Abstract
Abstract
Authors
Institutions
Provenance
crossref
Confidence 100%
pubmed
Confidence 98%
europepmc
Confidence 96%
openalex
Confidence 95%
unpaywall
Confidence 95%
doaj
Confidence 92%
datacite
Confidence 0%
No local reference links have been materialized yet.
No local citing links have been materialized yet.
10.4161/sgtp.1.1.12178
10.4161/sgtp.1.1.12178
10.1126/science.1062023
10.1126/science.1062023
10.1016/j.cell.2007.05.018
10.1016/j.cell.2007.05.018
10.1158/1541-7786.mcr-15-0203
10.1158/1541-7786.mcr-15-0203
10.1016/j.cell.2017.06.009
10.1016/j.cell.2017.06.009
RAS variant signalling
10.1042/bst20180173 · 2018
10.1093/nar/gkq929
10.1093/nar/gkq929
10.1146/annurev-biochem-062708-134043
10.1146/annurev-biochem-062708-134043
10.1016/0092-8674(90)90294-o
10.1016/0092-8674(90)90294-o
10.1016/j.pep.2010.05.015
10.1016/j.pep.2010.05.015
10.1038/sj.onc.1203818
10.1038/sj.onc.1203818
10.1002/j.1460-2075.1982.tb01276.x
10.1002/j.1460-2075.1982.tb01276.x
10.1016/0968-0004(90)90281-f
10.1016/0968-0004(90)90281-f
10.1073/pnas.1404639111
10.1073/pnas.1404639111
Regulating the regulator: post-translational modification of RAS
10.1038/nrm3255 · 2011
K-Ras4B phosphorylation at Ser181 is inhibited by calmodulin and modulates K-Ras activity and function
10.1038/onc.2010.298 · 2010
10.1158/0008-5472.can-13-1750
10.1158/0008-5472.can-13-1750
10.1126/scisignal.2001518
10.1126/scisignal.2001518
10.1073/pnas.1201487109
10.1073/pnas.1201487109
10.1515/hsz-2016-0118
10.1515/hsz-2016-0118
10.1038/s41598-019-46846-w
10.1038/s41598-019-46846-w
10.1016/j.semcancer.2017.12.005
10.1016/j.semcancer.2017.12.005
10.1038/nrc.2017.36
10.1038/nrc.2017.36
510 first to inhibit “Undruggable” KRAS
10.1158/2159-8290.cd-nb2019-073 · 2019
The clinical KRAS(G12C) inhibitor AMG 510 drives anti-tumour immunity
2019
10.1242/jcs.182873
10.1242/jcs.182873
10.1371/journal.pcbi.1006458
10.1371/journal.pcbi.1006458
10.1016/j.ccr.2014.02.017
10.1016/j.ccr.2014.02.017
10.1038/s41467-017-01519-y
10.1038/s41467-017-01519-y
10.1016/j.trecan.2017.08.006
10.1016/j.trecan.2017.08.006
Protein Data Bank: the single global archive for 3D macromolecular structure data
2018
Structural basis of recognition of farnesylated and methylated KRAS4b by PDEδ
10.1073/pnas.1615316113 · 2016
Oncogenic and RASopathy-associated K-RAS mutations relieve membrane-dependent occlusion of the effector-binding site
10.1073/pnas.1419895112 · 2015
10.1021/acs.biochem.7b00271
10.1021/acs.biochem.7b00271
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
10.1038/nature12796
10.1038/nature12796
Targeting KRAS mutant cancers with a covalent G12C-specific inhibitor
10.1016/j.cell.2018.01.006 · 2018
10.1073/pnas.1811360116
10.1073/pnas.1811360116
10.1021/acs.jcim.7b00399
10.1021/acs.jcim.7b00399
10.1038/ncomms16111
10.1038/ncomms16111
Finite-size-corrected rotational diffusion coefficients of membrane proteins and carbon nanotubes from molecular dynamics simulations
