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Showing 1 to 5 of 5 entries
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Photoaffinity-labeled Auxins: Synthesis and Biological Activity.

Plant physiology

Leonard NJ, Greenfield JC.
PMID: 16659209
Plant Physiol. 1975 Jun;55(6):1057-61. doi: 10.1104/pp.55.6.1057.

Two light-sensitive analogs of 2,4-dichlorophenoxyacetic acid, namely 4-azido-2-chlorophenoxyacetic acid and 3-azido-5-chlorophenoxyacetic acid, have been synthesized for use as auxin photoaffinity labels. The preparation and biological activity of the compounds are described. Both contain the photolabile azido group; the 2,4-substituted...

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Leonard NJ, Greenfield JC. Photoaffinity-labeled Auxins: Synthesis and Biological Activity. Plant Physiol. 1975;55(6):1057-61doi: 10.1104/pp.55.6.1057.
Leonard, N. J., & Greenfield, J. C. (1975). Photoaffinity-labeled Auxins: Synthesis and Biological Activity. Plant physiology, 55(6), 1057-61. https://doi.org/10.1104/pp.55.6.1057
Leonard, N J, and Greenfield, J C. "Photoaffinity-labeled Auxins: Synthesis and Biological Activity." Plant physiology vol. 55,6 (1975): 1057-61. doi: https://doi.org/10.1104/pp.55.6.1057
Leonard NJ, Greenfield JC. Photoaffinity-labeled Auxins: Synthesis and Biological Activity. Plant Physiol. 1975 Jun;55(6):1057-61. doi: 10.1104/pp.55.6.1057. PMID: 16659209; PMCID: PMC541765.
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Cleavable linkers and their application in MS-based target identification.

Molecular omics

Beard HA, Korovesis D, Chen S, Verhelst SHL.
PMID: 33507200
Mol Omics. 2021 Apr 01;17(2):197-209. doi: 10.1039/d0mo00181c. Epub 2021 Jan 28.

Covalent chemical probes are important tools in chemical biology. They range from post-translational modification (PTM)-derived metabolic probes, to activity-based probes and photoaffinity labels. Identification of the probe targets is often performed by tandem mass spectrometry-based proteomics methods. In the...

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Beard HA, Korovesis D, Chen S, et al. Cleavable linkers and their application in MS-based target identification. Mol Omics. 2021;17(2):197-209doi: 10.1039/d0mo00181c.
Beard, H. A., Korovesis, D., Chen, S., & Verhelst, S. H. L. (2021). Cleavable linkers and their application in MS-based target identification. Molecular omics, 17(2), 197-209. https://doi.org/10.1039/d0mo00181c
Beard, Hester A, et al. "Cleavable linkers and their application in MS-based target identification." Molecular omics vol. 17,2 (2021): 197-209. doi: https://doi.org/10.1039/d0mo00181c
Beard HA, Korovesis D, Chen S, Verhelst SHL. Cleavable linkers and their application in MS-based target identification. Mol Omics. 2021 Apr 01;17(2):197-209. doi: 10.1039/d0mo00181c. Epub 2021 Jan 28. PMID: 33507200.
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Effective and transient mapping of protein-protein interactions: Application of novel releasable photoaffinity linkers.

Drug development research

Wang J, Ma Y, Li J, Zhang Q, Pan X, Lu W, Zhang J.
PMID: 34424555
Drug Dev Res. 2021 Aug 23; doi: 10.1002/ddr.21866. Epub 2021 Aug 23.

Herein, two novel multifunctional releasable photoaffinity linkers were developed for effective and transient tracking interacting proteins with the overall objective of understanding their in vivo biological functions in real-time. These linkers could be used for the chemical modification of...

