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1 ed this activity with putative mycobacterial cutinase.
2 bound efficiently and specifically to LFA-1/cutinase.
3 ceptor that presents the nonmammalian enzyme cutinase.
4 was more pronounced for the lipase than the cutinase.
5 imilar tertiary structure is Fusarium solani cutinase.
6 y Rhizopus oryzae lipase and Fusarium solani cutinase.
7 ut2/3 matched with that of the peptides from cutinase 1 and cutinase 2, respectively, isolated from F
8 assemblies can much more effectively retain cutinase 2 activity on a surface after co-incubation and
9 hese hydrophobins and their interaction with cutinase 2 is crucial for the development of novel antif
10 ith that of the peptides from cutinase 1 and cutinase 2, respectively, isolated from F. solani pisi g
11 esion and to direct the action of the enzyme cutinase 2, resulting in penetration of the plant host.
12 e, a fusion protein containing an N-terminal cutinase and a C-terminal SnapTag domain react with an e
13 ability, and structure of Aspergillus oryzae cutinase and compare it to the well-studied enzyme from
17 PETases compared to close relatives from the cutinase and lipase families have resulted in increasing
20 carbohydrate esterase family 5 for putative cutinases and condensed it to 151 genes from known or pu
21 t encounter cutin; we demonstrate that known cutinases and MPLA cleave phospholipids in a PLA-type ma
22 cycling is gaining momentum, with engineered cutinases and PETases developed for the depolymerization
23 The covalent immobilization is specific for cutinase, and the glycol-terminated monolayer effectivel
28 mon resonance (SPR) spectroscopy showed that cutinase binds irreversibly to a monolayer presenting th
29 tions, however, requires deeper knowledge of cutinases' biodiversity and structure-function relations
30 rganization with a catalytic triad common to cutinases, but which contains an additional four-helix d
32 dies suggest an alternative use for putative cutinases by the M. tuberculosis group that is likely re
33 e used to immobilize proteins of interest, a cutinase-calmodulin fusion protein was constructed and i
34 ionalized with a novel calmodulin construct, cutinase-calmodulin-cutinase (CutCaMCut), reversibly shi
36 hey accept bulky and hydrophobic substrates, cutinases could be used in many applications, ranging fr
39 We then selected nine phylogenic diverse cutinases for recombinant production and characterized t
41 al dilute aqueous solutions or slurries, the cutinase from Humicola insolens can directly depolymeriz
44 y expressing the enzyme Fusarium solani pisi cutinase (FsC) on the cell surface of Baker's yeast Sacc
46 c sequence located at -159 base pairs of the cutinase gene in Fusarium solani f. sp. pisi (Nectria he
49 n previously to induce the expression of the cutinase gene via a palindromic sequence located at -159
53 y the low levels of constitutively expressed cutinase, induce high levels of cutinase that can help p
54 ed here provide insight into engineering new cutinase-inspired biocatalysts with tailor-made properti
55 uronidase gene fused to the promoters of the cutinases integrated into F. solani pisi genome indicate
59 gh the heavy chain variable domain to either cutinase or SnapTag, with a linker terminated in an irre
60 ffectors by IC: phytotoxins, ROS, proteases, cutinases, plant cell wall-degrading enzymes and plant c
61 SV40 in yeast, it transactivated the native cutinase promoter fused to the chloramphenicol acetyl tr
62 of three microbial lipases: Fusarium solani cutinase, Rv0183, and LipY from Mycobacterium tuberculos
63 megamolecules are prepared by attaching four Cutinase-SnapTag fusion proteins (CS fusions) to a four-
64 ly expressed cutinase, induce high levels of cutinase that can help pathogenic fungi to penetrate int
65 m tuberculosis has maintained seven putative cutinases, though it should not encounter cutin; we demo
66 y is based on binding of the serine esterase cutinase to a self-assembled monolayer presenting a phos
67 cDNA clone encoding a polypeptide designated cutinase transcription factor 1alpha (CTF1alpha) with a
68 flavodoxin family (CheY, apoflavodoxin, and cutinase) using a simple nucleation and growth model tha
73 o a phylogenetic analysis, which showed that cutinases with available crystal structures were phyloge