Mutations within the propeptide, the primary cleavage site or the catalytic site, or deletion of C-terminal sequences, prevents secretion of proPC2 from transfected COS-7 cells

Mutations within the propeptide, the primary cleavage site or the catalytic site, or deletion of C-terminal sequences, prevents secretion of proPC2 from transfected COS-7 cells

Item
http://www.wikidata.org/entity/Q24318604
Modulation of prohormone convertase 1/3 properties using site-directed mutagenesis.A novel familial mutation in the PCSK1 gene that alters the oxyanion hole residue of proprotein convertase 1/3 and impairs its enzymatic activity.Prohormone convertase 2 activity is increased in the hippocampus of Wfs1 knockout mice.A non canonical subtilase attenuates the transcriptional activation of defence responses in Arabidopsis thaliana.The RGD motif and the C-terminal segment of proprotein convertase 1 are critical for its cellular trafficking but not for its intracellular binding to integrin alpha5beta1.Structure-function analysis of the prosegment of the proprotein convertase PC5A.Activation of the kexin from Schizosaccharomyces pombe requires internal cleavage of its initially cleaved prosequence.Involvement of the membrane lipid bilayer in sorting prohormone convertase 2 into the regulated secretory pathway.Interaction of Drosophila melanogaster prohormone convertase 2 and 7B2. Insect cell-specific processing and secretion.Residues unique to the pro-hormone convertase PC2 modulate its autoactivation, binding to 7B2 and enzymatic activity.Processing and trafficking of a prohormone convertase 2 active site mutantThe integrity of the RRGDL sequence of the proprotein convertase PC1 is critical for its zymogen and C-terminal processing and for its cellular trafficking.Differences in the autocatalytic cleavage of pro-PC2 and pro-PC3 can be attributed to sequences within the propeptide and Asp310 of pro-PC2.Maturation of barley cysteine endopeptidase expressed in Trichoderma reesei is distorted by incomplete processing.Structural organization of precursors of thermolysin-like proteinases.
P2860

Mutations within the propeptide, the primary cleavage site or the catalytic site, or deletion of C-terminal sequences, prevents secretion of proPC2 from transfected COS-7 cells

Item
http://www.wikidata.org/entity/Q24318604
description
1997 nî lūn-bûn
@nan
1997 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1997 թվականի հունվարին հրատարակված գիտական հոդված
@hy
1997年の論文
@ja
1997年学术文章
@wuu
1997年学术文章
@zh-cn
1997年学术文章
@zh-hans
1997年学术文章
@zh-my
1997年学术文章
@zh-sg
1997年學術文章
@yue
name
Mutations within the propeptid ...... 2 from transfected COS-7 cells
@ast
Mutations within the propeptid ...... 2 from transfected COS-7 cells
@en
Mutations within the propeptid ...... 2 from transfected COS-7 cells
@en-gb
Mutations within the propeptid ...... 2 from transfected COS-7 cells
@nl
type
label
Mutations within the propeptid ...... 2 from transfected COS-7 cells
@ast
Mutations within the propeptid ...... 2 from transfected COS-7 cells
@en
Mutations within the propeptid ...... 2 from transfected COS-7 cells
@en-gb
Mutations within the propeptid ...... 2 from transfected COS-7 cells
@nl
prefLabel
Mutations within the propeptid ...... 2 from transfected COS-7 cells
@ast
Mutations within the propeptid ...... 2 from transfected COS-7 cells
@en
Mutations within the propeptid ...... 2 from transfected COS-7 cells
@en-gb
Mutations within the propeptid ...... 2 from transfected COS-7 cells
@nl
P1433
P1476
P2093
P2860
P304
P31
P3181
P356
P407
P478
P50
P577
P5875
P698
P921
P932
P3181
P356
P1433
P1476
Mutations within the propeptid ...... 2 from transfected COS-7 cells
@en
P2093
P2860
P304
P31
P3181
P356
P407
P478
P50
P577
P5875
P698
P921
P932