898563. Epub 2013 Sep 24. PMID: 24223594; PMCID: PMC3800581.
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The role of s-nitrosylation and s-glutathionylation of protein disulphide isomerase in protein misfolding and neurodegeneration.

International journal of cell biology

Halloran M, Parakh S, Atkin JD.
PMID: 24348565
Int J Cell Biol. 2013;2013:797914. doi: 10.1155/2013/797914. Epub 2013 Nov 18.

Neurodegenerative diseases involve the progressive loss of neurons, and a pathological hallmark is the presence of abnormal inclusions containing misfolded proteins. Although the precise molecular mechanisms triggering neurodegeneration remain unclear, endoplasmic reticulum (ER) stress, elevated oxidative and nitrosative stress,...

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Halloran M, Parakh S, Atkin JD. The role of s-nitrosylation and s-glutathionylation of protein disulphide isomerase in protein misfolding and neurodegeneration. Int J Cell Biol. 2013;2013:797914doi: 10.1155/2013/797914.
Halloran, M., Parakh, S., & Atkin, J. D. (2013). The role of s-nitrosylation and s-glutathionylation of protein disulphide isomerase in protein misfolding and neurodegeneration. International journal of cell biology, 2013797914. https://doi.org/10.1155/2013/797914
Halloran, M, et al. "The role of s-nitrosylation and s-glutathionylation of protein disulphide isomerase in protein misfolding and neurodegeneration." International journal of cell biology vol. 2013 (2013): 797914. doi: https://doi.org/10.1155/2013/797914
Halloran M, Parakh S, Atkin JD. The role of s-nitrosylation and s-glutathionylation of protein disulphide isomerase in protein misfolding and neurodegeneration. Int J Cell Biol. 2013;2013:797914. doi: 10.1155/2013/797914. Epub 2013 Nov 18. PMID: 24348565; PMCID: PMC3852308.
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Correction: Stoichiometry of Nck-dependent actin polymerization in living cells.

The Journal of cell biology

Ditlev JA, Michalski PJ, Huber G, Rivera GM, Mohler WA, Loew LM, Mayer BJ.
PMID: 26644519
J Cell Biol. 2015 Dec 07;211(5):1095-8. doi: 10.1083/jcb.20111111311232015c.

No abstract available.

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Ditlev JA, Michalski PJ, Huber G, et al. Correction: Stoichiometry of Nck-dependent actin polymerization in living cells. J Cell Biol. 2015;211(5):1095-8doi: 10.1083/jcb.20111111311232015c.
Ditlev, J. A., Michalski, P. J., Huber, G., Rivera, G. M., Mohler, W. A., Loew, L. M., & Mayer, B. J. (2015). Correction: Stoichiometry of Nck-dependent actin polymerization in living cells. The Journal of cell biology, 211(5), 1095-8. https://doi.org/10.1083/jcb.20111111311232015c
Ditlev, Jonathon A, et al. "Correction: Stoichiometry of Nck-dependent actin polymerization in living cells." The Journal of cell biology vol. 211,5 (2015): 1095-8. doi: https://doi.org/10.1083/jcb.20111111311232015c
Ditlev JA, Michalski PJ, Huber G, Rivera GM, Mohler WA, Loew LM, Mayer BJ. Correction: Stoichiometry of Nck-dependent actin polymerization in living cells. J Cell Biol. 2015 Dec 07;211(5):1095-8. doi: 10.1083/jcb.20111111311232015c. PMID: 26644519; PMCID: PMC4674272.
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Alternative splicing: role in cancer development and progression.

International journal of cell biology

Sette C, Ladomery M, Ghigna C.
PMID: 24348561
Int J Cell Biol. 2013;2013:421606. doi: 10.1155/2013/421606. Epub 2013 Nov 20.

No abstract available.

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Sette C, Ladomery M, Ghigna C. Alternative splicing: role in cancer development and progression. Int J Cell Biol. 2013;2013:421606doi: 10.1155/2013/421606.
Sette, C., Ladomery, M., & Ghigna, C. (2013). Alternative splicing: role in cancer development and progression. International journal of cell biology, 2013421606. https://doi.org/10.1155/2013/421606
Sette, Claudio, et al. "Alternative splicing: role in cancer development and progression." International journal of cell biology vol. 2013 (2013): 421606. doi: https://doi.org/10.1155/2013/421606
Sette C, Ladomery M, Ghigna C. Alternative splicing: role in cancer development and progression. Int J Cell Biol. 2013;2013:421606. doi: 10.1155/2013/421606. Epub 2013 Nov 20. PMID: 24348561; PMCID: PMC3852956.
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The mitochondrial disulfide relay system: roles in oxidative protein folding and beyond.

