Structure of the extracellular region of HER2 alone and in complex with the Herceptin Fab

By Hyun-soo Cho, K. Mason, Kasra X. Ramyar, A. Stanley, S. Gabelli, D. Denney, D. Leahy. Nature, 2003

1,641 citations recorded by the source corpus.

Subfields: Molecular Biology, Oncology, Radiology, Nuclear Medicine and Imaging

View Paper: https://www.semanticscholar.org/paper/0347c93de935b3073df391740cec1687601d37bd

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Molecular Biology

1. R. Roskoski
2. J. Baselga
3. Carlos L. Arteaga
4. N. Hynes
5. M. Moasser
6. Yigong Shi
7. Thomas Holbro
8. C. Blobel

In Oncology

1. N. Hynes
2. R. Roskoski
3. J. Baselga
4. M. Moasser
5. S. Swain
6. Carlos L. Arteaga
7. Thomas Holbro
8. C. Blobel

In Radiology, Nuclear Medicine and Imaging

1. N. Hynes
2. J. Baselga
3. M. Moasser
4. R. Roskoski
5. Carlos L. Arteaga
6. S. Swain
7. Thomas Holbro
8. C. Blobel

Citations in the corpus

• A central role for HER3 in HER2-amplified breast cancer: implications for targeted therapy. (2008, background): “The standard of care in first-line metastatic and adjuvant HER2-positive breast cancer is a regimen containing trastuzumab (Herceptin) that binds to subdomain IV of the extracellular region of HER2 (16).”
• The epidermal growth factor receptor family: Biology driving targeted therapeutics (2008, background): “Trastuzumab binds to ErbB2 in the juxtamembrane region of the ECD but the functional significance of this binding activity is not currently known [167].”
• ErbB receptors: directing key signaling networks throughout life. (2004, background): “The structure of ErbB2’s extracellular region revealed a major difference in comparison to ErbB1 and ErbB3 (19, 20).”
• ErbB receptors and signaling pathways in cancer. (2009, background): “The antibody binds to a region of ErbB2 not involved with receptor dimerization [58], which provides a mechanistic explanation.”
• Novel anticancer targets: revisiting ERBB2 and discovering ERBB3 (2009, background): “Trastuzumab binds to the extracellular juxtamembrane portion of ERBB2 (domain IV”
• Structural basis for inhibition of the epidermal growth factor receptor by cetuximab. (2005, background): “This is larger than typically observed for an antibody-antigen binding interface (Lawrence and Colman, 1993), but is similar to that observed for the interaction of sErbB2 with both trastuzumab (Cho et al., 2003) and pertuzumab (Franklin et al.”
• A glimpse of structural biology through X-ray crystallography. (2014, background): “A notable advance is the development of palbociclib, a highly selective inhibitor of CDK4 and CDK6, for treatment of the HER2 / ER+ breast cancer.”
• Risk Factors and Preventions of Breast Cancer (2017, background): “It can directly interact with the C-terminal portion of domain IV in the extracellular part of HER2 [113,114].”
• The ErbB/HER family of protein-tyrosine kinases and cancer. (2014, background): “determined the structure of the extracellular domain of (i) rat ErbB2 and (ii) human ErbB2 with trastuzumab [43].”
• The oncogene HER2: its signaling and transforming functions and its role in human cancer pathogenesis (2007, background): “Unlike the other members of the family, the extracellular domain of HER2 does not pivot between active and inactive conformations and constitutively exists in an activated conformation (Cho et al., 2003; Garrett et al., 2003).”
• The intrinsic contributions of tyrosine, serine, glycine and arginine to the affinity and specificity of antibodies. (2008, methodology): “nonoverlapping epitopes.(35,36) We used a phage ELISA to test whether HER2 captured with each immobilized antibody could simultaneously bind to phage-displayed Fab-200 (Fig.”