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References from The current understanding of KRAS protein structure and dynamics. Local targets link to admitted publications; unresolved targets remain external evidence.
10.4161/sgtp.1.1.12178
10.4161/sgtp.1.1.12178 · External reference
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10.1016/j.cell.2017.06.009
10.1016/j.cell.2017.06.009 · External reference
RAS variant signalling
10.1042/bst20180173 · 2018 · External reference
10.1093/nar/gkq929
10.1093/nar/gkq929 · External reference
10.1146/annurev-biochem-062708-134043
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10.1016/0092-8674(90)90294-o
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10.1016/j.pep.2010.05.015
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10.1002/j.1460-2075.1982.tb01276.x
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10.1016/0968-0004(90)90281-f
10.1016/0968-0004(90)90281-f · External reference
10.1073/pnas.1404639111
10.1073/pnas.1404639111 · External reference
Regulating the regulator: post-translational modification of RAS
10.1038/nrm3255 · 2011 · External reference
K-Ras4B phosphorylation at Ser181 is inhibited by calmodulin and modulates K-Ras activity and function
10.1038/onc.2010.298 · 2010 · External reference
10.1158/0008-5472.can-13-1750
10.1158/0008-5472.can-13-1750 · External reference
10.1126/scisignal.2001518
10.1126/scisignal.2001518 · External reference
10.1073/pnas.1201487109
10.1073/pnas.1201487109 · External reference
10.1515/hsz-2016-0118
10.1515/hsz-2016-0118 · External reference
10.1038/s41598-019-46846-w
10.1038/s41598-019-46846-w · External reference
10.1016/j.semcancer.2017.12.005
10.1016/j.semcancer.2017.12.005 · External reference
10.1038/nrc.2017.36
10.1038/nrc.2017.36 · External reference
510 first to inhibit “Undruggable” KRAS
10.1158/2159-8290.cd-nb2019-073 · 2019 · External reference
The clinical KRAS(G12C) inhibitor AMG 510 drives anti-tumour immunity
2019 · External reference
10.1242/jcs.182873
10.1242/jcs.182873 · External reference
10.1371/journal.pcbi.1006458
10.1371/journal.pcbi.1006458 · External reference
10.1016/j.ccr.2014.02.017
10.1016/j.ccr.2014.02.017 · External reference
10.1038/s41467-017-01519-y
10.1038/s41467-017-01519-y · External reference
10.1016/j.trecan.2017.08.006
10.1016/j.trecan.2017.08.006 · External reference
Protein Data Bank: the single global archive for 3D macromolecular structure data
2018 · External reference
Structural basis of recognition of farnesylated and methylated KRAS4b by PDEδ
10.1073/pnas.1615316113 · 2016 · External reference
Oncogenic and RASopathy-associated K-RAS mutations relieve membrane-dependent occlusion of the effector-binding site
10.1073/pnas.1419895112 · 2015 · External reference
10.1021/acs.biochem.7b00271
10.1021/acs.biochem.7b00271 · External reference
Inhibition of K-RAS4B by a unique mechanism of action: stabilizing membrane-dependent occlusion of the effector-binding site
10.1016/j.chembiol.2018.07.009 · 2018 · External reference
10.1038/nature12796
10.1038/nature12796 · External reference
Targeting KRAS mutant cancers with a covalent G12C-specific inhibitor
10.1016/j.cell.2018.01.006 · 2018 · External reference
10.1073/pnas.1811360116
10.1073/pnas.1811360116 · External reference
10.1021/acs.jcim.7b00399
10.1021/acs.jcim.7b00399 · External reference
10.1038/ncomms16111
10.1038/ncomms16111 · External reference
10.1038/s41594-018-0061-5
10.1038/s41594-018-0061-5 · External reference
10.1038/s41467-019-10419-2
10.1038/s41467-019-10419-2 · External reference
10.1007/s10858-014-9849-8
10.1007/s10858-014-9849-8 · External reference
10.1021/acsmedchemlett.8b00382
10.1021/acsmedchemlett.8b00382 · External reference
10.1002/anie.201201358
10.1002/anie.201201358 · External reference
K-Ras populates conformational states differently from its isoform H-Ras and oncogenic mutant K-RasG12D
1993 · External reference
An engineered protein antagonist of K-Ras/B-Raf interaction
10.1038/s41598-017-05889-7 · 2017 · External reference
Discovery of N-(1-Acryloylazetidin-3-yl)-2-(1H-indol-1-yl)acetamides as covalent inhibitors of KRASG12C
10.1021/acsmedchemlett.9b00258 · 2019 · External reference
10.1074/jbc.m117.816348
10.1074/jbc.m117.816348 · External reference
10.1073/pnas.1812963116
10.1073/pnas.1812963116 · External reference
10.1073/pnas.1908353116
10.1073/pnas.1908353116 · External reference
Isoform-specific destabilization of the active site reveals a molecular mechanism of intrinsic activation of KRas G13D
10.1016/j.celrep.2019.07.026 · 2019 · External reference
10.1107/s2059798317015418
10.1107/s2059798317015418 · External reference
10.1073/pnas.1116510109
10.1073/pnas.1116510109 · External reference
10.1074/jbc.ra119.009131
10.1074/jbc.ra119.009131 · External reference
Multivalent small-molecule Pan-RAS inhibitors
10.1016/j.cell.2017.02.006 · 2017 · External reference
10.1021/acsmedchemlett.7b00128
10.1021/acsmedchemlett.7b00128 · External reference
10.1021/acs.biochem.7b00974
10.1021/acs.biochem.7b00974 · External reference
10.1073/pnas.1904529116
10.1073/pnas.1904529116 · External reference
Ras binder induces a modified switch-II pocket in GTP and GDP states