International journal of cell biology

Fischer M, Riemer J.
PMID: 24348563
Int J Cell Biol. 2013;2013:742923. doi: 10.1155/2013/742923. Epub 2013 Nov 14.

Disulfide bond formation drives protein import of most proteins of the mitochondrial intermembrane space (IMS). The main components of this disulfide relay machinery are the oxidoreductase Mia40 and the sulfhydryl oxidase Erv1/ALR. Their precise functions have been elucidated in...

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Fischer M, Riemer J. The mitochondrial disulfide relay system: roles in oxidative protein folding and beyond. Int J Cell Biol. 2013;2013:742923doi: 10.1155/2013/742923.
Fischer, M., & Riemer, J. (2013). The mitochondrial disulfide relay system: roles in oxidative protein folding and beyond. International journal of cell biology, 2013742923. https://doi.org/10.1155/2013/742923
Fischer, Manuel, and Riemer, Jan. "The mitochondrial disulfide relay system: roles in oxidative protein folding and beyond." International journal of cell biology vol. 2013 (2013): 742923. doi: https://doi.org/10.1155/2013/742923
Fischer M, Riemer J. The mitochondrial disulfide relay system: roles in oxidative protein folding and beyond. Int J Cell Biol. 2013;2013:742923. doi: 10.1155/2013/742923. Epub 2013 Nov 14. PMID: 24348563; PMCID: PMC3848088.
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The Rise and Fall of Hyaluronan in Respiratory Diseases.

International journal of cell biology

Lauer ME, Dweik RA, Garantziotis S, Aronica MA.
PMID: 26448757
Int J Cell Biol. 2015;2015:712507. doi: 10.1155/2015/712507. Epub 2015 Sep 10.

In normal airways, hyaluronan (HA) matrices are primarily located within the airway submucosa, pulmonary vasculature walls, and, to a lesser extent, the alveoli. Following pulmonary injury, elevated levels of HA matrices accumulate in these regions, and in respiratory secretions,...

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Lauer ME, Dweik RA, Garantziotis S, et al. The Rise and Fall of Hyaluronan in Respiratory Diseases. Int J Cell Biol. 2015;2015:712507doi: 10.1155/2015/712507.
Lauer, M. E., Dweik, R. A., Garantziotis, S., & Aronica, M. A. (2015). The Rise and Fall of Hyaluronan in Respiratory Diseases. International journal of cell biology, 2015712507. https://doi.org/10.1155/2015/712507
Lauer, Mark E, et al. "The Rise and Fall of Hyaluronan in Respiratory Diseases." International journal of cell biology vol. 2015 (2015): 712507. doi: https://doi.org/10.1155/2015/712507
Lauer ME, Dweik RA, Garantziotis S, Aronica MA. The Rise and Fall of Hyaluronan in Respiratory Diseases. Int J Cell Biol. 2015;2015:712507. doi: 10.1155/2015/712507. Epub 2015 Sep 10. PMID: 26448757; PMCID: PMC4581576.
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Advances in Hyaluronan Biology: Signaling, Regulation, and Disease Mechanisms.

International journal of cell biology

Simpson MA, de la Motte C, Sherman LS, Weigel PH.
PMID: 26446415
Int J Cell Biol. 2015;2015:690572. doi: 10.1155/2015/690572. Epub 2015 Sep 13.

No abstract available.

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Simpson MA, de la Motte C, Sherman LS, et al. Advances in Hyaluronan Biology: Signaling, Regulation, and Disease Mechanisms. Int J Cell Biol. 2015;2015:690572doi: 10.1155/2015/690572.
Simpson, M. A., de la Motte, C., Sherman, L. S., & Weigel, P. H. (2015). Advances in Hyaluronan Biology: Signaling, Regulation, and Disease Mechanisms. International journal of cell biology, 2015690572. https://doi.org/10.1155/2015/690572
Simpson, Melanie A, et al. "Advances in Hyaluronan Biology: Signaling, Regulation, and Disease Mechanisms." International journal of cell biology vol. 2015 (2015): 690572. doi: https://doi.org/10.1155/2015/690572
Simpson MA, de la Motte C, Sherman LS, Weigel PH. Advances in Hyaluronan Biology: Signaling, Regulation, and Disease Mechanisms. Int J Cell Biol. 2015;2015:690572. doi: 10.1155/2015/690572. Epub 2015 Sep 13. PMID: 26446415; PMCID: PMC4584047.
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Showing 1 to 12 of 888 entries