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1 ed the LBD preference for l-Glu but also for sulfur-containing amino acids.
2 ocyanin, which possesses a minimal number of sulfur-containing amino acids.
3 eprived cells accumulate proteins with fewer sulfur-containing amino acids.
4 tary disorders that affect the catabolism of sulfur-containing amino acids.
5 of related peptides without the aromatic and sulfur-containing amino acids.
6 undance is controlled by the availability of sulfur-containing amino acids.
8 e-compensated nido-carboranyl derivatives of sulfur-containing amino acids and biotin has been synthe
9 Urate hydroperoxide oxidizes glutathione and sulfur-containing amino acids and is expected to react f
13 f protease activity by the modification of a sulfur-containing amino acid at the dimer interface may
14 an be regulated by reversible oxidation of a sulfur-containing amino acid at the dimer interface.
15 at the majority of retroviral proteases have sulfur-containing amino acids at the dimer interface.
17 ystem which are capable of rapidly oxidizing sulfur-containing amino acids, causing significant prote
18 e NBI and 7S globulin had a lower content of sulfur-containing amino acids compared to NBF and the el
19 ogen (i.e. storage protein) and sulfur (i.e. sulfur-containing amino acid) concentrations/contents.
20 se 4 (GPX-4), is generated directly from the sulfur-containing amino acid cysteine, and indirectly fr
23 aching response of cyanobacteria, to provide sulfur-containing amino acids during periods of sulfur d
24 ally biased criteria, such as the absence of sulfur-containing amino acids from the Urey-Miller exper
26 m catalysts are inhibited by the presence of sulfur-containing amino acids; however, these supported
27 cysteine content revealed no requirement for sulfur-containing amino acids in the target protein.
28 t that reducing agents, including endogenous sulfur-containing amino acid l-cysteine, selectively enh
29 ceptible to inactivation by oxidation of the sulfur-containing amino acid lanthionine, limiting their
33 metabolism of B. pertussis revealed that the sulfur-containing amino acids methionine and cysteine an
34 he proteins involved in the synthesis of the sulfur-containing amino acids methionine and cysteine, i
35 reference ranges, there were deficiencies in sulfur-containing amino acids (methionine, cysteine) in
36 In contrast, selective ligation to the other sulfur-containing amino acid, methionine, has been precl
38 hly conserved mechanism for metabolizing the sulfur-containing amino acids, methionine and cysteine.
39 e as the final step in the catabolism of the sulfur-containing amino acids, methionine and cysteine.
40 eadily sulfidize in the presence of isolated sulfur containing amino acids or proteins, such as cyste
41 dize a variety of cellular constituents, but sulfur-containing amino acid residues are especially sus
43 robably driven by dietary components such as sulfur-containing amino acids (SAAs) and inorganic sulfu
45 remethylation of homocysteine -- a cytotoxic sulfur-containing amino acid that can induce DNA strand
48 ption), and 3) raising the concentrations of sulfur-containing amino acids (thought to promote zinc a