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1 serine protease, Cupin, BetV1, Expansin and Prolamin).
2 y the identification of a new class of wheat prolamins.
3 isorder resulting from intolerance to cereal prolamins.
4 r, quinoa seed contains low concentration of prolamins (0.5-7% of total protein) making it suitable f
6 levels of 3.1% albumin, 0.3% globulins, 2.2% prolamin, 3.5% glutelin and 70.1% insoluble proteins.
8 8 cM genetic interval and harboring multiple prolamin and resistance-like gene families, was analyzed
11 g of RNAs that encode rice storage proteins, prolamines and glutelins to specific sub-domains of the
12 the storage proteins of rice (Oryza sativa), prolamines and glutelins, which are stored as inclusions
13 The presence of similar PSVs also containing prolamins and large systems of intravacuolar membranes i
17 youngest and largest gene family, the alpha prolamins, arose about 22-26 million years ago (Mya) aft
21 dosperm-expressed DNA-binding proteins, PBF (prolamin box-binding factor) and OHP1 (O2-heterodimerizi
23 ters contain a conserved cis-element, called prolamin-box (P-box), recognized by the trans-activator
24 oned an endosperm-specific maize cDNA, named prolamin-box binding factor (PBF), that encodes a member
25 gliadins and gamma3-hordeins form a distinct prolamin branch that existed separate from the gamma-gli
29 RNAs for the storage proteins, glutelins and prolamines, contain zipcode sequences, which target them
31 this protein to be located at the surface of prolamin-containing protein bodies, similar to other gam
32 that confer toxicity to gliadin and related prolamins continue to be defined, as do methods of asses
33 76.4% reduction in the amount of immunogenic prolamins, demonstrating the possibility of developing w
34 proteins (albumin, globulins, glutelin, and prolamins), drastically declined, resulting in poor-qual
35 imed to determine the amount of celiac-toxic prolamin epitopes in quinoa cultivars from different reg
37 was more soluble at room temperature whereas prolamin fraction presented high solubility at 70 degree
38 hermore, it was found that peptides from the prolamin fraction were characterised by the highest anti
41 adable and low-cost material such as zein, a prolamin from maize, and in combination with glycerol as
42 s been constructed for maize inbred B73, all prolamin gene copies can be identified in their chromoso
49 stand the structure and expression of cereal prolamin genes is demonstrated by the identification of
58 and DPF albumin (n = 12), globulin (n = 11), prolamin (n = 5) and glutelin (n = 17) had interaction w
60 oteins and similar alcohol-soluble proteins (prolamines) of barley and rye in genetically susceptible
61 gluten and similar alcohol-soluble proteins (prolamines) of barley and rye in genetically susceptible
62 enzymes and golgi body recycling as well as prolamin precursor proteins involved in refolding of pro
65 ic rye cultivar mixture were tested yielding prolamins (PROL), glutelins (GLUT), gluten (G) and aceto
69 rther applied for the modification of cereal prolamin proteins, since it appears to be a potential al
70 rongest correlations were found between the "prolamin/punicalagin-2" ratio and turbidity (r = 0.997)
71 Our analysis indicates that the insertion of prolamin-related genes occurred prior to the separation
75 ranscriptome, demonstrating variation in the prolamin superfamily and immune-reactive proteins across
76 es, the bulk of amino acids is stored in the prolamin superfamily that specifically accumulates in se
79 ection of aptamers for these water insoluble prolamins that was achieved choosing the immunodominant
80 t from the Andes, with low concentrations of prolamins, that has been recommended as part of a gluten
82 s to an estimated conversion factor from rye prolamins to gluten of 1.2, instead of the usual factor
83 high specificity, detecting the other three prolamins toxic for celiac patients and not showing cros
84 isolated protein-starch systems, indicating prolamins unravelled and complexed with PA during heatin
87 ated the interaction between GUB and zein, a prolamin with self-assembling property, using multiple s
88 Mechanisms responsible for the retention of prolamines within the ER lumen and their assembly into i
89 , starchy endosperm with a reduced amount of prolamin (zein) proteins and twice the lysine content of