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1 SAEHGSLH, corresponded to legumin, the main seed protein.
2 ds, but substantially diluted (13)C label in seed protein.
3 nanobodies (VHHs) against native Arabidopsis seed proteins.
4 library against native Arabidopsis thaliana seed proteins.
5 articularly to L. albus and L. angustifolius seed proteins.
6 lation and characterization of less abundant seed proteins.
7 ant storage proteins and a few less-abundant seed proteins.
8 interaction data, building out from selected seed proteins.
10 capacity of peptides released from amaranth seed proteins after enzymatic digestion, against dipepti
11 showed significant increases or decreases in seed protein and oil content across multiple generations
12 is one of the most important crop plants for seed protein and oil content, and for its capacity to fi
14 eliable methods for 2D separation of soybean seed proteins and subsequent identification by mass spec
20 n (Lupinus albus L.) is a valuable source of seed protein, carbohydrates and oil, but requires geneti
24 plants during seed fill did not alter final seed protein content of antisense lines compared with co
27 nificant increase in isoaspartyl residues in seed proteins coupled with reduced germination vigor und
31 essing the inhibitory potential of the major seed protein fractions from eight selected legume specie
32 enomic clone encoding a 22 kDa alpha-kafirin seed protein from sorghum, were translationally fused to
33 The promoter for the phaseolin (phas) bean seed protein gene adopts an inactive chromatin structure
36 lack of a collateral alteration of any other seed protein in the Gly m Bd 30 K-silenced seeds support
42 d to decreased silique and seed numbers, but seed protein levels were unchanged, demonstrating the im
44 red PrP(Sc) molecules retain the activity to seed protein misfolding cyclic amplification (PMCA) reac
46 selection of a drying process to yield chia seed protein powders with more desirable functionality.
47 ts did not exhibit overt toxicity, the major seed proteins primarily associated with nutrient storage
50 hypothesized to perform a unique function in seed protein processing, but we demonstrated previously
52 , which has high potential to provide stable seed protein production in a broad range of environments
54 r but sterile when the seed-specific unknown seed protein promoter or the Cauliflower mosaic virus 35
56 anelles are taken up into vacuoles where, in seed protein storage vacuoles, they form a membrane-cont
57 Many genes encoding important classes of seed proteins, such as storage proteins, oil biosynthesi
58 Together, these results demonstrate that seed protein synthesis and seed weight is dependent on N
59 on the phaseolin (phas) gene that encodes a seed protein to show how chromatin structure interacts w
63 ids and amino acids (after hydrolysis of the seed proteins) was determined by gas chromatography/mass
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