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Showing 1 to 12 of 41 entries
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[Proteins and growth].

Imprensa medica

CHAVES N.
PMID: 14897388
Imprensa Medica. 1951 May;27(449):57-61.

No abstract available.

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CHAVES N. Proteänas e crescimento. [Proteins and growth]. Imprensa Medica. 1951;27(449):57-61
CHAVES, N. (1951). Proteänas e crescimento. [Proteins and growth]. Imprensa medica, 27(449), 57-61.
CHAVES, N. "Proteänas e crescimento." [Proteins and growth]. Imprensa medica vol. 27,449 (1951): 57-61.
CHAVES N. Proteänas e crescimento. [Proteins and growth]. Imprensa Medica. 1951 May;27(449):57-61. Undetermined. PMID: 14897388.
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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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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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Biological methods of evaluating protein quality.

The Proceedings of the Nutrition Society

BENDER AE.
PMID: 13542617
Proc Nutr Soc. 1958;17(1):85-91. doi: 10.1079/pns19580016.

No abstract available.

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BENDER AE. Biological methods of evaluating protein quality. Proc Nutr Soc. 1958;17(1):85-91doi: 10.1079/pns19580016.
BENDER, A. E. (1958). Biological methods of evaluating protein quality. The Proceedings of the Nutrition Society, 17(1), 85-91. https://doi.org/10.1079/pns19580016
BENDER, A E. "Biological methods of evaluating protein quality." The Proceedings of the Nutrition Society vol. 17,1 (1958): 85-91. doi: https://doi.org/10.1079/pns19580016
BENDER AE. Biological methods of evaluating protein quality. Proc Nutr Soc. 1958;17(1):85-91. doi: 10.1079/pns19580016. PMID: 13542617.
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ISOTOPIC measurement of protein absorption.

Nutrition reviews

[No authors listed]
PMID: 13055146
Nutr Rev. 1953 May;11(5):136-7. doi: 10.1111/j.1753-4887.1953.tb01316.x.

No abstract available.

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ISOTOPIC measurement of protein absorption. Nutr Rev. 1953;11(5):136-7doi: 10.1111/j.1753-4887.1953.tb01316.x.
(1953). ISOTOPIC measurement of protein absorption. Nutrition reviews, 11(5), 136-7. https://doi.org/10.1111/j.1753-4887.1953.tb01316.x
"ISOTOPIC measurement of protein absorption." Nutrition reviews vol. 11,5 (1953): 136-7. doi: https://doi.org/10.1111/j.1753-4887.1953.tb01316.x
ISOTOPIC measurement of protein absorption. Nutr Rev. 1953 May;11(5):136-7. doi: 10.1111/j.1753-4887.1953.tb01316.x. PMID: 13055146.
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[Fate of intravenously administered protein].

Uspekhi sovremennoi biologii

GURVICH AE.
PMID: 13157255
Usp Sovrem Biol. 1954 Jan-Feb;37(1):94-113.

No abstract available.

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GURVICH AE. Sud'ba vnutrivenno vvedennogo belka. [Fate of intravenously administered protein]. Usp Sovrem Biol. 1954;37(1):94-113
GURVICH, A. E. (1954). Sud'ba vnutrivenno vvedennogo belka. [Fate of intravenously administered protein]. Uspekhi sovremennoi biologii, 37(1), 94-113.
GURVICH, A E. "Sud'ba vnutrivenno vvedennogo belka." [Fate of intravenously administered protein]. Uspekhi sovremennoi biologii vol. 37,1 (1954): 94-113.
GURVICH AE. Sud'ba vnutrivenno vvedennogo belka. [Fate of intravenously administered protein]. Usp Sovrem Biol. 1954 Jan-Feb;37(1):94-113. Undetermined. PMID: 13157255.
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Do protein-protein interaction databases identify moonlighting proteins?.

Molecular bioSystems

Gómez A, Hernández S, Amela I, Piñol J, Cedano J, Querol E.
PMID: 21677976
Mol Biosyst. 2011 Aug;7(8):2379-82. doi: 10.1039/c1mb05180f. Epub 2011 Jun 16.

One of the most striking results of the human (and mammalian) genomes is the low number of protein-coding genes. To-date, the main molecular mechanism to increase the number of different protein isoforms and functions is alternative splicing. However, a...

