Higher‐order interactions of <scp>Bcr‐Abl</scp> can broaden chronic myeloid leukemia (CML) drug repertoire-Reference-Cited by-同舟云学术

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Higher‐order interactions of Bcr‐Abl can broaden chronic myeloid leukemia (CML) drug repertoire

Published:2022-12-28 Issue:1 Volume:32 Page:
ISSN:0961-8368
Container-title:Protein Science
language:en
Short-container-title:Protein Science

Author:

Liu Yonglan¹,Zhang Mingzhen²,Jang Hyunbum²,Nussinov Ruth²³^ORCID

Affiliation:

1. Cancer Innovation Laboratory National Cancer Institute Frederick Maryland USA

2. Computational Structural Biology Section Frederick National Laboratory for Cancer Research Frederick Maryland USA

3. Department of Human Molecular Genetics and Biochemistry Sackler School of Medicine, Tel Aviv University Tel Aviv Israel

Funder

National Cancer Institute

National Institutes of Health

Council for Chemical Research

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/pro.4504

Reference82 articles.

1. Resistance to Tyrosine Kinase Inhibitors in Chronic Myeloid Leukemia—From Molecular Mechanisms to Clinical Relevance

2. Coiled coils: attractive protein folding motifs for the fabrication of self-assembled, responsive and bioactive materials

3. Atomistic Modeling of the ABL Kinase Regulation by Allosteric Modulators Using Structural Perturbation Analysis and Community-Based Network Reconstruction of Allosteric Communications

4. Targeting of the N-terminal coiled coil oligomerization interface by a helix-2 peptide inhibits unmutated and imatinib-resistant BCR/ABL

5. Targeting of the N-terminal coiled coil oligomerization interface of BCR interferes with the transformation potential of BCR-ABL and increases sensitivity to STI571

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