The dimer-dependent catalytic activity of RAF family kinases is revealed through characterizing their oncogenic mutants

10.1038/s41388-018-0365-2

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Main Authors:	Yuan, J, Ng, W.H, Lam, P.Y.P, Wang, Y, Xia, H, Yap, J, Guan, S.P, Lee, A.S.G, Wang, M, Baccarini, M, Hu, J
Other Authors:	PHYSIOLOGY
Format:	Article
Published:	Nature Publishing Group 2020
Subjects:	A Raf kinase B Raf kinase dimer glutamic acid isoenzyme mitogen activated protein kinase mitogen activated protein kinase kinase mutant protein Raf protein valine allosterism animal experiment animal model animal tissue Article binding affinity cancer therapy catalysis controlled study dimerization enzyme activation enzyme activity enzyme analysis enzyme phosphorylation female gene mutation human human cell molecular biology mouse nonhuman priority journal protein family protein motif animal enzymology genetics knockout mouse MAPK signaling metabolism mutation neoplasm pathology protein multimerization tumor cell line Animals Catalysis Cell Line, Tumor MAP Kinase Signaling System Mice Mice, Knockout Mutation Neoplasms Protein Multimerization raf Kinases
Online Access:	https://scholarbank.nus.edu.sg/handle/10635/175101
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Institution:	National University of Singapore

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spelling	sg-nus-scholar.10635-1751012024-11-13T05:46:09Z The dimer-dependent catalytic activity of RAF family kinases is revealed through characterizing their oncogenic mutants Yuan, J Ng, W.H Lam, P.Y.P Wang, Y Xia, H Yap, J Guan, S.P Lee, A.S.G Wang, M Baccarini, M Hu, J PHYSIOLOGY MICROBIOLOGY AND IMMUNOLOGY DUKE-NUS MEDICAL SCHOOL BIOCHEMISTRY A Raf kinase B Raf kinase dimer glutamic acid isoenzyme mitogen activated protein kinase mitogen activated protein kinase kinase mutant protein Raf protein valine Raf protein allosterism animal experiment animal model animal tissue Article binding affinity cancer therapy catalysis controlled study dimerization enzyme activation enzyme activity enzyme analysis enzyme phosphorylation female gene mutation human human cell molecular biology mouse nonhuman priority journal protein family protein motif animal catalysis enzymology genetics knockout mouse MAPK signaling metabolism mutation neoplasm pathology protein multimerization tumor cell line Animals Catalysis Cell Line, Tumor MAP Kinase Signaling System Mice Mice, Knockout Mutation Neoplasms Protein Multimerization raf Kinases 10.1038/s41388-018-0365-2 Oncogene 37 43 5719-5734 2020-09-09T03:44:39Z 2020-09-09T03:44:39Z 2018 Article Yuan, J, Ng, W.H, Lam, P.Y.P, Wang, Y, Xia, H, Yap, J, Guan, S.P, Lee, A.S.G, Wang, M, Baccarini, M, Hu, J (2018). The dimer-dependent catalytic activity of RAF family kinases is revealed through characterizing their oncogenic mutants. Oncogene 37 (43) : 5719-5734. ScholarBank@NUS Repository. https://doi.org/10.1038/s41388-018-0365-2 0950-9232 https://scholarbank.nus.edu.sg/handle/10635/175101 Nature Publishing Group Unpaywall 20200831
institution	National University of Singapore
building	NUS Library
continent	Asia
country	Singapore Singapore
content_provider	NUS Library
collection	ScholarBank@NUS
topic	A Raf kinase B Raf kinase dimer glutamic acid isoenzyme mitogen activated protein kinase mitogen activated protein kinase kinase mutant protein Raf protein valine Raf protein allosterism animal experiment animal model animal tissue Article binding affinity cancer therapy catalysis controlled study dimerization enzyme activation enzyme activity enzyme analysis enzyme phosphorylation female gene mutation human human cell molecular biology mouse nonhuman priority journal protein family protein motif animal catalysis enzymology genetics knockout mouse MAPK signaling metabolism mutation neoplasm pathology protein multimerization tumor cell line Animals Catalysis Cell Line, Tumor MAP Kinase Signaling System Mice Mice, Knockout Mutation Neoplasms Protein Multimerization raf Kinases
spellingShingle	A Raf kinase B Raf kinase dimer glutamic acid isoenzyme mitogen activated protein kinase mitogen activated protein kinase kinase mutant protein Raf protein valine Raf protein allosterism animal experiment animal model animal tissue Article binding affinity cancer therapy catalysis controlled study dimerization enzyme activation enzyme activity enzyme analysis enzyme phosphorylation female gene mutation human human cell molecular biology mouse nonhuman priority journal protein family protein motif animal catalysis enzymology genetics knockout mouse MAPK signaling metabolism mutation neoplasm pathology protein multimerization tumor cell line Animals Catalysis Cell Line, Tumor MAP Kinase Signaling System Mice Mice, Knockout Mutation Neoplasms Protein Multimerization raf Kinases Yuan, J Ng, W.H Lam, P.Y.P Wang, Y Xia, H Yap, J Guan, S.P Lee, A.S.G Wang, M Baccarini, M Hu, J The dimer-dependent catalytic activity of RAF family kinases is revealed through characterizing their oncogenic mutants
description	10.1038/s41388-018-0365-2
author2	PHYSIOLOGY
author_facet	PHYSIOLOGY Yuan, J Ng, W.H Lam, P.Y.P Wang, Y Xia, H Yap, J Guan, S.P Lee, A.S.G Wang, M Baccarini, M Hu, J
format	Article
author	Yuan, J Ng, W.H Lam, P.Y.P Wang, Y Xia, H Yap, J Guan, S.P Lee, A.S.G Wang, M Baccarini, M Hu, J
author_sort	Yuan, J
title	The dimer-dependent catalytic activity of RAF family kinases is revealed through characterizing their oncogenic mutants
title_short	The dimer-dependent catalytic activity of RAF family kinases is revealed through characterizing their oncogenic mutants
title_full	The dimer-dependent catalytic activity of RAF family kinases is revealed through characterizing their oncogenic mutants
title_fullStr	The dimer-dependent catalytic activity of RAF family kinases is revealed through characterizing their oncogenic mutants
title_full_unstemmed	The dimer-dependent catalytic activity of RAF family kinases is revealed through characterizing their oncogenic mutants
title_sort	dimer-dependent catalytic activity of raf family kinases is revealed through characterizing their oncogenic mutants
publisher	Nature Publishing Group
publishDate	2020
url	https://scholarbank.nus.edu.sg/handle/10635/175101
_version_	1821209476150067200

The dimer-dependent catalytic activity of RAF family kinases is revealed through characterizing their oncogenic mutants

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