ライフサイエンスコーパス: coatomer protein

1 alpha-adaptin; clathrin heavy chain; or beta-coatomer protein.

2 COP subunit of COPI (coat protein complex I) coatomer proteins.

3 ctive RACK, which was identified as the COPI coatomer protein, beta'-COP.

4 embles classic coat protein complex I (COPI) coatomer protein-binding KKXX signals, and indeed the di

5 GBF1 is mainly involved in the formation of coatomer protein complex (COPI) vesicles, maintenance an

6 COPZ1 encodes a subunit of coatomer protein complex 1 (COPI) involved in intracellu

7 recombinant SBP-AR and the ligand-sensitive coatomer protein complex I (COPI) retrograde trafficking

8 used by autosomal recessive mutations in the coatomer protein complex I (COPI) subunit zeta 1 (COPZ1)

9 the addition of cytosolic proteins including coatomer protein complex I (COPI) to the reaction mixtur

10 In this report, we identify the coatomer protein complex I (COPI) vesicle coat as a crit

11 This mutation abolished interaction with the coatomer protein complex I coatomer and resulted in accu

12 Given the known role of the coatomer protein complex I, we speculate that loss of CO

13 tivating protein (SCAP).SREBP-1c complex for coatomer protein complex II (COPII) vesicles.

14 the C1 cassette or by the presence of a PDZ/coatomer protein complex II-binding domain in the C2' ca

15 COPI is a coatomer protein complex responsible for intracellular p

16 Mutations in the N-terminal WD40 domain of coatomer protein complex subunit alpha (COPA) cause a ty

17 disorder caused by missense mutations in the coatomer protein complex subunit alpha (COPA) gene.

18 ynthetic T1 peptides the specific binding of coatomer protein complex subunit beta to this region of

19 ction-based genomic screening identified the coatomer protein complex zeta1 (COPZ1) gene as essential

20 of COPZ1, but not of COPZ2 encoding isoform coatomer protein complex zeta2, caused Golgi apparatus c

21 FLNB (filamin B, beta) and hypoedited COPA (coatomer protein complex, subunit alpha).

22 ion in a WD40 domain of the highly conserved Coatomer Protein Complex, Subunit Beta 2 (COPB2).

23 d to initiate the formation of clathrin- and coatomer protein (COP) I-coated vesicles on these membra

24 her H89 might act at the level of either the coatomer protein (COP)I or the COPII coat protein comple

25 140-kDa protein was the alpha-COP subunit of coatomer protein COPI, usually associated with trans-Gol

26 evidence has suggested that subunits of the coatomer protein (COPI) complexes are functionally assoc

27 SNAREs are also thought to prime coatomer protein I (COPI) assembly to ensure incorporati

28 These motifs were required to bind the coatomer protein I (COPI) complex, a vesicle coat comple

29 adaptor protein 1 (AP1) complex subunits and coatomer protein I (COPI) proteins, no longer promoted m

30 The COPa and COPb proteins of the coatomer protein I (COPI) vesicle complex were reported

31 Inhibition of the putative coatomer protein I (COPI) vesicle tethering complex, gia

32 Based on recent data showing that coatomer protein I (COPI) vesicle transport is involved

33 in the hKOPR C-tail decreased interaction of coatomer protein I (COPI) with the hKOPR and abolished 1

34 tif was responsible for the interaction with coatomer protein I (COPI), which was inversely correlate

35 the cell surface expression by mediating the coatomer protein I complex-dependent retrograde transpor

36 (ER) and must be transported to the Golgi in coatomer protein II (COPII) vesicles where two sequentia

37 protein, which is an essential component of coatomer protein II (COPII)-mediated cargo transport fro

38 ER) is mediated by the SEC24C isoform of the coatomer protein-II complex.

39 d that decreased expression of the gammaCOPI coatomer protein led to 89% mortality in blood-fed mosqu

40 Heterozygous missense mutations in coatomer protein subunit alpha, COPA, cause a syndrome o

41 crosomes and partitions with subunits of the coatomer proteins that coat ER-to-Golgi transport vesicl

42 Coatomer proteins were identified as components of Vid v

43 ng suggests that all four subunits are proto-coatomer proteins, with important implications for BLOC-