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A survey of diamagnetic probes for copper2+ binding to the prion protein. 1H NMR solution structure of the palladium2+ bound single octarepeat.

Dalton transactions (Cambridge, England : 2003)

Garnett AP, Jones CE, Viles JH.
PMID: 16395451
Dalton Trans. 2006 Jan 21;(3):509-18. doi: 10.1039/b511553a. Epub 2005 Oct 27.

The prion protein (PrP(C)) is a copper binding cell surface glycoprotein which when misfolded causes transmissible spongiform encephalopathies. The cooperative binding of Cu2+ to an unstructured octarepeat sequence within PrP(C) causes profound folding of this region. The use of...

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Garnett AP, Jones CE, Viles JH. A survey of diamagnetic probes for copper2+ binding to the prion protein. 1H NMR solution structure of the palladium2+ bound single octarepeat. Dalton Trans. 2005;(3):509-18doi: 10.1039/b511553a.
Garnett, A. P., Jones, C. E., & Viles, J. H. (2006). A survey of diamagnetic probes for copper2+ binding to the prion protein. 1H NMR solution structure of the palladium2+ bound single octarepeat. Dalton transactions (Cambridge, England : 2003), (3), 509-18. https://doi.org/10.1039/b511553a
Garnett, Anthony P, et al. "A survey of diamagnetic probes for copper2+ binding to the prion protein. 1H NMR solution structure of the palladium2+ bound single octarepeat." Dalton transactions (Cambridge, England : 2003) vol. ,3 (2006): 509-18. doi: https://doi.org/10.1039/b511553a
Garnett AP, Jones CE, Viles JH. A survey of diamagnetic probes for copper2+ binding to the prion protein. 1H NMR solution structure of the palladium2+ bound single octarepeat. Dalton Trans. 2006 Jan 21;(3):509-18. doi: 10.1039/b511553a. Epub 2005 Oct 27. PMID: 16395451.
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Efficacy of Intraperitoneal Administration of PEGylated NELL-1 for Bone Formation.

BioResearch open access

Tanjaya J, Zhang Y, Lee S, Shi J, Chen E, Ang P, Zhang X, Tetradis S, Ting K, Wu B, Soo C, Kwak JH.
PMID: 27354930
Biores Open Access. 2016 Jun 01;5(1):159-70. doi: 10.1089/biores.2016.0018. eCollection 2016.

Systemically delivered NEL-like molecule-1 (NELL-1), a potent pro-osteogenic protein, promotes bone formation in healthy and osteoporotic mouse models. PEGylation of NELL-1 (NELL-PEG) increases the half-life of the protein in a mouse model without compromising its osteogenic potential, thereby improving...

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Tanjaya J, Zhang Y, Lee S, et al. Efficacy of Intraperitoneal Administration of PEGylated NELL-1 for Bone Formation. Biores Open Access. 2016;5(1):159-70doi: 10.1089/biores.2016.0018.
Tanjaya, J., Zhang, Y., Lee, S., Shi, J., Chen, E., Ang, P., Zhang, X., Tetradis, S., Ting, K., Wu, B., Soo, C., & Kwak, J. H. (2016). Efficacy of Intraperitoneal Administration of PEGylated NELL-1 for Bone Formation. BioResearch open access, 5(1), 159-70. https://doi.org/10.1089/biores.2016.0018
Tanjaya, Justine, et al. "Efficacy of Intraperitoneal Administration of PEGylated NELL-1 for Bone Formation." BioResearch open access vol. 5,1 (2016): 159-70. doi: https://doi.org/10.1089/biores.2016.0018
Tanjaya J, Zhang Y, Lee S, Shi J, Chen E, Ang P, Zhang X, Tetradis S, Ting K, Wu B, Soo C, Kwak JH. Efficacy of Intraperitoneal Administration of PEGylated NELL-1 for Bone Formation. Biores Open Access. 2016 Jun 01;5(1):159-70. doi: 10.1089/biores.2016.0018. eCollection 2016. PMID: 27354930; PMCID: PMC4921932.
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Enzymatic production of mono-ubiquitinated proteins for structural studies: The example of the Josephin domain of ataxin-3.

