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Protein technologies.

Current opinion in biotechnology

Timms JF.
PMID: 18678249
Curr Opin Biotechnol. 2008 Aug;19(4):313-5. doi: 10.1016/j.copbio.2008.07.003. Epub 2008 Aug 11.

No abstract available.

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Timms JF. Protein technologies. Curr Opin Biotechnol. 2008;19(4):313-5doi: 10.1016/j.copbio.2008.07.003.
Timms, J. F. (2008). Protein technologies. Current opinion in biotechnology, 19(4), 313-5. https://doi.org/10.1016/j.copbio.2008.07.003
Timms, John F. "Protein technologies." Current opinion in biotechnology vol. 19,4 (2008): 313-5. doi: https://doi.org/10.1016/j.copbio.2008.07.003
Timms JF. Protein technologies. Curr Opin Biotechnol. 2008 Aug;19(4):313-5. doi: 10.1016/j.copbio.2008.07.003. Epub 2008 Aug 11. PMID: 18678249.
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ITM Probe: analyzing information flow in protein networks.

Bioinformatics (Oxford, England)

Stojmirović A, Yu YK.
PMID: 19561335
Bioinformatics. 2009 Sep 15;25(18):2447-9. doi: 10.1093/bioinformatics/btp398. Epub 2009 Jun 27.

SUMMARY: Founded upon diffusion with damping, ITM Probe is an application for modeling information flow in protein interaction networks without prior restriction to the sub-network of interest. Given a context consisting of desired origins and destinations of information, ITM...

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Stojmirović A, Yu YK. ITM Probe: analyzing information flow in protein networks. Bioinformatics. 2009;25(18):2447-9doi: 10.1093/bioinformatics/btp398.
Stojmirović, A., & Yu, Y. K. (2009). ITM Probe: analyzing information flow in protein networks. Bioinformatics (Oxford, England), 25(18), 2447-9. https://doi.org/10.1093/bioinformatics/btp398
Stojmirović, Aleksandar, and Yu, Yi-Kuo. "ITM Probe: analyzing information flow in protein networks." Bioinformatics (Oxford, England) vol. 25,18 (2009): 2447-9. doi: https://doi.org/10.1093/bioinformatics/btp398
Stojmirović A, Yu YK. ITM Probe: analyzing information flow in protein networks. Bioinformatics. 2009 Sep 15;25(18):2447-9. doi: 10.1093/bioinformatics/btp398. Epub 2009 Jun 27. PMID: 19561335; PMCID: PMC2735661.
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Advances in protein chemistry.

Archivio di scienze biologiche

CEDRANGOLO F.
PMID: 18101408
Arch Sci Biol (Bologna). 1948 Jul-Aug;32(5):366-89.

No abstract available.

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CEDRANGOLO F. Progressi nella chimica delle proteine. Advances in protein chemistry. Arch Sci Biol (Bologna). 1948;32(5):366-89
CEDRANGOLO, F. (1948). Progressi nella chimica delle proteine. Advances in protein chemistry. Archivio di scienze biologiche, 32(5), 366-89.
CEDRANGOLO, F. "Progressi nella chimica delle proteine." Advances in protein chemistry. Archivio di scienze biologiche vol. 32,5 (1948): 366-89.
CEDRANGOLO F. Progressi nella chimica delle proteine. Advances in protein chemistry. Arch Sci Biol (Bologna). 1948 Jul-Aug;32(5):366-89. Italian. PMID: 18101408.
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Comparison of human protein-protein interaction maps.

Bioinformatics (Oxford, England)

Futschik ME, Chaurasia G, Herzel H.
PMID: 17237052
Bioinformatics. 2007 Mar 01;23(5):605-11. doi: 10.1093/bioinformatics/btl683. Epub 2007 Jan 19.

MOTIVATION: Large-scale mappings of protein-protein interactions have started to give us new views of the complex molecular mechanisms inside a cell. After initial projects to systematically map protein interactions in model organisms such as yeast, worm and fly, researchers...

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Futschik ME, Chaurasia G, Herzel H. Comparison of human protein-protein interaction maps. Bioinformatics. 2007;23(5):605-11doi: 10.1093/bioinformatics/btl683.
Futschik, M. E., Chaurasia, G., & Herzel, H. (2007). Comparison of human protein-protein interaction maps. Bioinformatics (Oxford, England), 23(5), 605-11. https://doi.org/10.1093/bioinformatics/btl683
Futschik, Matthias E, et al. "Comparison of human protein-protein interaction maps." Bioinformatics (Oxford, England) vol. 23,5 (2007): 605-11. doi: https://doi.org/10.1093/bioinformatics/btl683
Futschik ME, Chaurasia G, Herzel H. Comparison of human protein-protein interaction maps. Bioinformatics. 2007 Mar 01;23(5):605-11. doi: 10.1093/bioinformatics/btl683. Epub 2007 Jan 19. PMID: 17237052.
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SCUD: fast structure clustering of decoys using reference state to remove overall rotation.

