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1 ases from H. irregulare, H. jecorina, and P. chrysosporium.
2 ished cellulolytic capability relative to P. chrysosporium.
3 e genome analysis of C. subvermispora and P. chrysosporium.
4 rom other morphologically similar species of Chrysosporium.
5 roxidase (LiP) isozyme H8 from Phanerochaete chrysosporium.
6 ed by ligninolytic cultures of Phanerochaete chrysosporium.
7 variant of MnP isozyme 1 from Phanerochaete chrysosporium.
8 ride monooxygenase (LPMO) from Phanerochaete chrysosporium.
13 roduced by the wood-rot fungus Phanerochaete chrysosporium as an essential component of its extracell
15 e site of glyoxal oxidase from Phanerochaete chrysosporium based on a combination of spectroscopic an
17 t half of dimer mineralization in wood by P. chrysosporium but was responsible for no more than 6-7%
18 peroxidase isozyme 1 (MnP1) of Phanerochaete chrysosporium by examining two mutants: R177A and R177K.
19 Lignin peroxidase (LiP) from Phanerochaete chrysosporium catalyzes irreversible oxidative damage to
20 Lignin peroxidase (LiP) from Phanerochaete chrysosporium catalyzes the H2O2 dependent one- and two-
21 rading basidiomycetous fungus, Phanerochaete chrysosporium, catalyzes the oxidation of MnII to MnIII.
22 improved Avicel hydrolysis by Phanerochaete chrysosporium CBH II, which is only 55-56% identical to
23 unnel that is more closed than Phanerochaete chrysosporium Cel7D and more open than Hypocrea jecorina
26 an electron transfer domain of Phanerochaete chrysosporium-derived cellobiose dehydrogenase (Pcyb) wa
30 In the present work, we used Phanerochaete chrysosporium for biochemical characterization and analy
33 ce for surface translation indicates that P. chrysosporium GH61D exhibits energy wells whose spacing
34 structure of the basidiomycete Phanerochaete chrysosporium GH61D LPMO, and, for the first time, measu
35 e (LiP) from the basidiomycete Phanerochaete chrysosporium has been determined to 2.6 A resolution by
37 y suggest that LiP produced by Phanerochaete chrysosporium has the potential to be used in the medica
42 ncode peroxidases structurally similar to P. chrysosporium lignin peroxidase and, following heterolog
48 acellular enzyme purified from Phanerochaete chrysosporium NK-1 isolated from a forest soil can effec
50 tion and characterization of the new species Chrysosporium ophiodiicola from a mycotic granuloma of a
51 LiP) from the white-rot fungus Phanerochaete chrysosporium oxidize veratryl alcohol (VA) by two elect
52 anganese peroxidase (MnP) from Phanerochaete chrysosporium oxidizes nonphenolic beta-1 diarylpropane
53 hemical properties of CDH from Phanerochaete chrysosporium (PcCDH) and Ceriporiopsis subvermispora (C
54 were produced by homologous expression in P. chrysosporium, purified to homogeneity, and characterize
59 30-million base-pair genome of Phanerochaete chrysosporium strain RP78 using a whole genome shotgun a
60 osely related white-rot fungus Phanerochaete chrysosporium support an evolutionary shift from white-r
61 omycetes Agaricus bisporus and Phanerochaete chrysosporium that were used successfully to control the
62 MnP) from the white-rot fungus Phanerochaete chrysosporium to investigate the role of the axial ligan
64 anganese peroxidase (MnP) from Phanerochaete chrysosporium undergoes a pH-dependent conformational ch
65 dase from the white-rot fungus Phanerochaete chrysosporium utilize the same Mn-binding site for catal
66 roxidase isozyme 1 (mnp1) from Phanerochaete chrysosporium was generated by overlap extension with th
67 dase from the white-rot fungus Phanerochaete chrysosporium was very susceptible to thermal inactivati
68 roxidase isozyme 1 (mnp1) from Phanerochaete chrysosporium, was created by overlap extension, using t
69 H2OH] by the white-rot fungus, Phanerochaete chrysosporium, was investigated in laboratory studies.
72 ities of a known LiP producer, Phanerochaete chrysosporium, with those of a reported nonproducer, Cer
73 ophilicum, Xerochrysium xerophilum (formerly Chrysosporium xerophilum) and Xeromyces bisporus, were p
74 on limited in vitro susceptibility data for Chrysosporium zonatum, amphotericin B is the most active