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  • 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. (en)
  • 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. (cs)
Title
  • Activation processing of cathepsin H impairs recognition by its propeptide
  • Activation processing of cathepsin H impairs recognition by its propeptide (en)
  • Aktivační procesing kathepsinu H brání interakci s propeptidem (cs)
skos:prefLabel
  • Activation processing of cathepsin H impairs recognition by its propeptide
  • Activation processing of cathepsin H impairs recognition by its propeptide (en)
  • Aktivační procesing kathepsinu H brání interakci s propeptidem (cs)
skos:notation
  • RIV/61388963:_____/05:00021256!RIV06-MSM-61388963
http://linked.open.../vavai/riv/strany
  • 941;947
http://linked.open...avai/riv/aktivita
http://linked.open...avai/riv/aktivity
  • P(GP203/01/D008), P(IAA4055303), P(LC512), Z(AV0Z40550506)
http://linked.open...iv/cisloPeriodika
  • -
http://linked.open...vai/riv/dodaniDat
http://linked.open...aciTvurceVysledku
http://linked.open.../riv/druhVysledku
http://linked.open...iv/duvernostUdaju
http://linked.open...titaPredkladatele
http://linked.open...dnocenehoVysledku
  • 511304
http://linked.open...ai/riv/idVysledku
  • RIV/61388963:_____/05:00021256
http://linked.open...riv/jazykVysledku
http://linked.open.../riv/klicovaSlova
  • aminopeptidase; cysteine peptidase; inhibition (en)
http://linked.open.../riv/klicoveSlovo
http://linked.open...odStatuVydavatele
  • DE - Spolková republika Německo
http://linked.open...ontrolniKodProRIV
  • [A8CD4286F989]
http://linked.open...i/riv/nazevZdroje
  • Biological Chemistry
http://linked.open...in/vavai/riv/obor
http://linked.open...ichTvurcuVysledku
http://linked.open...cetTvurcuVysledku
http://linked.open...vavai/riv/projekt
http://linked.open...UplatneniVysledku
http://linked.open...v/svazekPeriodika
  • 386
http://linked.open...iv/tvurceVysledku
  • Horn, Martin
  • Mareš, Michael
  • Máša, Martin
  • Rulíšek, Lubomír
  • Marešová, Lucie
  • Baudyš, Miroslav
  • Gan-Erdene, T.
  • Turk, B.
  • Vasiljeva, O.
http://linked.open...n/vavai/riv/zamer
issn
  • 1431-6730
number of pages
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