FEBS open bio

Faggiano S, Menon RP, Kelly GP, McCormick J, Todi SV, Scaglione KM, Paulson HL, Pastore A.
PMID: 24251111
FEBS Open Bio. 2013 Oct 12;3:453-8. doi: 10.1016/j.fob.2013.10.005. eCollection 2013.

Protein ubiquitination occurs through formation of an isopeptide bond between the C-terminal glycine of ubiquitin (Ub) and the ɛ-amino group of a substrate lysine residue. This post-translational modification, which occurs through the attachment of single and/or multiple copies of...

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Faggiano S, Menon RP, Kelly GP, et al. Enzymatic production of mono-ubiquitinated proteins for structural studies: The example of the Josephin domain of ataxin-3. FEBS Open Bio. 2013;3:453-8doi: 10.1016/j.fob.2013.10.005.
Faggiano, S., Menon, R. P., Kelly, G. P., McCormick, J., Todi, S. V., Scaglione, K. M., Paulson, H. L., & Pastore, A. (2013). Enzymatic production of mono-ubiquitinated proteins for structural studies: The example of the Josephin domain of ataxin-3. FEBS open bio, 3453-8. https://doi.org/10.1016/j.fob.2013.10.005
Faggiano, Serena, et al. "Enzymatic production of mono-ubiquitinated proteins for structural studies: The example of the Josephin domain of ataxin-3." FEBS open bio vol. 3 (2013): 453-8. doi: https://doi.org/10.1016/j.fob.2013.10.005
Faggiano S, Menon RP, Kelly GP, McCormick J, Todi SV, Scaglione KM, Paulson HL, Pastore A. Enzymatic production of mono-ubiquitinated proteins for structural studies: The example of the Josephin domain of ataxin-3. FEBS Open Bio. 2013 Oct 12;3:453-8. doi: 10.1016/j.fob.2013.10.005. eCollection 2013. PMID: 24251111; PMCID: PMC3829987.
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Creating a twin STAR.

Structure (London, England : 1993)

Cukier CD, Ramos A.
PMID: 20223209
Structure. 2010 Mar 10;18(3):279-80. doi: 10.1016/j.str.2010.02.003.

The Signal Transduction and Activation of RNA (STAR) protein family regulates different levels of RNA metabolism. STAR proteins have been shown to act as homodimers, and the structure of the QUA1 dimerization region of the GLD-1 protein described in...

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Cukier CD, Ramos A. Creating a twin STAR. Structure. 2010;18(3):279-80doi: 10.1016/j.str.2010.02.003.
Cukier, C. D., & Ramos, A. (2010). Creating a twin STAR. Structure (London, England : 1993), 18(3), 279-80. https://doi.org/10.1016/j.str.2010.02.003
Cukier, Cyprian D, and Ramos, Andres. "Creating a twin STAR." Structure (London, England : 1993) vol. 18,3 (2010): 279-80. doi: https://doi.org/10.1016/j.str.2010.02.003
Cukier CD, Ramos A. Creating a twin STAR. Structure. 2010 Mar 10;18(3):279-80. doi: 10.1016/j.str.2010.02.003. PMID: 20223209.
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Measurement of .

Journal of magnetic resonance (San Diego, Calif. : 1997)

Hansen DF.
PMID: 28511856
J Magn Reson. 2017 Jun;279:91-98. doi: 10.1016/j.jmr.2017.01.015.

Many chemical and biological processes rely on the movement of monovalent cations and an understanding of such processes can therefore only be achieved by characterising the dynamics of the involved ions. It has recently been shown that

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Hansen DF. Measurement of . J Magn Reson. 2017;279:91-98doi: 10.1016/j.jmr.2017.01.015.
Hansen, D. F. (2017). Measurement of . Journal of magnetic resonance (San Diego, Calif. : 1997), 27991-98. https://doi.org/10.1016/j.jmr.2017.01.015
Hansen, D Flemming. "Measurement of ." Journal of magnetic resonance (San Diego, Calif. : 1997) vol. 279 (2017): 91-98. doi: https://doi.org/10.1016/j.jmr.2017.01.015
Hansen DF. Measurement of . J Magn Reson. 2017 Jun;279:91-98. doi: 10.1016/j.jmr.2017.01.015. PMID: 28511856; PMCID: PMC5441844.
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Bioactivity and structural properties of chimeric analogs of the starfish SALMFamide neuropeptides S1 and S2.

