Zobrazeno 1 - 10
of 22
pro vyhledávání: '"Anna Janicka-Klos"'
Autor:
Magdalena Szota, Urszula Szwedowicz, Nina Rembialkowska, Anna Janicka-Klos, Daniel Doveiko, Yu Chen, Julita Kulbacka, Barbara Jachimska
Publikováno v:
International Journal of Molecular Sciences, Vol 25, Iss 13, p 7201 (2024)
The unique structure of G4.0 PAMAM dendrimers allows a drug to be enclosed in internal spaces or immobilized on the surface. In the conducted research, the conditions for the formation of the active G4.0 PAMAM complex with doxorubicin hydrochloride (
Externí odkaz:
https://doaj.org/article/04d82a27460d42bab527d4bf79434082
Autor:
Dorota Dudek, Anna Janicka-Klos, Slawomir Potocki, Paula Delgado, Magdalena Rowińska-Żyrek, Henryk Kozlowski
Publikováno v:
Inorganica Chimica Acta. 488:255-259
PhtA, a Streptococcus pneumoniae polyhistidine triad protein, which contributes to virulence by interacting with components of the immune system, by being involved in adherence of bacteria and in Zn(II) uptake, contains five copies of the HxxHxH sequ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9067a8cb2e7597319a273a1b5a361ba1
https://www.sciencedirect.com/science/article/pii/S0020169318317961?via=ihub
https://www.sciencedirect.com/science/article/pii/S0020169318317961?via=ihub
Autor:
Anna Janicka-Klos, Elżbieta Gębarowska, Beata Tylińska, Aneta Cieśla-Niechwiadowicz, Żaneta Czyżnikowska, Benita Wiatrak
Publikováno v:
International Journal of Molecular Sciences
Volume 22
Issue 8
International Journal of Molecular Sciences, Vol 22, Iss 3825, p 3825 (2021)
Volume 22
Issue 8
International Journal of Molecular Sciences, Vol 22, Iss 3825, p 3825 (2021)
In the present paper, new pyrimidine derivatives were designed, synthesized and analyzed in terms of their anticancer properties. The tested compounds were evaluated in vitro for their antitumor activity. The cytotoxic effect on normal human dermal f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::06393b485b29db6e622a0322d6c2180e
Publikováno v:
International Journal of Molecular Sciences
International Journal of Molecular Sciences, Vol 23, Iss 418, p 418 (2022)
International Journal of Molecular Sciences; Volume 23; Issue 1; Pages: 418
International Journal of Molecular Sciences, Vol 23, Iss 418, p 418 (2022)
International Journal of Molecular Sciences; Volume 23; Issue 1; Pages: 418
Mucin 7 (encoded byMUC7) is a human salivary protein that has a role in the natural immune system. Fragments of mucin 7 exhibit antimicrobial activity against bacteria and yeast. Although the antimicrobial properties of peptides have been known and s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::66f0782e05a04d7a9ac9ddcf9d1e185c
https://doi.org/10.3390/ijms23010418
https://doi.org/10.3390/ijms23010418
Publikováno v:
Journal of inorganic biochemistry. 203
Mucin 7 (called MUC7 or MG2) is a salivary protein whose fragments exhibit a strong antimicrobial activity and is a natural protection of organisms against pathogens. Up to date however the exact mechanism of their actions is unknown. One hypothesis
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f5fb3713e156431f13e2208efefd5cd1
https://pubmed.ncbi.nlm.nih.gov/31837617
https://pubmed.ncbi.nlm.nih.gov/31837617
Publikováno v:
Inorganica Chimica Acta. 421:67-73
In the present study, the coordination abilities of Ac-TLEGTKKGHKLHL β DY-NH 2 peptide (the analogue of SPARC 114–128 fragment containing β -Asp 127 residue) are discussed. The analysis is provided based on the results of potentiometric and spect
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1b4426e3e03a3726dcb13840143aa729
https://doi.org/10.1016/j.ica.2014.05.017
https://doi.org/10.1016/j.ica.2014.05.017
Autor:
Anna Janicka-Klos, Justyna Brasuń, Elena Gaggelli, Gianni Valensin, Daniela Valensin, Henryk Kozlowski
Publikováno v:
Coordination Chemistry Reviews. 253:2665-2685
Metal ions, especially with high chemical activity (e.g. redox-active Cu and Fe) must be carefully managed in biological systems. The “uncontrolled” activity, e.g. catalysis of Fenton-like reactions by ions like Cu(I) or Fe(II), is so damaging fo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::69b69052647f07ff81f9787e95c70275
https://doi.org/10.1016/j.ccr.2009.05.011
https://doi.org/10.1016/j.ccr.2009.05.011
Autor:
Pawel Stanczak, Kinga Kulon, Anna Janicka-Klos, Henryk Kozlowski, Gianni Valensin, Daniela Valensin
Publikováno v:
Coordination Chemistry Reviews. 252:1069-1078
The prion proteins may play a critical role in copper homeostasis and the antioxidant activity in the brain. This review presents the state of art in the studies on Cu 2+ prion systems. The proteins discussed are from different species from mammals t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2740d05ed6d879d619fcbac60deb2009
https://doi.org/10.1016/j.ccr.2007.08.006
https://doi.org/10.1016/j.ccr.2007.08.006
Publikováno v:
Polyhedron. 27:1511-1516
The aim of this work was to check experimentally the relationship between the five-nitrogen donor system {3 × Nimid, 2 × N−} seen e.g. in the peptide fragments of the cysteine-rich amyloid precursor protein (APP) region and the albumin-like {NH2,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::28080bff2cd5b6d55dffc0d563816f14
https://doi.org/10.1016/j.poly.2008.01.025
https://doi.org/10.1016/j.poly.2008.01.025
Autor:
Elena Porciatti, Chiara Conato, Stanisław Ołdziej, Anna Janicka-Klos, Gianni Valensin, Daniela Valensin, Henryk Kozlowski, Maurizio Remelli
Publikováno v:
Dalton transactions (Cambridge, England : 2003). 42(2)
The binding mode provided by an unprotected peptide with non-coordinating side-chains is simple and well understood. However, when particular residues are inserted into the peptide sequence, they can have a significant impact on the stability of the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6e7965c5d7030bd945c8eaf40e6f30ed
https://pubmed.ncbi.nlm.nih.gov/23085940
https://pubmed.ncbi.nlm.nih.gov/23085940