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Wang J, Ma Y, Li J, et al. Effective and transient mapping of protein-protein interactions: Application of novel releasable photoaffinity linkers. Drug Dev Res. 2021;doi: 10.1002/ddr.21866.
Wang, J., Ma, Y., Li, J., Zhang, Q., Pan, X., Lu, W., & Zhang, J. (2021). Effective and transient mapping of protein-protein interactions: Application of novel releasable photoaffinity linkers. Drug development research, . https://doi.org/10.1002/ddr.21866
Wang, Jin, et al. "Effective and transient mapping of protein-protein interactions: Application of novel releasable photoaffinity linkers." Drug development research vol. (2021). doi: https://doi.org/10.1002/ddr.21866
Wang J, Ma Y, Li J, Zhang Q, Pan X, Lu W, Zhang J. Effective and transient mapping of protein-protein interactions: Application of novel releasable photoaffinity linkers. Drug Dev Res. 2021 Aug 23; doi: 10.1002/ddr.21866. Epub 2021 Aug 23. PMID: 34424555.
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Photoaffinity-labeled Cytokinins: Synthesis and Biological Activity.

Plant physiology

Theiler JB, Leonard NJ.
PMID: 16659772
Plant Physiol. 1976 Dec;58(6):803-5. doi: 10.1104/pp.58.6.803.

Two new azidopurine derivatives, 2-azido-N(6)-(Delta(2)-isopentenyl)adenine and 2-azido-N(6)-benzyladenine, have been synthesized as potential photoaffinity labels for probing cytokinin-binding sites. The preparation and the biological activity of these compounds are described.

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Theiler JB, Leonard NJ. Photoaffinity-labeled Cytokinins: Synthesis and Biological Activity. Plant Physiol. 1976;58(6):803-5doi: 10.1104/pp.58.6.803.
Theiler, J. B., & Leonard, N. J. (1976). Photoaffinity-labeled Cytokinins: Synthesis and Biological Activity. Plant physiology, 58(6), 803-5. https://doi.org/10.1104/pp.58.6.803
Theiler, J B, and Leonard, N J. "Photoaffinity-labeled Cytokinins: Synthesis and Biological Activity." Plant physiology vol. 58,6 (1976): 803-5. doi: https://doi.org/10.1104/pp.58.6.803
Theiler JB, Leonard NJ. Photoaffinity-labeled Cytokinins: Synthesis and Biological Activity. Plant Physiol. 1976 Dec;58(6):803-5. doi: 10.1104/pp.58.6.803. PMID: 16659772; PMCID: PMC542314.
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Structure-Activity Relationship of Semicarbazone EGA Furnishes Photoaffinity Inhibitors of Anthrax Toxin Cellular Entry.

ACS medicinal chemistry letters

Jung ME, Chamberlain BT, Ho CL, Gillespie EJ, Bradley KA.
PMID: 24900841
ACS Med Chem Lett. 2014 Jan 21;5(4):363-7. doi: 10.1021/ml400486k. eCollection 2014 Apr 10.

EGA, 1, prevents the entry of multiple viruses and bacterial toxins into mammalian cells by inhibiting vesicular trafficking. The cellular target of 1 is unknown, and a structure-activity relationship study was conducted in order to develop a strategy for...

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Jung ME, Chamberlain BT, Ho CL, et al. Structure-Activity Relationship of Semicarbazone EGA Furnishes Photoaffinity Inhibitors of Anthrax Toxin Cellular Entry. ACS Med Chem Lett. 2014;5(4):363-7doi: 10.1021/ml400486k.
Jung, M. E., Chamberlain, B. T., Ho, C. L., Gillespie, E. J., & Bradley, K. A. (2014). Structure-Activity Relationship of Semicarbazone EGA Furnishes Photoaffinity Inhibitors of Anthrax Toxin Cellular Entry. ACS medicinal chemistry letters, 5(4), 363-7. https://doi.org/10.1021/ml400486k
Jung, Michael E, et al. "Structure-Activity Relationship of Semicarbazone EGA Furnishes Photoaffinity Inhibitors of Anthrax Toxin Cellular Entry." ACS medicinal chemistry letters vol. 5,4 (2014): 363-7. doi: https://doi.org/10.1021/ml400486k
Jung ME, Chamberlain BT, Ho CL, Gillespie EJ, Bradley KA. Structure-Activity Relationship of Semicarbazone EGA Furnishes Photoaffinity Inhibitors of Anthrax Toxin Cellular Entry. ACS Med Chem Lett. 2014 Jan 21;5(4):363-7. doi: 10.1021/ml400486k. eCollection 2014 Apr 10. PMID: 24900841; PMCID: PMC4027791.
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Showing 1 to 5 of 5 entries