All

What are you looking for?

All
Projects
Results
Organizations

Quick search

  • Projects supported by TA ČR
  • Excellent projects
  • Projects with the highest public support
  • Current projects

Smart search

  • That is how I find a specific +word
  • That is how I leave the -word out of the results
  • “That is how I can find the whole phrase”

Cysteine peptidases of Eudiplozoon nipponicum: a broad repertoire of structurally assorted cathepsins L in contrast to the scarcity of cathepsins B in an invasive species of haematophagous monogenean of common carp

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60460709%3A41210%2F18%3A78039" target="_blank" >RIV/60460709:41210/18:78039 - isvavai.cz</a>

  • Alternative codes found

    RIV/61388963:_____/18:00489775 RIV/00216224:14310/18:00100859 RIV/00216208:11310/18:10376237

  • Result on the web

    <a href="http://dx.doi.org/10.1186/s13071-018-2666-2" target="_blank" >http://dx.doi.org/10.1186/s13071-018-2666-2</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1186/s13071-018-2666-2" target="_blank" >10.1186/s13071-018-2666-2</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Cysteine peptidases of Eudiplozoon nipponicum: a broad repertoire of structurally assorted cathepsins L in contrast to the scarcity of cathepsins B in an invasive species of haematophagous monogenean of common carp

  • Original language description

    Transcriptomic analysis revealed a set of ten distinct transcripts that encode EnCLs. The enzymes are significantly variable in their active sites, specifically the S2 subsites responsible for interaction with substrates. Some of them display unusual structural features that resemble cathepsins B and S. Two recombinant EnCLs had different pH activity profiles against both synthetic and macromolecular substrates, and were able to hydrolyse blood proteins and collagen I. They were localised in the haematin cells of the worm digestive tract and in gut lumen. The EnCB showed similarity with cathepsin B2 of Schistosoma mansoni. It displays molecular features typical of cathepsins B, including an occluding loop responsible for its exopeptidase activity. Although the EnCB hydrolysed haemoglobin in vitro, it was localised in the vitelline cells of the parasite and not the digestive tract.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    30310 - Parasitology

Result continuities

  • Project

    Result was created during the realization of more than one project. More information in the Projects tab.

  • Continuities

    S - Specificky vyzkum na vysokych skolach

Others

  • Publication year

    2018

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Parasites & Vectors

  • ISSN

    1756-3305

  • e-ISSN

    1756-3305

  • Volume of the periodical

    11

  • Issue of the periodical within the volume

    142

  • Country of publishing house

    CZ - CZECH REPUBLIC

  • Number of pages

    17

  • Pages from-to

    1-17

  • UT code for WoS article

    000427131600001

  • EID of the result in the Scopus database

    2-s2.0-85043226328