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1 sed genomic map EcoMap7) near gadB (encoding glutamate decarboxylase).
2 ivity for gamma-aminobutyric acid (GABA) and glutamate decarboxylase.
3 e mice generated Abs against host insulin or glutamate decarboxylase.
4 caused increased levels of the GadA and GadB glutamate decarboxylases.
5 setting caused by epigenetic upregulation of glutamate decarboxylase 1 (GAD1), a regulator of the GAB
8 otein 1, synaptosomal-associated protein 29, glutamate decarboxylase 1, metabotropic glutamate recept
9 n of the gene for the GABA synthetic enzyme, glutamate decarboxylase 65 (GAD(65)), reduce basal corti
10 tion of gamma-aminobutyric acid synthesis by glutamate decarboxylase 65 (GAD65) in response to high i
11 gamma-aminobutyric acid-synthesizing enzyme glutamate decarboxylase 65 (GAD65) to presynaptic cluste
12 expression leads to decreased expression of glutamate decarboxylase 65 (GAD65), the enzyme required
14 amacrine cells (82%), was immunoreactive to glutamate decarboxylase 65, but no Per1 : :GFP(+) amacri
15 whether messenger RNA interference targeting glutamate decarboxylase 65/67 (GAD65/67) gene expression
16 r genes that may be related to regulation of glutamate decarboxylase 67 (GAD(67)), a marker for this
17 ynaptic density protein 95 (PSD95) and lower glutamate decarboxylase 67 (GAD67) expression in GluD1 K
18 The temporal and spatial distribution of glutamate decarboxylase 67 (GAD67) mRNA-containing neuro
19 ization with the interneuron-specific enzyme glutamate decarboxylase 67 (Gad67), but not other cell-t
20 al nAChR subunit mRNAs are co-expressed with glutamate decarboxylase 67 (GAD67), the marker for GABAe
23 f ARC neurons coexpress orexin receptors and glutamate decarboxylase-67 and are excited by orexin.
24 n-10 (IL-10), IL1 receptor 1, BDNF, NGF, and glutamate decarboxylase-67 in vitro using hypothalamic a
25 immunoreactive contacts with ChAT-, PV-, and glutamate decarboxylase-67-positive neurons that project
27 s is believed to be initiated by a change in glutamate decarboxylase activity, but the underlying mec
28 s suggest that GadC (XasA) participates in a glutamate decarboxylase alkalinization cycle to protect
29 is located downstream of gadA, which encodes glutamate decarboxylase, an enzyme involved in acid resi
30 ry gene gadE resulted in very high levels of glutamate decarboxylase and almost complete protection a
34 aminobutyric acid (GABA)ergic markers (GABA, glutamate decarboxylase) and to peptides and calcium bin
35 ase), bNOS (brain-type nitric oxidase), GAD (glutamate decarboxylase), and glial markers, and occasio
36 uble staining studies (using SMI-32 and anti-glutamate decarboxylase antibodies, both markers of cort
37 related to carbon isotope discrimination and glutamate decarboxylase associated with foliar nitrogen
38 regulates two genes that encode isoforms of glutamate decarboxylase critical to this system, but add
39 d2 mRNA in POMC neurons, as these encode the glutamate decarboxylase enzymes GAD67 and GAD65, respect
40 nsity of both the 65- and 67-kDa isoforms of glutamate decarboxylase (GAD(65) and GAD(67)) -immunorea
42 f mRNA encoding the 67-kilodalton isoform of glutamate decarboxylase (GAD(67)), an enzyme for GABA sy
43 then expressed three TCR specific for either glutamate decarboxylase (GAD) 206-220 or GAD 524-538 or
44 ine whether CGRP-containing neurons also had glutamate decarboxylase (GAD) and other markers for GABA
45 of evidence are presented to indicate that l-glutamate decarboxylase (GAD) can become membrane-associ
48 zes, which were colocalized with clusters of glutamate decarboxylase (GAD) immunoreactivity at rates
49 eads to persistent reductions in hippocampal glutamate decarboxylase (GAD) interneuron numbers withou
50 Two distinct cDNA clones encoding for the glutamate decarboxylase (GAD) isoenzymes GAD1 and GAD2 f
51 a microti possesses a potentially functional glutamate decarboxylase (GAD) system involved in extreme
52 n essential transcriptional activator of the glutamate decarboxylase (GAD) system, the most efficient
53 isiae homologue of the GABA-producing enzyme glutamate decarboxylase (GAD) that is required for norma
