Hairpin loop mutations of chicken cystatin have different effects on the inhibition of cathepsin B, cathepsin L and papain.
about
The N-terminal part of recombinant human tear lipocalin/von Ebner's gland protein confers cysteine proteinase inhibition depending on the presence of the entire cystatin-like sequence motifsInhibition of mammalian legumain by Michael acceptors and AzaAsn-halomethylketones.Phage display selection of hairpin loop soyacystatin variants that mediate high affinity inhibition of a cysteine proteinase.Viral cystatin evolution and three-dimensional structure modelling: a case of directional selection acting on a viral protein involved in a host-parasitoid interaction.Salivary (SD-type) cystatins: over one billion years in the making--but to what purpose?The proteasome: a macromolecular assembly designed to confine proteolysis to a nanocompartment.Molecular background of EPM1-Unverricht-Lundborg disease.Hybrids of chicken cystatin with human kininogen domain 2 sequences exhibit novel inhibition of calpain, improved inhibition of actinidin and impaired inhibition of papain, cathepsin L and cathepsin B.A multifunctional protease inhibitor to regulate endolysosomal function.Quail cystatin: isolation and characterisation of a new member of the cystatin family and its hypothetical interaction with cathepsin B.Cystatins as calpain inhibitors: engineered chicken cystatin- and stefin B-kininogen domain 2 hybrids support a cystatin-like mode of interaction with the catalytic subunit of mu-calpain.The role of the second binding loop of the cysteine protease inhibitor, cystatin A (stefin A), in stabilizing complexes with target proteases is exerted predominantly by Leu73.Characterization of cystatin C from bovine parotid glands: cysteine proteinase inhibition and antiviral properties.
P2860
Q28208063-4CB030B5-4740-45CB-99AE-F21FD419508AQ30320744-CBCD386B-AA8A-4DCD-A7EF-172CCD817968Q30726026-EEF88365-AECB-4B81-8F19-F38C00C31A0AQ33368470-CF43611A-A082-4520-B95A-9CBE789327F3Q35033473-E4D41C9E-2766-40B4-A7F5-F5179942A863Q36862775-1E013D0B-FA08-4625-BE8F-9A2CA402FF9CQ37009004-0AEE4D22-12B8-4B73-9BCB-AE6DA2C4C0A1Q38362165-F9138E27-C399-4EA6-A5B2-20F7547F350EQ39233985-80A13334-E7CF-4610-A905-9B1509D5F6FCQ42662817-229CD648-68BF-4870-8FFE-599A79F594B3Q43547466-57EB6FE1-5812-4B14-8EB9-C1AE22B03C4EQ44210405-38BAE318-A235-4E8C-A46B-9D4E5FAD9CC0Q45192161-2670B9CD-0E2D-4DA6-BFA1-7168F92A340C
P2860
Hairpin loop mutations of chicken cystatin have different effects on the inhibition of cathepsin B, cathepsin L and papain.
description
1995 nî lūn-bûn
@nan
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
1995年论文
@zh
1995年论文
@zh-cn
name
Hairpin loop mutations of chic ...... sin B, cathepsin L and papain.
@en
type
label
Hairpin loop mutations of chic ...... sin B, cathepsin L and papain.
@en
prefLabel
Hairpin loop mutations of chic ...... sin B, cathepsin L and papain.
@en
P2093
P2860
P1433
P1476
Hairpin loop mutations of chic ...... sin B, cathepsin L and papain.
@en
P2093
Assfalg-Machleidt I
Auerswald EA
Machleidt W
P2860
P304
P356
10.1016/0014-5793(95)00175-9
P407
P577
1995-03-01T00:00:00Z