Surfing the insulin signaling web

Research output: Contribution to journal › Review › Research › peer-review

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Surfing the insulin signaling web. / Van Obberghen, E.; Baron, V.; Delahaye, L.; Emanuelli, B.; Filippa, N.; Giorgetti-Peraldi, S.; Lebrun, P.; Mothe-Satney, I.; Peraldi, P.; Rocchi, S.; Sawka-Verhelle, D.; Tartare-Deckert, S.; Giudicelli, J.

In: European Journal of Clinical Investigation, Vol. 31, No. 11, 01.12.2001, p. 966-977.

Research output: Contribution to journal › Review › Research › peer-review

Harvard

Van Obberghen, E, Baron, V, Delahaye, L, Emanuelli, B, Filippa, N, Giorgetti-Peraldi, S, Lebrun, P, Mothe-Satney, I, Peraldi, P, Rocchi, S, Sawka-Verhelle, D, Tartare-Deckert, S & Giudicelli, J 2001, 'Surfing the insulin signaling web', European Journal of Clinical Investigation, vol. 31, no. 11, pp. 966-977. https://doi.org/10.1046/j.1365-2362.2001.00896.x

APA

Van Obberghen, E., Baron, V., Delahaye, L., Emanuelli, B., Filippa, N., Giorgetti-Peraldi, S., Lebrun, P., Mothe-Satney, I., Peraldi, P., Rocchi, S., Sawka-Verhelle, D., Tartare-Deckert, S., & Giudicelli, J. (2001). Surfing the insulin signaling web. European Journal of Clinical Investigation, 31(11), 966-977. https://doi.org/10.1046/j.1365-2362.2001.00896.x

Vancouver

Van Obberghen E, Baron V, Delahaye L, Emanuelli B, Filippa N, Giorgetti-Peraldi S et al. Surfing the insulin signaling web. European Journal of Clinical Investigation. 2001 Dec 1;31(11):966-977. https://doi.org/10.1046/j.1365-2362.2001.00896.x

Author

Van Obberghen, E. ; Baron, V. ; Delahaye, L. ; Emanuelli, B. ; Filippa, N. ; Giorgetti-Peraldi, S. ; Lebrun, P. ; Mothe-Satney, I. ; Peraldi, P. ; Rocchi, S. ; Sawka-Verhelle, D. ; Tartare-Deckert, S. ; Giudicelli, J. / Surfing the insulin signaling web. In: European Journal of Clinical Investigation. 2001 ; Vol. 31, No. 11. pp. 966-977.

Bibtex

@article{b62b38889e084bdfbc01beaa28ba6a77,
title = "Surfing the insulin signaling web",
abstract = "The diverse biological actions of insulin and insulin-like growth factor I (IGF-I) are initiated by binding of the polypeptides to their respective cell surface tyrosine kinase receptors. These activated receptors phosphorylate a series of endogenous substrates on tyrosine, amongst which the insulin receptor substrate (IRS) proteins are the best characterized. Their phosphotyrosine-containing motifs become binding sites for Src homology 2 (SH2) domains on proteins such as SH2 domain-containing protein-tyrosine-phosphatase (SHP)-2/Syp, growth factor receptor bound-2 protien, (Grb-2), and phosphatidyl inositol 3 kinase (PI3 kinase), which participate in activation of specific signaling cascades. However, the IRS molecules are not only platforms for signaling molecules, they also orchestrate the generation of signal specificity, integration of signals induced by several extracellular stimuli, and signal termination and modulation. An extensive review is beyond the scope of the present article, which will be centered on our own contribution and reflect our biases.",
keywords = "IGF-I, Insulin, Insulin/IGF-I action, Insulin/IGF-I receptor, Tyrosine kinases",
author = "{Van Obberghen}, E. and V. Baron and L. Delahaye and B. Emanuelli and N. Filippa and S. Giorgetti-Peraldi and P. Lebrun and I. Mothe-Satney and P. Peraldi and S. Rocchi and D. Sawka-Verhelle and S. Tartare-Deckert and J. Giudicelli",
year = "2001",
month = dec,
day = "1",
doi = "10.1046/j.1365-2362.2001.00896.x",
language = "English",
volume = "31",
pages = "966--977",
journal = "European Journal of Clinical Investigation, Supplement",
issn = "0960-135X",
publisher = "Wiley-Blackwell",
number = "11",

}

RIS

TY - JOUR

T1 - Surfing the insulin signaling web

AU - Van Obberghen, E.

AU - Baron, V.

AU - Delahaye, L.

AU - Emanuelli, B.

AU - Filippa, N.

AU - Giorgetti-Peraldi, S.

AU - Lebrun, P.

AU - Mothe-Satney, I.

AU - Peraldi, P.

AU - Rocchi, S.

AU - Sawka-Verhelle, D.

AU - Tartare-Deckert, S.

AU - Giudicelli, J.

PY - 2001/12/1

Y1 - 2001/12/1

N2 - The diverse biological actions of insulin and insulin-like growth factor I (IGF-I) are initiated by binding of the polypeptides to their respective cell surface tyrosine kinase receptors. These activated receptors phosphorylate a series of endogenous substrates on tyrosine, amongst which the insulin receptor substrate (IRS) proteins are the best characterized. Their phosphotyrosine-containing motifs become binding sites for Src homology 2 (SH2) domains on proteins such as SH2 domain-containing protein-tyrosine-phosphatase (SHP)-2/Syp, growth factor receptor bound-2 protien, (Grb-2), and phosphatidyl inositol 3 kinase (PI3 kinase), which participate in activation of specific signaling cascades. However, the IRS molecules are not only platforms for signaling molecules, they also orchestrate the generation of signal specificity, integration of signals induced by several extracellular stimuli, and signal termination and modulation. An extensive review is beyond the scope of the present article, which will be centered on our own contribution and reflect our biases.

AB - The diverse biological actions of insulin and insulin-like growth factor I (IGF-I) are initiated by binding of the polypeptides to their respective cell surface tyrosine kinase receptors. These activated receptors phosphorylate a series of endogenous substrates on tyrosine, amongst which the insulin receptor substrate (IRS) proteins are the best characterized. Their phosphotyrosine-containing motifs become binding sites for Src homology 2 (SH2) domains on proteins such as SH2 domain-containing protein-tyrosine-phosphatase (SHP)-2/Syp, growth factor receptor bound-2 protien, (Grb-2), and phosphatidyl inositol 3 kinase (PI3 kinase), which participate in activation of specific signaling cascades. However, the IRS molecules are not only platforms for signaling molecules, they also orchestrate the generation of signal specificity, integration of signals induced by several extracellular stimuli, and signal termination and modulation. An extensive review is beyond the scope of the present article, which will be centered on our own contribution and reflect our biases.

KW - IGF-I

KW - Insulin

KW - Insulin/IGF-I action

KW - Insulin/IGF-I receptor

KW - Tyrosine kinases

UR - http://www.scopus.com/inward/record.url?scp=0035779997&partnerID=8YFLogxK

U2 - 10.1046/j.1365-2362.2001.00896.x

DO - 10.1046/j.1365-2362.2001.00896.x

M3 - Review

C2 - 11737239

AN - SCOPUS:0035779997

VL - 31

SP - 966

EP - 977

JO - European Journal of Clinical Investigation, Supplement

JF - European Journal of Clinical Investigation, Supplement

SN - 0960-135X

IS - 11

ER -

ID: 200864724