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1  a standard NOS heme structure as a thiolate hemeprotein.
2 O and NO were very high as compared to other hemeproteins.
3 terin and Arg to allow comparison with other hemeproteins.
4 que mechanisms of interaction between NO and hemeproteins.
5 the versatile nature by which NO can bind to hemeproteins.
6  trigger heme release and delivery to client hemeproteins.
7 th GAPDH to regulate nNOS and possibly other hemeproteins.
8 P signaling and to more generally tune their hemeprotein activities wherever NO biosynthesis takes pl
9 mple chemical strategy was also applied to a hemeprotein and an aspartyl protease, setting the stage
10 ntral role both for characterizing different hemeproteins and their conformational states but also fo
11  the reactions of NO with ferric and ferrous hemeproteins are not as well characterized.
12 ood cells are destroyed and large amounts of hemeproteins are released.
13 ) by which it can utilize the hosts heme and hemeproteins as a source of iron.
14 monoxide; NO) reacts with the iron center of hemeproteins at near diffusion-controlled rates.
15 otected from vinyl group modification by the hemeprotein covalent bonds, we prepared the F41E mutant
16 f a transient protein radical and a covalent hemeprotein cross-link.
17 loperoxidase (MPO) is a neutrophil lysosomal hemeprotein essential for optimal oxygen-dependent micro
18    We cloned, expressed, and characterized a hemeprotein from Deinococcus radiodurans (D. radiodurans
19 ith mitochondria and prevents GAPDH and cell hemeproteins from receiving heme.
20                       Interaction of CO with hemeproteins has physiological importance.
21                            Although multiple hemeproteins have been reported to function as nitrite r
22                       Complex IV is the only hemeprotein in the cell that contains heme a, which may
23 is a critical danger molecule liberated from hemeproteins in various conditions, including from hemog
24 eme molecule is the prosthetic group of many hemeproteins involved in essential physiological process
25    In that the heme content of many critical hemeproteins is regulated by Hsp90 and the heme chaperon
26 s of NO from some, not all, noniron sites in hemeproteins is very slow (t(1/2) approximately hours).
27 es oxygen when binding to the iron center of hemeproteins, leading to a reduction in blood oxygen lev
28 arbon monoxide (CO) to iron(II) sites of the hemeproteins led to evidence of NO binding to noniron, n
29 in circulation, and suggests that additional hemeproteins might be involved in sulfide homeostasis in
30 ms may utilize heme directly from the host's hemeproteins or via a hemophore that sequesters and tran
31 sion between respiratory complexes, enhances hemeprotein peroxidase and reactive oxygen species scave
32                                              Hemeproteins play an important role in the signaling pro
33  facilitate both thermal and photo-initiated hemeprotein reduction over large macroscopic distances.
34 yst for such reactions is myeloperoxidase, a hemeprotein secreted by activated phagocytes.
35 ential mechanism involves myeloperoxidase, a hemeprotein secreted by human phagocytes.
36 ex with heme (Kd = 2.5 +/- 1 microM) and has hemeprotein spectra similar to those previously reported
37 ults in spectral properties of the resulting hemeprotein that are consistent with the loss of a thiol
38                              Myoglobin (Mb), hemeprotein that binds dioxygen in muscle, affects meat
39 nducible nitric oxide synthase (iNOSox) is a hemeprotein that binds L-arginine (L-Arg) and tetrahydro
40       Human cystathionine beta-synthase is a hemeprotein that catalyzes a pyridoxal phosphate (PLP)-d
41                The latter enzyme is a unique hemeprotein that catalyzes pyridoxal phosphate (PLP)-dep
42  Cystathionine beta-synthase is a tetrameric hemeprotein that catalyzes the pyridoxal 5'-phosphate-de
43 me c oxidase (CcO) is a large membrane-bound hemeprotein that catalyzes the reduction of dioxygen to
44  Neuronal nitric-oxide synthase (NOS-1) is a hemeprotein that generates NO and citrulline from L-argi
45 le NO synthase (iNOS) is a flavin-containing hemeprotein that must dimerize to generate NO.
46  Inducible nitric-oxide synthase (iNOS) is a hemeprotein that requires tetrahydrobiopterin (H4B) for
47             Nitric oxide synthases (NOS) are hemeproteins that catalyze oxidation of L-arginine to ni
48                                              Hemeproteins, the largest source of iron within vertebra
49 phan to N-formyl kynurenine catalyzed by two hemeproteins, tryptophan 2,3-dioxygenase (hTDO) and indo
50            Unlike classical dioxygen binding hemeproteins with a heme b group in their active sites,