10.1021/acs.jpcb.9b01656 · doi-reference
10.1021/jp0477147
10.1021/jp0477147 · doi-reference
10.1016/j.sbi.2014.04.002
10.1016/j.sbi.2014.04.002 · doi-reference
Best practices for foundations in molecular simulations [Article v1.0]
10.33011/livecoms.1.1.5957 · doi-reference
10.1038/nchembio.1435
10.1038/nchembio.1435 · doi-reference
10.1038/nrd.2018.77
10.1038/nrd.2018.77 · doi-reference
The structural basis of the farnesylated and methylated KRas4B interaction with calmodulin
10.1016/j.str.2019.08.009 · doi-reference
10.1039/c9cp00101h
10.1039/c9cp00101h · doi-reference
10.1021/jacs.7b12191
10.1021/jacs.7b12191 · doi-reference
The structural basis of oncogenic mutations G12, G13 and Q61 in small GTPase K-Ras4B
10.1038/srep21949 · doi-reference
Oncogenic G12D mutation alters local conformations and dynamics of K-Ras
10.1038/s41598-019-48029-z · doi-reference
10.1002/prot.25317
10.1002/prot.25317 · doi-reference
Probing the conformational and energy landscapes of KRAS membrane orientation
10.1021/acs.jpcb.9b05796 · doi-reference
10.1016/j.bpj.2018.12.011
10.1016/j.bpj.2018.12.011 · doi-reference
10.1016/j.bpj.2016.01.019
10.1016/j.bpj.2016.01.019 · doi-reference
10.1021/acs.jpcb.5b11110
10.1021/acs.jpcb.5b11110 · doi-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 · doi-reference
10.1016/j.bpj.2015.09.034
10.1016/j.bpj.2015.09.034 · doi-reference
10.1007/s00018-017-2564-3
10.1007/s00018-017-2564-3 · doi-reference
10.1074/jbc.m117.778886
10.1074/jbc.m117.778886 · doi-reference
10.1002/prot.24805
10.1002/prot.24805 · doi-reference
10.1016/j.bbagen.2013.07.024
10.1016/j.bbagen.2013.07.024 · doi-reference
10.1038/nature06522
10.1038/nature06522 · doi-reference
10.1016/j.drudis.2016.07.001
10.1016/j.drudis.2016.07.001 · doi-reference
Organization of farnesylated, carboxymethylated KRAS4B on membranes
10.1016/j.jmb.2019.07.025 · doi-reference
10.1016/j.str.2015.04.019
10.1016/j.str.2015.04.019 · doi-reference
10.1021/jacs.7b06292
10.1021/jacs.7b06292 · doi-reference
10.1016/j.bpj.2017.10.042
10.1016/j.bpj.2017.10.042 · doi-reference
10.1158/0008-5472.can-17-2727
10.1158/0008-5472.can-17-2727 · doi-reference
10.1038/s41467-018-08115-8
10.1038/s41467-018-08115-8 · doi-reference
10.1074/jbc.m110.145235
10.1074/jbc.m110.145235 · doi-reference
10.1073/pnas.081441398
10.1073/pnas.081441398 · doi-reference
10.1021/bi970296u
10.1021/bi970296u · doi-reference
10.1093/nar/gkv1047
10.1093/nar/gkv1047 · doi-reference
LiteMol suite: interactive web-based visualization of large-scale macromolecular structure data
10.1038/nmeth.4499 · doi-reference
Crystal packing effects on protein loops
10.1002/prot.20492 · doi-reference
Protein-protein crystal-packing contacts
10.1002/pro.5560061021 · doi-reference
10.1158/2159-8290.cd-15-1105
10.1158/2159-8290.cd-15-1105 · doi-reference
10.1093/emboj/cdg571
10.1093/emboj/cdg571 · doi-reference
10.1038/nature00986
10.1038/nature00986 · doi-reference