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1 d it extends preexisting chains initiated by glycogenin.
2 ff but this was eliminated by overexpressing glycogenin.
3 roblasts stably overexpressing rabbit muscle glycogenin.
4  chromosomal location of the gene coding for glycogenin.
5                                              Glycogenin-1 and glycogenin-2 interact with one another,
6 und heterozygous deleterious variants in the glycogenin-1 gene (GYG1).
7            Most patients showed depletion of glycogenin-1 in skeletal muscle, whereas 1 showed presen
8 keletal muscle, whereas 1 showed presence of glycogenin-1 lacking the C-terminal that normally binds
9 ur results indicate that either depletion of glycogenin-1 or impaired interaction with glycogen synth
10 lso expressed the muscle form of glycogenin (glycogenin-1), which was attached to a chromatographical
11 etion in skeletal muscle and accumulation of glycogenin-1.
12 and human RD-ES cell extracts also contained glycogenin-1.
13 to self-glucosylate but not to interact with glycogenin-1.
14 ion of novel forms of glycogenin, designated glycogenin-2 (GN-2), encoded by a second gene that is ex
15 portant since it indicates that the level of glycogenin-2 can determine glycogen accumulation and hen
16 e explains much of the observed diversity in glycogenin-2 cDNA sequences as being due to alternate ex
17                         Cloning of the human glycogenin-2 gene, GYG2, has revealed the presence of 11
18                    Cloning of cDNAs encoding glycogenin-2 indicated the existence of multiple species
19                             Glycogenin-1 and glycogenin-2 interact with one another, based on in vitr
20                                              Glycogenin-2 is a recently described self-glucosylating
21                                              Glycogenin-2 is one of two self-glucosylating proteins i
22                                              Glycogenin-2 maps between the microsatellite anchor mark
23 stent with mapping information obtained from glycogenin-2 STS sequences.
24                       Mutation of Tyr-196 in glycogenin-2 to a Phe residue abolished the ability of g
25 -2 to a Phe residue abolished the ability of glycogenin-2 to self-glucosylate but not to interact wit
26                                              Glycogenin-2 was found in Ewing's sarcoma RD-ES cells wh
27         In human liver extracts, most of the glycogenin-2 was only detectable after treatment with al
28                     Stable overexpression of glycogenin-2alpha in Rat-1 fibroblast cells resulted in
29 action, the predominant isoform in liver was glycogenin-2beta.
30                                              Glycogenin, a self-glucosylating protein involved in the
31 nge in their intracellular localization; (b) glycogenin and elevated glucose have opposing effects on
32 have opposing effects on the distribution of glycogenin and glycogen synthase in rat 1 cells; and (c)
33                     Two of the cDNAs encoded glycogenin and glycogen synthase, respectively, proteins
34 e sequenced the cDNA coding for human muscle glycogenin and have deduced the corresponding amino acid
35 n apo-enzyme structure and a complex between glycogenin and UDP-glucose/Mn2+ were solved by molecular
36              By using rabbit skeletal muscle glycogenin as a bait, cDNAs encoding three different pro
37      Initiation of glucose polymerization by glycogenin autoglucosylation at Tyr-194 is required to p
38  Overall, GN-2 has 40-45% identity to muscle glycogenin but is 72% identical over a 200-residue segme
39  gel electrophoresis revealed a continuum of glycogenin-containing species from low molecular mass to
40                                              Glycogenin contains a conserved DxD motif and an N-termi
41 and could support glycogen accumulation in a glycogenin-deficient yeast strain.
42 cribe the characterization of novel forms of glycogenin, designated glycogenin-2 (GN-2), encoded by a
43                            Overexpression of glycogenin did not affect total intracellular glycogen a
44       We conclude that (a) overexpression of glycogenin does not enhance glycogen synthesis but cause
45 eds by intersubunit glucosylation of dimeric glycogenin, even though it has not been demonstrated tha
46 vealed a diffuse cytoplasmic distribution of glycogenin expressed in rat 1 cells.
47 se- or [35S]methionine-labeled extracts from glycogenin-expressing cells by continuous polyacrylamide
48 ne structure is similar to that of the other glycogenin gene, GYG.
49 e forms complexes in solution with the yeast glycogenin Glg2p, but this interaction appears not to af
50 IEC3 cells also expressed the muscle form of glycogenin (glycogenin-1), which was attached to a chrom
51 ooperative action of glycogen synthase (GS), glycogenin (GN), and glycogen branching enzyme and forms
52 ll glucopolymerization capacity of monomeric glycogenin indicates that the enzyme is able to synthesi
53 of unknown function and was designated GNIP (glycogenin interacting protein).
54                                              Glycogenin is a glycosyltransferase that functions as th
55                                              Glycogenin is a self-glucosylating protein involved in t
56                                              Glycogenin is a self-glucosylating protein involved in t
57                                              Glycogenin is the autocatalytic, self-glucosylating prim
58                 The effect of increasing the glycogenin level on glycogen synthesis was studied in ra
59 ral related proteins, GUX2 to GUX5 and Plant Glycogenin-like Starch Initiation Protein6, are Golgi lo
60 s II includes galactinol synthases and plant glycogenin-like starch initiation proteins that are not
61 tent (MSAE) produced by the non-glucosylated glycogenin monomer is 13.3 +/- 1.9 glucose units, simila
62                 The MSAE of non-glucosylated glycogenin produced by dimer intrasubunit glucosylation
63 and in addition GNIP2 was shown to stimulate glycogenin self-glucosylation 3-4-fold.
64 the bound UDP-glucose far from Tyr194 in the glycogenin structure raises questions as to the mechanis
65            Unlike the mammalian counterpart, glycogenin, the yeast Glg proteins appear to require mul
66           To identify possible regulators of glycogenin, the yeast two-hybrid strategy was employed.
67              However, partially glucosylated glycogenin was able to almost complete its autoglucosyla
68 he presence of glucose, all of the expressed glycogenin was attached to polysaccharide and the free p
69       Physical interaction between GNIP2 and glycogenin was confirmed by co-immunoprecipitation, and
70                             The structure of glycogenin was solved in two different crystal forms.
71 hesis is initiated by a specialized protein, glycogenin, which has the unusual property of transferri
72 the intramonomer glucosylation capability of glycogenin without determining the extent of autoglucopo

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