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Statements

Subject Item
n2:RIV%2F61388963%3A_____%2F05%3A00021256%21RIV06-MSM-61388963
rdf:type
skos:Concept n17:Vysledek
dcterms:description
We studied the inhibitory interaction of cathepsin H with its propeptide fragments using the fully processed wild-type enzyme and the recombinant enzyme lacking the mini-chain. The difference between both enzymes with respect to propeptide recognition suggests a structural rearrangement in the cathepsin H molecule induced by maturation processing. The acquired changes, dominated by the mini-chain formation, impair the effective recognition of the mature cathepsin H by its own propeptide. We studied the inhibitory interaction of cathepsin H with its propeptide fragments using the fully processed wild-type enzyme and the recombinant enzyme lacking the mini-chain. The difference between both enzymes with respect to propeptide recognition suggests a structural rearrangement in the cathepsin H molecule induced by maturation processing. The acquired changes, dominated by the mini-chain formation, impair the effective recognition of the mature cathepsin H by its own propeptide. Studovali jsme inhibiční interakci fragmentů propeptidu se zralým kathepsinem H a rekombinantním kathepsinem H, který neobsahuje miniřetězec. Rozdíl v interakci u obou enzymů ukazuje, že v molekule kathepsinu H probíhají strukturní změny indukované během zrání, zejména tvorba miniřetězce. Tyto změny brání účinné inhibici zralého kathepsinu H jeho vlastním propeptidem.
dcterms:title
Aktivační procesing kathepsinu H brání interakci s propeptidem Activation processing of cathepsin H impairs recognition by its propeptide Activation processing of cathepsin H impairs recognition by its propeptide
skos:prefLabel
Activation processing of cathepsin H impairs recognition by its propeptide Activation processing of cathepsin H impairs recognition by its propeptide Aktivační procesing kathepsinu H brání interakci s propeptidem
skos:notation
RIV/61388963:_____/05:00021256!RIV06-MSM-61388963
n4:strany
941;947
n4:aktivita
n5:Z n5:P
n4:aktivity
P(GP203/01/D008), P(IAA4055303), P(LC512), Z(AV0Z40550506)
n4:cisloPeriodika
-
n4:dodaniDat
n9:2006
n4:domaciTvurceVysledku
n10:9846476 n10:7667108 n10:8365423 n10:8133859 n10:6559670 n10:7465157
n4:druhVysledku
n16:J
n4:duvernostUdaju
n18:S
n4:entitaPredkladatele
n14:predkladatel
n4:idSjednocenehoVysledku
511304
n4:idVysledku
RIV/61388963:_____/05:00021256
n4:jazykVysledku
n13:eng
n4:klicovaSlova
aminopeptidase; cysteine peptidase; inhibition
n4:klicoveSlovo
n8:cysteine%20peptidase n8:aminopeptidase n8:inhibition
n4:kodStatuVydavatele
DE - Spolková republika Německo
n4:kontrolniKodProRIV
[A8CD4286F989]
n4:nazevZdroje
Biological Chemistry
n4:obor
n11:CE
n4:pocetDomacichTvurcuVysledku
6
n4:pocetTvurcuVysledku
9
n4:projekt
n6:IAA4055303 n6:GP203%2F01%2FD008 n6:LC512
n4:rokUplatneniVysledku
n9:2005
n4:svazekPeriodika
386
n4:tvurceVysledku
Turk, B. Horn, Martin Baudyš, Miroslav Marešová, Lucie Rulíšek, Lubomír Gan-Erdene, T. Mareš, Michael Vasiljeva, O. Máša, Martin
n4:zamer
n15:AV0Z40550506
s:issn
1431-6730
s:numberOfPages
7