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Gómez A, Hernández S, Amela I, et al. Do protein-protein interaction databases identify moonlighting proteins?. Mol Biosyst. 2011;7(8):2379-82doi: 10.1039/c1mb05180f.
Gómez, A., Hernández, S., Amela, I., Piñol, J., Cedano, J., & Querol, E. (2011). Do protein-protein interaction databases identify moonlighting proteins?. Molecular bioSystems, 7(8), 2379-82. https://doi.org/10.1039/c1mb05180f
Gómez, Antonio, et al. "Do protein-protein interaction databases identify moonlighting proteins?." Molecular bioSystems vol. 7,8 (2011): 2379-82. doi: https://doi.org/10.1039/c1mb05180f
Gómez A, Hernández S, Amela I, Piñol J, Cedano J, Querol E. Do protein-protein interaction databases identify moonlighting proteins?. Mol Biosyst. 2011 Aug;7(8):2379-82. doi: 10.1039/c1mb05180f. Epub 2011 Jun 16. PMID: 21677976.
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Towards a human proteomics atlas.

Analytical and bioanalytical chemistry

Gonnelli G, Hulstaert N, Degroeve S, Martens L.
PMID: 22447219
Anal Bioanal Chem. 2012 Sep;404(4):1069-77. doi: 10.1007/s00216-012-5940-8. Epub 2012 Mar 25.

Proteomics research has taken up an increasingly important role in life sciences over the past few years. Due to a strong push from publishers and funders alike, the community has also started to freely share its data in earnest,...

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Gonnelli G, Hulstaert N, Degroeve S, et al. Towards a human proteomics atlas. Anal Bioanal Chem. 2012;404(4):1069-77doi: 10.1007/s00216-012-5940-8.
Gonnelli, G., Hulstaert, N., Degroeve, S., & Martens, L. (2012). Towards a human proteomics atlas. Analytical and bioanalytical chemistry, 404(4), 1069-77. https://doi.org/10.1007/s00216-012-5940-8
Gonnelli, Giulia, et al. "Towards a human proteomics atlas." Analytical and bioanalytical chemistry vol. 404,4 (2012): 1069-77. doi: https://doi.org/10.1007/s00216-012-5940-8
Gonnelli G, Hulstaert N, Degroeve S, Martens L. Towards a human proteomics atlas. Anal Bioanal Chem. 2012 Sep;404(4):1069-77. doi: 10.1007/s00216-012-5940-8. Epub 2012 Mar 25. PMID: 22447219.
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Modules, modularity and adaptation: Comment on "The emergence of modularity in biological systems" by Dirk M. Lorenz, Alice Jeng, Michael W. Deem.

Physics of life reviews

Buchman TG.
PMID: 21600860
Phys Life Rev. 2011 Jun;8(2):163-4; discussion 167-8. doi: 10.1016/j.plrev.2011.05.002. Epub 2011 May 06.

No abstract available.

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Buchman TG. Modules, modularity and adaptation: Comment on "The emergence of modularity in biological systems" by Dirk M. Lorenz, Alice Jeng, Michael W. Deem. Phys Life Rev. 2011;8(2):163-4; discussion 167-8doi: 10.1016/j.plrev.2011.05.002.
Buchman, T. G. (2011). Modules, modularity and adaptation: Comment on "The emergence of modularity in biological systems" by Dirk M. Lorenz, Alice Jeng, Michael W. Deem. Physics of life reviews, 8(2), 163-4; discussion 167-8. https://doi.org/10.1016/j.plrev.2011.05.002
Buchman, Timothy G. "Modules, modularity and adaptation: Comment on "The emergence of modularity in biological systems" by Dirk M. Lorenz, Alice Jeng, Michael W. Deem." Physics of life reviews vol. 8,2 (2011): 163-4; discussion 167-8. doi: https://doi.org/10.1016/j.plrev.2011.05.002
Buchman TG. Modules, modularity and adaptation: Comment on "The emergence of modularity in biological systems" by Dirk M. Lorenz, Alice Jeng, Michael W. Deem. Phys Life Rev. 2011 Jun;8(2):163-4; discussion 167-8. doi: 10.1016/j.plrev.2011.05.002. Epub 2011 May 06. PMID: 21600860.
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Anomalous protein-DNA interactions behind neurological disorders.

Advances in protein chemistry and structural biology

Camero S, Benítez MJ, Jiménez JS.
PMID: 23790210
Adv Protein Chem Struct Biol. 2013;91:37-63. doi: 10.1016/B978-0-12-411637-5.00002-0.

