Skip to main content

Advertisement

Log in

Resonance assignments of human C35 (C17orf37) protein, a novel tumor biomarker

  • Article
  • Published:
Biomolecular NMR Assignments Aims and scope Submit manuscript

Abstract

A new tumor-specific target, termed C35 (C17orf37), has been identified by representational difference analysis of tumor and normal human mammary cell lines. C35 protein is considered to be an important target for cancer therapy, since the over expression of C35 functionally enhances migration and invasion of tumor cells. Here we report the NMR resonance assignments of C35 protein for further structural determination and functional studies.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Fig. 1
Fig. 2

Similar content being viewed by others

References

  • Dasgupta S, Wasson LM, Rauniyar N, Prokai L, Borejdo J, Vishwanatha JK (2009) Novel gene C17orf37 in 17q12 amplicon promotes migration and invasion of prostate cancer cells. Oncogene 28(32):2860–2872

    Article  Google Scholar 

  • Evans EE, Henn AD, Jonason A, Paris MJ, Schiffhauer LM, Borrello MA, Smith ES, Sahasrabudhe DM, Zauderer M (2006) C35 (C17orf37) is a novel tumor biomarker abundantly expressed in breast cancer. Mol Cancer Ther 5(11):2919–2930

    Article  Google Scholar 

  • Goddard TD, Kneller DG, SPARKY 3, University of California, San Francisco Kauraniemi P, Kallioniemi A (2006) Activation of multiple cancer-associated genes at the ERBB2 amplicon in breast cancer. Endocr Relat Cancer 13(1):39–49

    Google Scholar 

  • Markley JL, Bax A, Arata Y, Hilbers CW, Kaptein R, Sykes BD, Wright PE, Wuthrich K (1998) Recommendations for the presentation of NMR structures of proteins and nucleic acids. IUPAC-IUBMB-IUPAB Inter-Union Task Group on the standardization of data bases of protein and nucleic acid structures determined by NMR spectroscopy. J Biomol NMR 12:1–23

    Article  Google Scholar 

  • Sattler M, Schleucher J, Griesinger C (1999) Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients. Prog Nucl Magn Reson Spectrosc 34:93–158

    Article  Google Scholar 

  • Wishart DS, Sykes BD (1994) The 13C chemical shift index: a simple method for the identification of protein secondary structure using 13C chemical shift data. J Biomol NMR 4:171–180

    Article  Google Scholar 

Download references

Acknowledgments

The NMR spectra were obtained at High-Field Nuclear Magnetic Resonance Center (HF-NMRC) supported by the National Research Program for Genomic Medicine. This work was supported by the National Science Council, Taiwan to C.-H. HSU (NSC96-2113-M-002-028-MY2 and NSC97-2113-M-002-005-MY2).

Author information

Authors and Affiliations

Authors

Corresponding authors

Correspondence to Chi-Fon Chang or Chun-Hua Hsu.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Yang, CJ., Chang, CF., Huang, LY. et al. Resonance assignments of human C35 (C17orf37) protein, a novel tumor biomarker. Biomol NMR Assign 4, 191–193 (2010). https://doi.org/10.1007/s12104-010-9218-9

Download citation

  • Received:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s12104-010-9218-9

Keywords

Navigation