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1 cture-function properties of a mitochondrial cysteine desulfurase.
2 and the adjacent gene, nifZ, encoding for a cysteine desulfurase.
3 IscS is one of the three Escherichia coli l-cysteine desulfurases.
4 s unknown, and many archaea lack homologs of cysteine desulfurases.
5 lfur clusters is derived from L-cysteine via cysteine desulfurases.
6 layed both SufE activity (stimulating CpNifS cysteine desulfurase activity 70-fold) and quinolinate s
7 S homologs, csdA and csdB, each of which has cysteine desulfurase activity and could potentially dona
8 t proteins were similar to wild type in both cysteine desulfurase activity and sulfur transfer to Isc
9 at, of the multiple proteins in E. coli with cysteine desulfurase activity as observed by native gel
15 port that the SufE protein can stimulate the cysteine desulfurase activity of the SufS enzyme up to 8
16 esidues 376-413 (IscSDelta376-413) displayed cysteine desulfurase activity similar to the full-length
17 formation of a ternary complex with reduced cysteine desulfurase activity, and we determined a low-r
18 se data support the conclusion that, via its cysteine desulfurase activity, IscS provides the sulfur
19 sphate (PLP)-dependent enzyme with intrinsic cysteine desulfurase activity, no evidence for PLP bindi
25 in archaea is not known as many archaea lack cysteine desulfurase and an RLD of the putative ThiI.
26 ssense mutations exhibited similar losses of cysteine desulfurase and Fe-S cluster assembly activitie
27 Our analysis revealed Lecsl to be a novel cysteine desulfurase and not a type of cysteine sulfoxid
28 anistically unified by the requirement for a cysteine desulfurase and the participation of an [Fe-S]
29 ck of the gene encoding for a canonical IscS cysteine desulfurase and the presence of a short sequenc
33 ied the (35)S-labeled persulfide on the NFS1 cysteine desulfurase as a genuine intermediate en route
34 persulfide intermediate in the reaction of a cysteine desulfurase (CD), CD0387 from Synechocystis sp.
36 ed the two constituent proteins of the human cysteine desulfurase complex (NFS1 and ISD11) separately
37 er on the scaffold protein (ISCU) involves a cysteine desulfurase complex (NFS1/ISD11) and frataxin (
38 ion into multiple biosynthetic pathways by a cysteine desulfurase complex that consists of a catalyti
43 h SufE and IscU with the mutually homologous cysteine desulfurase enzymes present in their respective
46 D-0387), a sequence group I (NifS/IscS-like) cysteine desulfurase from Synechocystis sp. PCC 6803, by
47 und that the iscS gene, a member of the nifS cysteine desulfurase gene family, is required for 4-thio
48 eria, including Bacillus subtilis, contain a cysteine desulfurase gene sufS located adjacent to the g
51 erase, receiving the sulfur donated from the cysteine desulfurase IscS and transferring it to the tar
53 following two enzymes for its synthesis: the cysteine desulfurase IscS, which forms a Cys persulfide
56 ons share strong sequence homology, e.g. the cysteine desulfurases IscS and SufS, and presumably play
57 IscX binds iron ions and interacts with the cysteine desulfurase (IscS) and the scaffold protein for
58 reduce sulfane sulfur (S(0)) produced by the cysteine desulfurase (IscS) to sulfide (S(2-)) as requir
60 scU in the presence of the iron-loaded IscA, cysteine desulfurase (IscS), and L-cysteine, demonstrati
61 orms a stable complex in vivo with the human cysteine desulfurase (ISCS), which generates the inorgan
62 ter, we identified and characterized the Mtb cysteine desulfurase (IscS; Rv3025c) and developed a nat
63 es place in the complex between IscU and the cysteine desulfurase, IscS, and our NMR studies demonstr
66 tudies showed that TUM1 interacts with the l-cysteine desulfurase NFS1 and the rhodanese-like protein
68 r example, the assembly process requires the cysteine desulfurase Nfs1, which serves as the sulfur do
69 Frataxin interacts with Isu, iron, and the cysteine desulfurase Nfs1, which supplies sulfide, thus
71 ter assembly; this complex also includes the cysteine desulfurase (Nfs1 in yeast) and the accessory p
73 r modeling suggests that two subunits of the cysteine desulfurase, Nfs1, may bind symmetrically on to
75 evidence for PLP binding or for PLP-induced cysteine desulfurase or biotin synthase activity was obs
78 Increasing evidence suggests that IscS, a cysteine desulfurase, provides sulfur for assembly of tr
79 e active role for SufE in promoting the SufS cysteine desulfurase reaction for Fe-S cluster assembly.
82 hesized in a multistep process that utilizes cysteine desulfurases, scaffold proteins, chaperones, an
83 olves interaction of Isu with both Nfs1, the cysteine desulfurase serving as a sulfur donor, and the
86 , the cytosolic form of ISCS is a functional cysteine desulfurase that can collaborate with cytosolic
88 odimeric IscS protein has been shown to be a cysteine desulfurase that catalyzes the reductive conver
89 that the cytosolic form of ISCS is an active cysteine desulfurase that covalently binds 35S acquired
91 proteins specifically associate with IscS, a cysteine desulfurase that is proposed to sequester inorg
92 port cloning of the human homolog of NifS, a cysteine desulfurase that is proposed to supply the inor
93 as IscS, a recently characterized NifS-like cysteine desulfurase that mobilizes sulfur for the synth
94 hat decreased expression of Nfs1p, the yeast cysteine desulfurase that plays a central role in Fe-S c
97 r source, and the sulfur is transferred from cysteine desulfurase through a persulfidic intermediate
98 Lecsl and that the gene Csl encoded a novel cysteine desulfurase to influence organosulfur compounds
100 of IscS (SA1450) in S. aureus is active as a cysteine desulfurase, which enables the in vitro reconst
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