A single structurally conserved SUMOylation site in CRMP2 controls NaV1.7 function.
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Tuning microtubule dynamics to enhance cancer therapy by modulating FER-mediated CRMP2 phosphorylation.SUMO on CRMPs - wrestling for pain?CRMP2-Neurofibromin Interface Drives NF1-related Pain.Chemical shift perturbation mapping of the Ubc9-CRMP2 interface identifies a pocket in CRMP2 amenable for allosteric modulation of Nav1.7 channelsCRMP2 and voltage-gated ion channels: potential roles in neuropathic pain
P2860
A single structurally conserved SUMOylation site in CRMP2 controls NaV1.7 function.
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2017 nî lūn-bûn
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2017年の論文
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2017年学术文章
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2017年学术文章
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A single structurally conserved SUMOylation site in CRMP2 controls NaV1.7 function.
@en
A single structurally conserved SUMOylation site in CRMP2 controls NaV1.7 function.
@nl
type
label
A single structurally conserved SUMOylation site in CRMP2 controls NaV1.7 function.
@en
A single structurally conserved SUMOylation site in CRMP2 controls NaV1.7 function.
@nl
prefLabel
A single structurally conserved SUMOylation site in CRMP2 controls NaV1.7 function.
@en
A single structurally conserved SUMOylation site in CRMP2 controls NaV1.7 function.
@nl
P2093
P2860
P50
P1433
P1476
A single structurally conserved SUMOylation site in CRMP2 controls NaV1.7 function
@en
P2093
Aubin Moutal
Erik Thomas Dustrude
Liberty François-Moutal
May Khanna
Samantha Perez-Miller
P2860
P304
P356
10.1080/19336950.2017.1299838
P577
2017-02-28T00:00:00Z