ABCD1 p.Ser514Asn
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PMID: 22045812
[PubMed]
Hillebrand M et al: "Identification of a new fatty acid synthesis-transport machinery at the peroxisomal membrane."
No.
Sentence
Comment
231
We analyzed, whether five missense mutations in the ABCD1 gene known to be associated with near normal ALDP protein amounts (G116R, S514N, G607D, G629H, and T693M) would induce edgetic perturbations by altering ALDP homo-oligomerization or the interaction of ALDP with FASN, ACLY, or FATP4 (Fig. 5).
X
ABCD1 p.Ser514Asn 22045812:231:12
status: NEWX
ABCD1 p.Ser514Asn 22045812:231:132
status: NEW232 Two mutations, S514N and G629H, led to a reduction of the BRET ratio related to ALDP homo-oligomerization.
X
ABCD1 p.Ser514Asn 22045812:232:15
status: NEW233 Conversely, S514N and G607D increased the BRET ratio for the interaction of ALDP with FASN, whereas G116R had the same effect on the interaction between ALDP and ACLY.
X
ABCD1 p.Ser514Asn 22045812:233:12
status: NEW273 WT ALDP was compared with ALDP constructs representing disease-causing missense mutations (G116R, S514N, G607D, G629H, and T693M); homomeric interactions as well as interactions with FASN, ACLY, and FATP4 were determined.
X
ABCD1 p.Ser514Asn 22045812:273:98
status: NEW300 We showed that three of these mutations, G116R, S514N, and G607D, induced edgetic perturbations of PPI by exerting partly countervailing effects on ALDP homo-oligomerization and the interaction between ALDP and FASN and ALDP and ACLY, respectively.
X
ABCD1 p.Ser514Asn 22045812:300:48
status: NEW227 We analyzed, whether five missense mutations in the ABCD1 gene known to be associated with near normal ALDP protein amounts (G116R, S514N, G607D, G629H, and T693M) would induce edgetic perturbations by altering ALDP homo-oligomerization or the interaction of ALDP with FASN, ACLY, or FATP4 (Fig. 5).
X
ABCD1 p.Ser514Asn 22045812:227:132
status: NEW228 Two mutations, S514N and G629H, led to a reduction of the BRET ratio related to ALDP homo-oligomerization.
X
ABCD1 p.Ser514Asn 22045812:228:15
status: NEW229 Conversely, S514N and G607D increased the BRET ratio for the interaction of ALDP with FASN, whereas G116R had the same effect on the interaction between ALDP and ACLY.
X
ABCD1 p.Ser514Asn 22045812:229:12
status: NEWX
ABCD1 p.Ser514Asn 22045812:229:132
status: NEW269 WT ALDP was compared with ALDP constructs representing disease-causing missense mutations (G116R, S514N, G607D, G629H, and T693M); homomeric interactions as well as interactions with FASN, ACLY, and FATP4 were determined.
X
ABCD1 p.Ser514Asn 22045812:269:98
status: NEW296 We showed that three of these mutations, G116R, S514N, and G607D, induced edgetic perturbations of PPI by exerting partly countervailing effects on ALDP homo-oligomerization and the interaction between ALDP and FASN and ALDP and ACLY, respectively.
X
ABCD1 p.Ser514Asn 22045812:296:48
status: NEW230 Two mutations, S514N and G629H, led to a reduction of the BRET ratio related to ALDP homo-oligomerization.
X
ABCD1 p.Ser514Asn 22045812:230:15
status: NEW271 WT ALDP was compared with ALDP constructs representing disease-causing missense mutations (G116R, S514N, G607D, G629H, and T693M); homomeric interactions as well as interactions with FASN, ACLY, and FATP4 were determined.
X
ABCD1 p.Ser514Asn 22045812:271:98
status: NEW298 We showed that three of these mutations, G116R, S514N, and G607D, induced edgetic perturbations of PPI by exerting partly countervailing effects on ALDP homo-oligomerization and the interaction between ALDP and FASN and ALDP and ACLY, respectively.
X
ABCD1 p.Ser514Asn 22045812:298:48
status: NEW