Journal of computational chemistry

Li H, Zhou Y.
PMID: 15954080
J Comput Chem. 2005 Aug;26(11):1189-92. doi: 10.1002/jcc.20251.

We developed a method for fast decoy clustering by using reference root-mean-squared distance (rRMSD) rather than commonly used pairwise RMSD (pRMSD) values. For 41 proteins with 2000 decoys each, the computing efficiency increases nine times without a significant change...

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Li H, Zhou Y. SCUD: fast structure clustering of decoys using reference state to remove overall rotation. J Comput Chem. 2005;26(11):1189-92doi: 10.1002/jcc.20251.
Li, H., & Zhou, Y. (2005). SCUD: fast structure clustering of decoys using reference state to remove overall rotation. Journal of computational chemistry, 26(11), 1189-92. https://doi.org/10.1002/jcc.20251
Li, Hongzhi, and Zhou, Yaoqi. "SCUD: fast structure clustering of decoys using reference state to remove overall rotation." Journal of computational chemistry vol. 26,11 (2005): 1189-92. doi: https://doi.org/10.1002/jcc.20251
Li H, Zhou Y. SCUD: fast structure clustering of decoys using reference state to remove overall rotation. J Comput Chem. 2005 Aug;26(11):1189-92. doi: 10.1002/jcc.20251. PMID: 15954080.
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The high-throughput protein-to-structure pipeline at SECSG.

Acta crystallographica. Section D, Biological crystallography

Liu ZJ, Tempel W, Ng JD, Lin D, Shah AK, Chen L, Horanyi PS, Habel JE, Kataeva IA, Xu H, Yang H, Chang JC, Huang L, Chang SH, Zhou W, Lee D, Praissman JL, Zhang H, Newton MG, Rose JP, Richardson JS, Richardson DC, Wang BC.
PMID: 15930619
Acta Crystallogr D Biol Crystallogr. 2005 Jun;61:679-84. doi: 10.1107/S0907444905013132. Epub 2005 May 26.

Using a high degree of automation, the crystallography core at the Southeast Collaboratory for Structural Genomics (SECSG) has developed a high-throughput protein-to-structure pipeline. Various robots and automation procedures have been adopted and integrated into a pipeline that is capable...

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Liu ZJ, Tempel W, Ng JD, et al. The high-throughput protein-to-structure pipeline at SECSG. Acta Crystallogr D Biol Crystallogr. 2005;61:679-84doi: 10.1107/S0907444905013132.
Liu, Z. J., Tempel, W., Ng, J. D., Lin, D., Shah, A. K., Chen, L., Horanyi, P. S., Habel, J. E., Kataeva, I. A., Xu, H., Yang, H., Chang, J. C., Huang, L., Chang, S. H., Zhou, W., Lee, D., Praissman, J. L., Zhang, H., Newton, M. G., Rose, J. P., Richardson, J. S., Richardson, D. C., & Wang, B. C. (2005). The high-throughput protein-to-structure pipeline at SECSG. Acta crystallographica. Section D, Biological crystallography, 61679-84. https://doi.org/10.1107/S0907444905013132
Liu, Zhi-Jie, et al. "The high-throughput protein-to-structure pipeline at SECSG." Acta crystallographica. Section D, Biological crystallography vol. 61 (2005): 679-84. doi: https://doi.org/10.1107/S0907444905013132
Liu ZJ, Tempel W, Ng JD, Lin D, Shah AK, Chen L, Horanyi PS, Habel JE, Kataeva IA, Xu H, Yang H, Chang JC, Huang L, Chang SH, Zhou W, Lee D, Praissman JL, Zhang H, Newton MG, Rose JP, Richardson JS, Richardson DC, Wang BC. The high-throughput protein-to-structure pipeline at SECSG. Acta Crystallogr D Biol Crystallogr. 2005 Jun;61:679-84. doi: 10.1107/S0907444905013132. Epub 2005 May 26. PMID: 15930619.
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Multiple enzyme layers on carbon nanotubes for electrochemical detection down to 80 DNA copies.

Analytical chemistry

Munge B, Liu G, Collins G, Wang J.
PMID: 16013886
Anal Chem. 2005 Jul 15;77(14):4662-6. doi: 10.1021/ac050132g.

Signal amplification using enzyme multilayers on carbon nanotube (CNT) templates is shown to yield a remarkably sensitive electrochemical detection of proteins and nucleic acids. The electrostatic layer-by-layer (LBL) self-assembly onto CNT carriers maximizes the ratio of enzyme tags per...