Aggregation, nuclear location, and nucleic acid interaction are common features shared by a number of proteins related to neurodegenerative diseases, including Alzheimer's disease, Parkinson's disease, amyotrophic lateral sclerosis, transmissible spongiform encephalopathy, Huntington's disease, spinobulbar muscular atrophy, dentatorubro-pallidoluysian atrophy, and...

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Camero S, Benítez MJ, Jiménez JS. Anomalous protein-DNA interactions behind neurological disorders. Adv Protein Chem Struct Biol. 2013;91:37-63doi: 10.1016/B978-0-12-411637-5.00002-0.
Camero, S., Benítez, M. J., & Jiménez, J. S. (2013). Anomalous protein-DNA interactions behind neurological disorders. Advances in protein chemistry and structural biology, 9137-63. https://doi.org/10.1016/B978-0-12-411637-5.00002-0
Camero, Sergio, et al. "Anomalous protein-DNA interactions behind neurological disorders." Advances in protein chemistry and structural biology vol. 91 (2013): 37-63. doi: https://doi.org/10.1016/B978-0-12-411637-5.00002-0
Camero S, Benítez MJ, Jiménez JS. Anomalous protein-DNA interactions behind neurological disorders. Adv Protein Chem Struct Biol. 2013;91:37-63. doi: 10.1016/B978-0-12-411637-5.00002-0. PMID: 23790210.
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Characterization of a high field Orbitrap mass spectrometer for proteome analysis.

Proteomics

Pachl F, Ruprecht B, Lemeer S, Kuster B.
PMID: 23836775
Proteomics. 2013 Sep;13(17):2552-62. doi: 10.1002/pmic.201300076. Epub 2013 Jul 30.

The field of proteomics continues to be driven by improvements in analytical technology, notably in peptide separation, quantitative MS, and informatics. In this study, we have characterized a hybrid linear ion trap high field Orbitrap mass spectrometer (Orbitrap Elite)...

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Pachl F, Ruprecht B, Lemeer S, et al. Characterization of a high field Orbitrap mass spectrometer for proteome analysis. Proteomics. 2013;13(17):2552-62doi: 10.1002/pmic.201300076.
Pachl, F., Ruprecht, B., Lemeer, S., & Kuster, B. (2013). Characterization of a high field Orbitrap mass spectrometer for proteome analysis. Proteomics, 13(17), 2552-62. https://doi.org/10.1002/pmic.201300076
Pachl, Fiona, et al. "Characterization of a high field Orbitrap mass spectrometer for proteome analysis." Proteomics vol. 13,17 (2013): 2552-62. doi: https://doi.org/10.1002/pmic.201300076
Pachl F, Ruprecht B, Lemeer S, Kuster B. Characterization of a high field Orbitrap mass spectrometer for proteome analysis. Proteomics. 2013 Sep;13(17):2552-62. doi: 10.1002/pmic.201300076. Epub 2013 Jul 30. PMID: 23836775.
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Mapping the stabilome: a novel computational method for classifying metabolic protein stability.

BMC systems biology

Patrick R, Cao KA, Davis M, Kobe B, Bodén M.
PMID: 22682214
BMC Syst Biol. 2012 Jun 08;6:60. doi: 10.1186/1752-0509-6-60.

BACKGROUND: The half-life of a protein is regulated by a range of system properties, including the abundance of components of the degradative machinery and protein modifiers. It is also influenced by protein-specific properties, such as a protein's structural make-up...

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Patrick R, Cao KA, Davis M, et al. Mapping the stabilome: a novel computational method for classifying metabolic protein stability. BMC Syst Biol. 2012;6:60doi: 10.1186/1752-0509-6-60.
Patrick, R., Cao, K. A., Davis, M., Kobe, B., & Bodén, M. (2012). Mapping the stabilome: a novel computational method for classifying metabolic protein stability. BMC systems biology, 660. https://doi.org/10.1186/1752-0509-6-60
Patrick, Ralph, et al. "Mapping the stabilome: a novel computational method for classifying metabolic protein stability." BMC systems biology vol. 6 (2012): 60. doi: https://doi.org/10.1186/1752-0509-6-60
Patrick R, Cao KA, Davis M, Kobe B, Bodén M. Mapping the stabilome: a novel computational method for classifying metabolic protein stability. BMC Syst Biol. 2012 Jun 08;6:60. doi: 10.1186/1752-0509-6-60. PMID: 22682214; PMCID: PMC3439251.
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Showing 1 to 12 of 41 entries