「Proline」の共起表現一覧(1語右で並び替え)

Proline

1語右で並び替え

該当件数:63件

  • ns with high proportions of alanine, glycine, proline, and glutamic acid.
  • DBP is a member of the PAR bZIP ( Proline and Acidic amino acid-Rich basic leucine ZIPp
  • ric repulsion due to the pyrrolidone rings of proline and hydroxyproline residues.
  • nherited cause of excess urinary excretion of proline and glycine, similar to that found in iminogl
  • transporters for monoamines, the amino acids proline and glycine, GABA, and a group of orphan tran
  • e high-affinity renal transporter of glycine, proline and hydroxyproline found to be defective in b
  • The pathways linking arginine, glutamine, and proline are bidirectional.
  • only proteinogenic amino acid of this type is proline) are sometimes named imino acids, though this
  • This enzyme begins the process of degrading proline by starting the reaction that converts it to
  • somal dominant retinitis pigmentosa, in which proline changed to alanine.
  • In enzymology, a proline dehydrogenase (EC 1.5.99.8) is an enzyme that
  • I homing endonuclease / maturase and the PutA proline dehydrogenase / transcription factor, have be
  • Proline derivative 3d is prepared in a separate leg f
  • This boroxine reacts with the proline derivative (3d) to form the basic oxazaboroli
  • Protegrin-5 substitutes a proline for an arginine with one less positive charge
  • PELP-1 ( proline, glutamic acid and leucine rich protein 1) PE
  • ssue is collagen, which is made up of lysine, proline, glycine, alanine, and other amino acids .
  • oradrenaline/adrenaline, dopamine, serotonin, proline, glycine, choline, betaine and taurine.
  • Each residue of the protein (except proline) has an amide proton attached to a nitrogen i
  • bromination, amidation of the C-terminus, and proline hydroxylation.
  • although some AT-hooks contain only a single proline in the core sequence.
  • ne altered ALDH4A1 gene have normal levels of proline in their blood.
  • β-Casomorphin 8 that has histidine instead of proline in position 8, depending on whether it is der
  • PRODH gene have moderately elevated levels of proline in their blood, but these levels do not cause
  • Proline is often seen immediately following the end o
  • Because proline is cheaply available in high optical purity,
  • ct biosynthetical precursor to the amino acid proline is the imino acid (S)-Δ1-pyrroline-5-carboxyl
  • n of codon 23 in the rhodopsin gene, in which proline is changed to histidine, accounts for the lar
  • ain many Gly-X-Y sequences, where X and Y are proline, isoleucine, or hydroxylysine; they, therefor
  • Hyperprolinemia type II results in proline levels in the blood between 10 and 15 times h
  • This enzyme participates in arginine and proline metabolism and aminoacyl-trna biosynthesis.
  • etabolism, glutamate metabolism, arginine and proline metabolism, and nitrogen metabolism.
  • This enzyme participates in arginine and proline metabolism.
  • ates in glutamate metabolism and arginine and proline metabolism.
  • ipates in lysine degradation and arginine and proline metabolism.
  • lucuronate interconversions, and arginine and proline metabolism.
  • PROLINO" or "ProliNO") is the abbreviation of proline nitric oxide or proline NO.
  • iad (where Xaa and Yaa are any amino acid), a proline occupying the Yaa position is hydroxylated to
  • Other names in common use include proline oxidase, L-proline oxidase, 1-pyrroline-5-car
  • in the PRODH gene, which codes for the enzyme proline oxidase.
  • Hydroxyproline and proline play key roles for collagen stability.
  • This modification of the proline residue increases the stability of the collag
  • ween the thermostability of a protein and its proline residue content.
  • he N-terminal amino acid from peptides with a proline residue in the penultimate position.
  • ) the site of cleavage is on either side of a proline residue, (iii) the N-terminal residue is lysi
  • Proline residues are known to be structure-breaking r
  • peptide bonds from trans form to cis form at proline residues and facilitates protein folding.
  • nt DNA technology, the penultimate lysine and proline residues on the C-terminal end of the B-chain
  • o peptidic bonds in protein (especially, like proline residues) and that is why it can precipitate
  • eaves peptide bonds at the C-terminal side of proline residues.
  • in folding chaperones for proteins containing proline residues.
  • ch domain, a pleckstrin homology domain and a proline rich region
  • m the N-terminal region of the protein PROL1 ( proline rich, lacrimal 1).
  • d, glycine, histidine, lysine, phenylalanine, proline, serine, and threonine belong to class-II syn
  • deficiency patients is caused by a leucine to proline substitution.
  • N-terminal domain is also found in the PROSC ( proline synthetase co-transcribed bacterial homolog)
  • ntaining tandem repeats rich in threonine and proline that varies between 50 and 115 copies in diff
  • ed structure suggests that it is derived from proline, the results from the experiments indicated t
  • ver, these atoms are both H-bond acceptors in proline; there is no H-bond donor due to the cyclic s
  • A change in codon 102 from proline to leucine on chromosome 20, has been found i
  • ase, prolyl-transfer ribonucleate synthetase, proline translase, prolyl-transfer ribonucleic acid s
  • Proline U100 in South Africa.
  • ol is obtained by reduction of the amino acid proline using lithium aluminium hydride.