54 on of an immunodominant epitope derived from glutamate decarboxylase (GAD) was observed regardless of
56 ll bodies were identified by the presence of glutamate decarboxylase (GAD)-67 mRNA or glycine transpo
57 receptors were found to be co-localized with glutamate decarboxylase (GAD)-positive neurons (approxim
60 the cloned yhiX gene increased production of glutamate decarboxylases (GAD) and activated the transcr
61 mouse and human genes coding for the 67 kDa glutamate decarboxylase (Gad1) also contain binding site
62 ate transporters (vglut1, vglut2.1, vglut3), glutamate decarboxylases (gad1, gad2), and choline acety
65 n localizing the two GABA-producing forms of glutamate decarboxylase (GAD65 and GAD67) in the normal
67 ated that a spontaneous Th1 response against glutamate decarboxylase (GAD65) arises in NOD mice at fo
68 -cell responses to the beta-cell autoantigen glutamate decarboxylase (GAD65), induced an active form
69 mice had no spontaneous responses to 65-kDa glutamate decarboxylase (GAD65), its immunodominant pept
71 h corresponding reductions in this region of glutamate decarboxylase (GAD65/67) and markers of dendri
72 earliest times of detection for two forms of glutamate decarboxylase (GAD67 and GAD65) in the embryon
73 -related genes such as the 67 kDa isoform of glutamate decarboxylase (GAD67) and parvalbumin (PV), ap
74 protein levels of tyrosine hydroxylase (TH), glutamate decarboxylase (GAD67), and vesicular glutamate
75 orescence studies using antibodies to TH and glutamate decarboxylase (GAD67), the synthetic enzyme fo
77 els for Lhx6, parvalbumin, somatostatin, and glutamate decarboxylase (GAD67; the principal enzyme in
79 esistance system encompasses two isoforms of glutamate decarboxylase (gadA and gadB) and a putative g
80 tection at pH 2.5, one of two genes encoding glutamate decarboxylase (gadA or gadB), and the gene enc
81 smid with a 3.1-kb insert that contained the glutamate decarboxylase (gadA) and D-alanine racemase (a
82 and autoantibody responses to insulin (IAA), glutamate decarboxylase (GADA), IA-2, IA-2beta, and ZnT8
83 y-negative on the basis of existing markers [glutamate decarboxylase (GADA), protein tyrosine phospha
85 efficient and most studied uses isozymes of glutamate decarboxylase (GadA/GadB) to consume intracell
86 n the acid challenge media and relies on two glutamate decarboxylases (GadA and B) combined with a pu
89 ly development, and GABA is generated by the glutamate decarboxylase, GadB, during growth and in earl
92 ow that UNC-30 directly regulates the unc-25/glutamate decarboxylase gene that encodes the enzyme for
93 ing the expression and activity of three tea glutamate decarboxylase genes (CsGAD1, 2, and 3), and th
94 aminase under anaerobiosis; in addition, the glutamate decarboxylase genes gadA and gadB were induced
95 major autoantigens are established (insulin, glutamate decarboxylase, IA2, and zinc transporter-8), b
101 e-specific transcription of mouse and cattle glutamate decarboxylase-like protein 1 (GADL1) and the b
102 nd part of the promoter of the gene encoding glutamate decarboxylase-like protein 1 (GADL1) in 94 pat
103 ults suggest that three distinct moieties of glutamate decarboxylase localize to membrane compartment
104 mma-aminobutyric acid-synthesizing enzyme, l-glutamate decarboxylase (MGAD), is regulated by the vesi
105 t acid stress by increasing the synthesis of glutamate decarboxylase, presumably by increasing the le
107 lt, more glutamate becomes accessible to the glutamate decarboxylase reaction to yield gamma-aminobut
108 subpopulation of neurons; immunostaining for glutamate decarboxylase revealed the responding neurons
109 ansporter GlyT2 and the intracellular enzyme glutamate decarboxylase supply the majority of glycine a
110 showed that this defect is due to decreased glutamate decarboxylase synthesis, probably caused by el
111 21a-AR-Ss, by inserting Shigella glutaminase-glutamate decarboxylase systems coexpressed with S. sonn
114 aminobutyric acid (GABA)-synthesizing enzyme glutamate decarboxylase, which is present in inhibitory
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