Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Lucie Dolečková-Marešová"'
Autor:
Jana Hýblová, Ivana Křížková-Kudlíková, Zuzana Münzbergová, Vaclav Stejskal, Stanislav Pekár, Jan Hubert, Lucie Dolečková-Marešová, Marek Mareš
Publikováno v:
Physiological Entomology. 32:41-49
Acarus siro is the most abundant and frequent mite to infest stored-food products, causing allergies and transmitting mycotoxin producing fungi. The predatory mite Cheyletus malaccensis is a candidate species in the biocontrol programme for this pest
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3ac83c76a533be82cd22a2e4264e9b09
https://doi.org/10.1111/j.1365-3032.2006.00539.x
https://doi.org/10.1111/j.1365-3032.2006.00539.x
Autor:
Juraj Sedlacek, Jaromír Plešek, Vladimír Král, Jan Konvalinka, Jiří Brynda, Jochen Bodem, Martin Máša, Hans-Georg Kräusslich, Jana Pokorná, Zbyszek Otwinowski, Pavlína Řezáčová, Bohumír Grüner, Lucie Dolečková-Marešová, Petr Cigler, Milan Kožíšek
Publikováno v:
Proceedings of the National Academy of Sciences. 102:15394-15399
HIV protease (PR) represents a prime target for rational drug design, and protease inhibitors (PI) are powerful antiviral drugs. Most of the current PIs are pseudopeptide compounds with limited bioavailability and stability, and their use is compromi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::529f6deaa7aa85ad2eb5f794846f40a9
https://doi.org/10.1073/pnas.0507577102
https://doi.org/10.1073/pnas.0507577102
Autor:
Jana Hýblová, Lucie Dolečková-Marešová, Martin Horn, František Kocourek, Zdeněk Voburka, Jan Hubert, Iva Kudlı́ková, Ivan Kluh, Michael Mareš
Publikováno v:
Phytochemistry. 66:31-39
The primary structure and proteolytic processing of the alpha-amylase isoinhibitor alpha AI-1 from common bean (Phaseolus vulgaris cv. Magna) was determined by protein chemistry techniques. The inhibitory specificity of alphaAI-1 was screened with a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ce19160c9d598d6cf1d1a27a8ed958a9
https://doi.org/10.1016/j.phytochem.2004.11.001
https://doi.org/10.1016/j.phytochem.2004.11.001
Autor:
Lucie Dolečková-Marešová, Tudeviin Gan-Erdene, Boris Turk, Olga Vasiljeva, Martin Horn, Miroslav Baudyš, Lubomír Rulíšek, Martin Máša, Michael Mareš
Publikováno v:
Biological chemistry. 386(9)
Free propeptides are known to function as inhibitors of the parental mature cysteine cathepsins. This general rule, however, does not apply to the aminopeptidase cathepsin H. Screening of propeptide fragments for their inhibitory potency revealed no
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3ba31e9d60a9da43a6d1f79b1cbd6475
https://pubmed.ncbi.nlm.nih.gov/16164419
https://pubmed.ncbi.nlm.nih.gov/16164419
Autor:
Lucie Dolečková-Marešová, Michael Mareš, Aparna G. Patankar, Ian T. Baldwin, Martin Horn, Jianqiang Wu, Jorge A. Zavala, Milana Vůjtěchová
Publikováno v:
Plant Physiology
Trypsin proteinase inhibitors (TPIs) of Nicotiana attenuata are major antiherbivore defenses that increase dramatically in leaves after attack or methyl jasmonate (MeJA) elicitation. To understand the elicitation process, we characterized the proteol
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::259c6a3144695e5394feaae8de698545
https://pubmed.ncbi.nlm.nih.gov/16113221
https://pubmed.ncbi.nlm.nih.gov/16113221
Autor:
Jana Hýblová, Lucie Dolečková-Marešová, Jan Hubert, Václav Stejskal, Michael Mareš, Iva Kudlíková
Publikováno v:
Experimentalapplied acarology. 35(4)
The stored-product mites are the most abundant and frequent group of pests living on the stored food products in Europe. They endanger public health since they produce allergens and transmit mycotoxin-producing fungi. Novel acaricidal compounds with
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2f4385e150a48e85f48cdd290f5f2bbc
https://pubmed.ncbi.nlm.nih.gov/15969461
https://pubmed.ncbi.nlm.nih.gov/15969461
Publikováno v:
Chemistrybiology. 12(12)
We report a low molecular weight inhibitor of alpha-amylases based on a linear peptidic scaffold designed de novo through the use of combinatorial chemistry. The inhibitory motif denoted PAMI (peptide amylase inhibitor) was selected by using L-peptid
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0c659df6ea7d69008cd7b6149bb91142
https://pubmed.ncbi.nlm.nih.gov/16356842
https://pubmed.ncbi.nlm.nih.gov/16356842