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Cited by 261

The DOI matches its Crossref record; 45 of the 45 references it cites were found in a registry or an index.

Affinity-based proteomics reveal cancer-specific networks coordinated by Hsp90

Open access
Moulick, Kamalika, Ahn, James H, Zong, Hongliang, Rodina, Anna, Cerchietti, Leandro, Gomes DaGama, Erica M, Caldas-Lopes, Eloisi, Beebe, Kristin, Perna, Fabiana, Hatzi, Katerina, Vu, Ly P, Zhao, Xinyang, Zatorska, Danuta, Taldone, Tony, Smith-Jones, Peter, Alpaugh, Mary, Gross, Steven S, Pillarsetty, Nagavarakishore, Ku, Thomas, Lewis, Jason S, Larson, Steven M, Levine, Ross, Erdjument-Bromage, Hediye, Guzman, Monica L, Nimer, Stephen D, Melnick, Ari, Neckers, Len, Chiosis, Gabriela·2011·Nature Chemical Biology

Abstract

Most cancers are characterized by multiple molecular alterations, but identification of the key proteins involved in these signaling pathways is currently beyond reach. We show that the inhibitor PU-H71 preferentially targets tumor-enriched Hsp90 complexes and affinity captures Hsp90-dependent oncogenic client proteins. We have used PU-H71 affinity capture to design a proteomic approach that, when combined with bioinformatic pathway analysis, identifies dysregulated signaling networks and key oncoproteins in chronic myeloid leukemia. The identified interactome overlaps with the well-characterized altered proteome in this cancer, indicating that this method can provide global insights into the biology of individual tumors, including primary patient specimens. In addition, we show that this approach can be used to identify previously uncharacterized oncoproteins and mechanisms, potentially leading to new targeted therapies. We further show that the abundance of the PU-H71-enriched Hsp90 species, which is not dictated by Hsp90 expression alone, is predictive of the cell’s sensitivity to Hsp90 inhibition.

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Metadata

Authors
Moulick, K., Ahn, J. H., Zong, H., Rodina, A., Cerchietti, L., Gomes DaGama, E. M., Caldas-Lopes, E., Beebe, K., Perna, F., Hatzi, K., Vu, L. P., Zhao, X., Zatorska, D., Taldone, T., Smith-Jones, P., Alpaugh, M., Gross, S. S., Pillarsetty, N., Ku, T., Lewis, J. S., Larson, S. M., Levine, R., Erdjument-Bromage, H., Guzman, M. L., Nimer, S. D., Melnick, A., Neckers, L., & Chiosis, G.
Venue
Nature Chemical Biology
Published
2011-09-25
Volume
7
Issue
11
Pages
818-826
ISSN
  • 1552-4450 (ISSN-L)
  • 1552-4469
OpenAlex
W2029431941
Cited by
261
References
45
FWCI
9.29
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Affinity-based proteomics reveal cancer-specific networks coordinated by Hsp90. https://app.cochat.ai/papers/10.1038/nchembio.670
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Moulick, K., Ahn, J. H., Zong, H., Rodina, A., Cerchietti, L., Gomes DaGama, E. M., Caldas-Lopes, E., Beebe, K., Perna, F., Hatzi, K., Vu, L. P., Zhao, X., Zatorska, D., Taldone, T., Smith-Jones, P., Alpaugh, M., Gross, S. S., Pillarsetty, N., Ku, T., . . . Chiosis, G. (2011). Affinity-based proteomics reveal cancer-specific networks coordinated by Hsp90. Nature Chemical Biology. https://doi.org/10.1038/nchembio.670

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.