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Munge B, Liu G, Collins G, et al. Multiple enzyme layers on carbon nanotubes for electrochemical detection down to 80 DNA copies. Anal Chem. 2005;77(14):4662-6doi: 10.1021/ac050132g.
Munge, B., Liu, G., Collins, G., & Wang, J. (2005). Multiple enzyme layers on carbon nanotubes for electrochemical detection down to 80 DNA copies. Analytical chemistry, 77(14), 4662-6. https://doi.org/10.1021/ac050132g
Munge, Bernard, et al. "Multiple enzyme layers on carbon nanotubes for electrochemical detection down to 80 DNA copies." Analytical chemistry vol. 77,14 (2005): 4662-6. doi: https://doi.org/10.1021/ac050132g
Munge B, Liu G, Collins G, Wang J. Multiple enzyme layers on carbon nanotubes for electrochemical detection down to 80 DNA copies. Anal Chem. 2005 Jul 15;77(14):4662-6. doi: 10.1021/ac050132g. PMID: 16013886.
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Unfolded proteins.

Advances in protein chemistry

[No authors listed]
PMID: 14750509
Adv Protein Chem. 2002;62:i-xxiv, 1-398.

No abstract available.

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Unfolded proteins. Adv Protein Chem. 2002;62:i-xxiv, 1-398
(2002). Unfolded proteins. Advances in protein chemistry, 62i-xxiv, 1-398.
"Unfolded proteins." Advances in protein chemistry vol. 62 (2002): i-xxiv, 1-398.
Unfolded proteins. Adv Protein Chem. 2002;62:i-xxiv, 1-398. PMID: 14750509.
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Fog chamber images of mesons of small mass.

Experientia

RULING J, STEINMAURER R.
PMID: 18148056
Experientia. 1949 Sep 15;5(9):355-7. doi: 10.1007/BF02174511.

No abstract available.

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RULING J, STEINMAURER R. Nebelkammeraufnahmen von Mesonen kleiner Masse. Fog chamber images of mesons of small mass. Experientia. 1949;5(9):355-7doi: 10.1007/BF02174511.
RULING, J., & STEINMAURER, R. (1949). Nebelkammeraufnahmen von Mesonen kleiner Masse. Fog chamber images of mesons of small mass. Experientia, 5(9), 355-7. https://doi.org/10.1007/BF02174511
RULING, J, and STEINMAURER, R. "Nebelkammeraufnahmen von Mesonen kleiner Masse." Fog chamber images of mesons of small mass. Experientia vol. 5,9 (1949): 355-7. doi: https://doi.org/10.1007/BF02174511
RULING J, STEINMAURER R. Nebelkammeraufnahmen von Mesonen kleiner Masse. Fog chamber images of mesons of small mass. Experientia. 1949 Sep 15;5(9):355-7. doi: 10.1007/BF02174511. German. PMID: 18148056.
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The internal structure of protein molecules.

Experientia

HAUROWITZ F.
PMID: 18139340
Experientia. 1949 Sep 15;5(9):347-54.

No abstract available.

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HAUROWITZ F. The internal structure of protein molecules. Experientia. 1949;5(9):347-54
HAUROWITZ, F. (1949). The internal structure of protein molecules. Experientia, 5(9), 347-54.
HAUROWITZ, F. "The internal structure of protein molecules." Experientia vol. 5,9 (1949): 347-54.
HAUROWITZ F. The internal structure of protein molecules. Experientia. 1949 Sep 15;5(9):347-54. PMID: 18139340.
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On the acyl shift in protein reactions.

Enzymologia

SAROFF HA.
PMID: 14441780
Enzymologia. 1959 Oct 15;21:101-13.

No abstract available.

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SAROFF HA. On the acyl shift in protein reactions. Enzymologia. 1959;21:101-13
SAROFF, H. A. (1959). On the acyl shift in protein reactions. Enzymologia, 21101-13.
SAROFF, H A. "On the acyl shift in protein reactions." Enzymologia vol. 21 (1959): 101-13.
SAROFF HA. On the acyl shift in protein reactions. Enzymologia. 1959 Oct 15;21:101-13. PMID: 14441780.
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NMR and structural genomics.

Accounts of chemical research

Staunton D, Owen J, Campbell ID.
PMID: 12641478
Acc Chem Res. 2003 Mar;36(3):207-14. doi: 10.1021/ar010119s.

The role of NMR in structural genomics is outlined, with particular emphasis on using protein domains as targets. Strategies for domain expression, characterization, and labeling are presented.

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Staunton D, Owen J, Campbell ID. NMR and structural genomics. Acc Chem Res. 2003;36(3):207-14doi: 10.1021/ar010119s.
Staunton, D., Owen, J., & Campbell, I. D. (2003). NMR and structural genomics. Accounts of chemical research, 36(3), 207-14. https://doi.org/10.1021/ar010119s
Staunton, David, et al. "NMR and structural genomics." Accounts of chemical research vol. 36,3 (2003): 207-14. doi: https://doi.org/10.1021/ar010119s
Staunton D, Owen J, Campbell ID. NMR and structural genomics. Acc Chem Res. 2003 Mar;36(3):207-14. doi: 10.1021/ar010119s. PMID: 12641478.
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Showing 1 to 12 of 84 entries