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Visualization and biochemical analyses of the emerging mammalian 14-3-3-phosphoproteome

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Visualization and biochemical analyses of the emerging mammalian 14-3-3-phosphoproteome. / Johnson, Catherine; Tinti, Michele; Wood, Nicola T.; Campbell, David G.; Toth, Rachel; Dubois, Fanny; Geraghty, Kathryn M.; Wong, Barry H. C.; Brown, Laura J.; Tyler, Jennifer; Gernez, Aurelie; Chen, Shuai; Synowsky, Silvia; MacKintosh, Carol.

In: Molecular & Cellular Proteomics, Vol. 10, No. 10, 10.2011, p. -.

Research output: Contribution to journalArticle

Harvard

Johnson, C, Tinti, M, Wood, NT, Campbell, DG, Toth, R, Dubois, F, Geraghty, KM, Wong, BHC, Brown, LJ, Tyler, J, Gernez, A, Chen, S, Synowsky, S & MacKintosh, C 2011, 'Visualization and biochemical analyses of the emerging mammalian 14-3-3-phosphoproteome' Molecular & Cellular Proteomics, vol 10, no. 10, pp. -.

APA

Johnson, C., Tinti, M., Wood, N. T., Campbell, D. G., Toth, R., Dubois, F., Geraghty, K. M., Wong, B. H. C., Brown, L. J., Tyler, J., Gernez, A., Chen, S., Synowsky, S., & MacKintosh, C. (2011). Visualization and biochemical analyses of the emerging mammalian 14-3-3-phosphoproteome. Molecular & Cellular Proteomics, 10(10), -doi: 10.1074/mcp.M110.005751

Vancouver

Johnson C, Tinti M, Wood NT, Campbell DG, Toth R, Dubois F et al. Visualization and biochemical analyses of the emerging mammalian 14-3-3-phosphoproteome. Molecular & Cellular Proteomics. 2011 Oct;10(10):-.

Author

Johnson, Catherine; Tinti, Michele; Wood, Nicola T.; Campbell, David G.; Toth, Rachel; Dubois, Fanny; Geraghty, Kathryn M.; Wong, Barry H. C.; Brown, Laura J.; Tyler, Jennifer; Gernez, Aurelie; Chen, Shuai; Synowsky, Silvia; MacKintosh, Carol / Visualization and biochemical analyses of the emerging mammalian 14-3-3-phosphoproteome.

In: Molecular & Cellular Proteomics, Vol. 10, No. 10, 10.2011, p. -.

Research output: Contribution to journalArticle

Bibtex - Download

@article{e68f93c15e74425ca81c762be33a270c,
title = "Visualization and biochemical analyses of the emerging mammalian 14-3-3-phosphoproteome",
author = "Catherine Johnson and Michele Tinti and Wood, {Nicola T.} and Campbell, {David G.} and Rachel Toth and Fanny Dubois and Geraghty, {Kathryn M.} and Wong, {Barry H. C.} and Brown, {Laura J.} and Jennifer Tyler and Aurelie Gernez and Shuai Chen and Silvia Synowsky and Carol MacKintosh",
year = "2011",
volume = "10",
number = "10",
pages = "--",
journal = "Molecular & Cellular Proteomics",
issn = "1535-9476",

}

RIS (suitable for import to EndNote) - Download

TY - JOUR

T1 - Visualization and biochemical analyses of the emerging mammalian 14-3-3-phosphoproteome

A1 - Johnson,Catherine

A1 - Tinti,Michele

A1 - Wood,Nicola T.

A1 - Campbell,David G.

A1 - Toth,Rachel

A1 - Dubois,Fanny

A1 - Geraghty,Kathryn M.

A1 - Wong,Barry H. C.

A1 - Brown,Laura J.

A1 - Tyler,Jennifer

A1 - Gernez,Aurelie

A1 - Chen,Shuai

A1 - Synowsky,Silvia

A1 - MacKintosh,Carol

AU - Johnson,Catherine

AU - Tinti,Michele

AU - Wood,Nicola T.

AU - Campbell,David G.

AU - Toth,Rachel

AU - Dubois,Fanny

AU - Geraghty,Kathryn M.

AU - Wong,Barry H. C.

AU - Brown,Laura J.

AU - Tyler,Jennifer

AU - Gernez,Aurelie

AU - Chen,Shuai

AU - Synowsky,Silvia

AU - MacKintosh,Carol

PY - 2011/10

Y1 - 2011/10

N2 - <p>Hundreds of candidate 14-3-3-binding (phospho) proteins have been reported in publications that describe one interaction at a time, as well as high-throughput 14-3-3-affinity and mass spectrometry-based studies. Here, we transcribed these data into a common format, deposited the collated data from low-throughput studies in MINT (http://mint.bio.uniroma2.it/mint), and compared the low-and high-throughput data in VisANT graphs that are easy to analyze and extend. Exploring the graphs prompted questions about technical and biological specificity, which were addressed experimentally, resulting in identification of phosphorylated 14-3-3-binding sites in the mitochondrial import sequence of the iron-sulfur cluster assembly enzyme (ISCU), cytoplasmic domains of the mitochondrial fission factor (MFF), and endoplasmic reticulum-tethered receptor expression-enhancing protein 4 (REEP4), RNA regulator SMAUG2, and cytoskeletal regulatory proteins, namely debrin-like protein (DBNL) and kinesin light chain (KLC) isoforms. Therefore, 14-3-3s undergo physiological interactions with proteins that are destined for diverse subcellular locations. Graphing and validating interactions underpins efforts to use 14-3-3-phosphoproteomics to identify mechanisms and biomarkers for signaling pathways in health and disease. Molecular &amp; Cellular Proteomics 10: 10.1074/mcp.M110.005751, 1-15, 2011.</p>

AB - <p>Hundreds of candidate 14-3-3-binding (phospho) proteins have been reported in publications that describe one interaction at a time, as well as high-throughput 14-3-3-affinity and mass spectrometry-based studies. Here, we transcribed these data into a common format, deposited the collated data from low-throughput studies in MINT (http://mint.bio.uniroma2.it/mint), and compared the low-and high-throughput data in VisANT graphs that are easy to analyze and extend. Exploring the graphs prompted questions about technical and biological specificity, which were addressed experimentally, resulting in identification of phosphorylated 14-3-3-binding sites in the mitochondrial import sequence of the iron-sulfur cluster assembly enzyme (ISCU), cytoplasmic domains of the mitochondrial fission factor (MFF), and endoplasmic reticulum-tethered receptor expression-enhancing protein 4 (REEP4), RNA regulator SMAUG2, and cytoskeletal regulatory proteins, namely debrin-like protein (DBNL) and kinesin light chain (KLC) isoforms. Therefore, 14-3-3s undergo physiological interactions with proteins that are destined for diverse subcellular locations. Graphing and validating interactions underpins efforts to use 14-3-3-phosphoproteomics to identify mechanisms and biomarkers for signaling pathways in health and disease. Molecular &amp; Cellular Proteomics 10: 10.1074/mcp.M110.005751, 1-15, 2011.</p>

U2 - 10.1074/mcp.M110.005751

DO - 10.1074/mcp.M110.005751

M1 - Article

JO - Molecular & Cellular Proteomics

JF - Molecular & Cellular Proteomics

SN - 1535-9476

IS - 10

VL - 10

SP - -

ER -

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