10.1016/j.chembiol.2017.08.025 · 2017 · External reference
KRAS binders hidden in nature
2019 · External reference
BRET-based RAS biosensors that show a novel small molecule is an inhibitor of RAS-effector protein-protein interactions
2018 · External reference
10.1038/s41467-018-05707-2
10.1038/s41467-018-05707-2 · External reference
KRAS G12C drug development: discrimination between Switch II pocket configurations using hydrogen/deuterium-exchange mass spectrometry
1993 · External reference
Potent and selective covalent quinazoline inhibitors of KRAS G12C
10.1016/j.chembiol.2017.06.017 · 2017 · External reference
10.1021/acsmedchemlett.6b00373
10.1021/acsmedchemlett.6b00373 · External reference
Atypical KRASG12R mutant is impaired in PI3K signaling and macropinocytosis in pancreatic cancer
2019 · External reference
10.1158/2159-8290.cd-18-1220
10.1158/2159-8290.cd-18-1220 · External reference
The basis for K-Ras4B binding specificity to protein farnesyltransferase revealed by 2 A resolution ternary complex structures
1993 · External reference
10.1038/nature00986
10.1038/nature00986 · External reference
10.1093/emboj/cdg571
10.1093/emboj/cdg571 · External reference
10.1158/2159-8290.cd-15-1105
10.1158/2159-8290.cd-15-1105 · External reference
Protein-protein crystal-packing contacts
10.1002/pro.5560061021 · 1997 · External reference
Crystal packing effects on protein loops
10.1002/prot.20492 · 2005 · External reference
LiteMol suite: interactive web-based visualization of large-scale macromolecular structure data
10.1038/nmeth.4499 · 2017 · External reference
10.1093/nar/gkv1047
10.1093/nar/gkv1047 · External reference
10.1021/bi970296u
10.1021/bi970296u · External reference
10.1073/pnas.081441398
10.1073/pnas.081441398 · External reference
10.1074/jbc.m110.145235
10.1074/jbc.m110.145235 · External reference
10.1038/s41467-018-08115-8
10.1038/s41467-018-08115-8 · External reference
10.1158/0008-5472.can-17-2727
10.1158/0008-5472.can-17-2727 · External reference
10.1016/j.bpj.2017.10.042
10.1016/j.bpj.2017.10.042 · External reference
10.1021/jacs.7b06292
10.1021/jacs.7b06292 · External reference
10.1016/j.str.2015.04.019
10.1016/j.str.2015.04.019 · External reference
Organization of farnesylated, carboxymethylated KRAS4B on membranes
10.1016/j.jmb.2019.07.025 · 2019 · External reference
Oncogenic KRas mobility in the membrane and signaling response
2019 · External reference
10.1016/j.drudis.2016.07.001
10.1016/j.drudis.2016.07.001 · External reference
10.1038/nature06522
10.1038/nature06522 · External reference
10.1016/j.bbagen.2013.07.024
10.1016/j.bbagen.2013.07.024 · External reference
10.1002/prot.24805
10.1002/prot.24805 · External reference
10.1074/jbc.m117.778886
10.1074/jbc.m117.778886 · External reference
10.1007/s00018-017-2564-3
10.1007/s00018-017-2564-3 · External reference
10.1016/j.bpj.2015.09.034
10.1016/j.bpj.2015.09.034 · External reference
The higher level of complexity of K-Ras4B activation at the membrane
2016 · External reference
GTP binding and oncogenic mutations may attenuate hypervariable region (HVR)-catalytic domain interactions in small GTPase K-Ras4B, exposing the effector binding site
10.1074/jbc.m115.664755 · 2015 · External reference
10.1021/acs.jpcb.5b11110
10.1021/acs.jpcb.5b11110 · External reference
10.1016/j.bpj.2016.01.019
10.1016/j.bpj.2016.01.019 · External reference
Computational modeling reveals that signaling lipids modulate the orientation of K-Ras4A at the membrane reflecting protein topology
1993 · External reference
10.1016/j.bpj.2018.12.011
10.1016/j.bpj.2018.12.011 · External reference
Probing the conformational and energy landscapes of KRAS membrane orientation
10.1021/acs.jpcb.9b05796 · 2019 · External reference
10.1002/prot.25317
10.1002/prot.25317 · External reference
Oncogenic G12D mutation alters local conformations and dynamics of K-Ras
10.1038/s41598-019-48029-z · 2019 · External reference
The structural basis of oncogenic mutations G12, G13 and Q61 in small GTPase K-Ras4B
10.1038/srep21949 · 2016 · External reference
10.1021/jacs.7b12191
10.1021/jacs.7b12191 · External reference
10.1039/c9cp00101h
10.1039/c9cp00101h · External reference
10.1039/c8sc04498h
10.1039/c8sc04498h · External reference
The structural basis of the farnesylated and methylated KRas4B interaction with calmodulin
10.1016/j.str.2019.08.009 · 2019 · External reference
10.1038/nrd.2018.77
10.1038/nrd.2018.77 · External reference
Is Nanoclustering essential for all oncogenic KRas pathways? can it explain why wild-type KRas can inhibit its oncogenic variant?
2019 · External reference
10.1038/nchembio.1435
10.1038/nchembio.1435 · External reference
Best practices for foundations in molecular simulations [Article v1.0]
10.33011/livecoms.1.1.5957 · 2018 · External reference
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2018 · External reference
10.1016/j.sbi.2014.04.002
10.1016/j.sbi.2014.04.002 · External reference
10.1021/jp0477147
10.1021/jp0477147 · External reference
Finite-size-corrected rotational diffusion coefficients of membrane proteins and carbon nanotubes from molecular dynamics simulations
10.1021/acs.jpcb.9b01656 · 2019 · External reference