Biochimica et biophysica acta

Jones CE, Otara CB, Younan ND, Viles JH, Elphick MR.
PMID: 25110179
Biochim Biophys Acta. 2014 Oct;1844(10):1842-50. doi: 10.1016/j.bbapap.2014.08.001. Epub 2014 Aug 08.

The starfish SALMFamide neuropeptides S1 (GFNSALMFamide) and S2 (SGPYSFNSGLTFamide) are the prototypical members of a family of neuropeptides that act as muscle relaxants in echinoderms. Comparison of the bioactivity of S1 and S2 as muscle relaxants has revealed that...

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Jones CE, Otara CB, Younan ND, et al. Bioactivity and structural properties of chimeric analogs of the starfish SALMFamide neuropeptides S1 and S2. Biochim Biophys Acta. 2014;1844(10):1842-50doi: 10.1016/j.bbapap.2014.08.001.
Jones, C. E., Otara, C. B., Younan, N. D., Viles, J. H., & Elphick, M. R. (2014). Bioactivity and structural properties of chimeric analogs of the starfish SALMFamide neuropeptides S1 and S2. Biochimica et biophysica acta, 1844(10), 1842-50. https://doi.org/10.1016/j.bbapap.2014.08.001
Jones, Christopher E, et al. "Bioactivity and structural properties of chimeric analogs of the starfish SALMFamide neuropeptides S1 and S2." Biochimica et biophysica acta vol. 1844,10 (2014): 1842-50. doi: https://doi.org/10.1016/j.bbapap.2014.08.001
Jones CE, Otara CB, Younan ND, Viles JH, Elphick MR. Bioactivity and structural properties of chimeric analogs of the starfish SALMFamide neuropeptides S1 and S2. Biochim Biophys Acta. 2014 Oct;1844(10):1842-50. doi: 10.1016/j.bbapap.2014.08.001. Epub 2014 Aug 08. PMID: 25110179.
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Allosteric regulation of deubiquitylase activity through ubiquitination.

Frontiers in molecular biosciences

Faggiano S, Menon RP, Kelly GP, Todi SV, Scaglione KM, Konarev PV, Svergun DI, Paulson HL, Pastore A.
PMID: 25988170
Front Mol Biosci. 2015 Feb 05;2:2. doi: 10.3389/fmolb.2015.00002. eCollection 2015.

Ataxin-3, the protein responsible for spinocerebellar ataxia type-3, is a cysteine protease that specifically cleaves poly-ubiquitin chains and participates in the ubiquitin proteasome pathway. The enzymatic activity resides in the N-terminal Josephin domain. An unusual feature of ataxin-3 is...

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Faggiano S, Menon RP, Kelly GP, et al. Allosteric regulation of deubiquitylase activity through ubiquitination. Front Mol Biosci. 2015;2:2doi: 10.3389/fmolb.2015.00002.
Faggiano, S., Menon, R. P., Kelly, G. P., Todi, S. V., Scaglione, K. M., Konarev, P. V., Svergun, D. I., Paulson, H. L., & Pastore, A. (2015). Allosteric regulation of deubiquitylase activity through ubiquitination. Frontiers in molecular biosciences, 22. https://doi.org/10.3389/fmolb.2015.00002
Faggiano, Serena, et al. "Allosteric regulation of deubiquitylase activity through ubiquitination." Frontiers in molecular biosciences vol. 2 (2015): 2. doi: https://doi.org/10.3389/fmolb.2015.00002
Faggiano S, Menon RP, Kelly GP, Todi SV, Scaglione KM, Konarev PV, Svergun DI, Paulson HL, Pastore A. Allosteric regulation of deubiquitylase activity through ubiquitination. Front Mol Biosci. 2015 Feb 05;2:2. doi: 10.3389/fmolb.2015.00002. eCollection 2015. PMID: 25988170; PMCID: PMC4428445.
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Showing 1 to 7 of 7 entries