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  1. Article: Selective chemical reagents to investigate the role of caspase 6 in apoptosis in acute leukemia T cells.

    Groborz, Katarzyna M / Kalinka, Małgorzata / Grzymska, Justyna / Kołt, Sonia / Snipas, Scott J / Poręba, Marcin

    Chemical science

    2023  Volume 14, Issue 9, Page(s) 2289–2302

    Abstract: Activated effector caspases 3, 6 and 7 are responsible for cleaving a number of target substrates, leading to the ultimate destruction of ... ...

    Abstract Activated effector caspases 3, 6 and 7 are responsible for cleaving a number of target substrates, leading to the ultimate destruction of cells
    Language English
    Publishing date 2023-01-03
    Publishing country England
    Document type Journal Article
    ZDB-ID 2559110-1
    ISSN 2041-6539 ; 2041-6520
    ISSN (online) 2041-6539
    ISSN 2041-6520
    DOI 10.1039/d2sc05827h
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Evaluation of the effects of phosphorylation of synthetic peptide substrates on their cleavage by caspase-3 and -7.

    Maluch, Izabela / Grzymska, Justyna / Snipas, Scott J / Salvesen, Guy S / Drag, Marcin

    The Biochemical journal

    2021  Volume 478, Issue 12, Page(s) 2233–2245

    Abstract: Caspases are a family of enzymes that play roles in cell death and inflammation. It has been suggested that in the execution phase of the apoptotic pathway, caspase-3, -6 and -7 are involved. The substrate specificities of two proteases (caspases 3 and 7) ...

    Abstract Caspases are a family of enzymes that play roles in cell death and inflammation. It has been suggested that in the execution phase of the apoptotic pathway, caspase-3, -6 and -7 are involved. The substrate specificities of two proteases (caspases 3 and 7) are highly similar, which complicates the design of compounds that selectively interact with a single enzyme exclusively. The recognition of residues other than Asp in the P1 position of the substrate by caspase-3/-7 has been reported, promoting interest in the effects of phosphorylation of amino acids in the direct vicinity of the scissile bond. To evaluate conflicting reports on this subject, we synthesized a series of known caspase-3 and -7 substrates and phosphorylated analogs, performed enzyme kinetic assays and mapped the peptide cleavage sites using internally quenched fluorescent peptide substrates. Caspases 3 and 7 will tolerate pSer at the P1 position but only poorly at the P2' position. Our investigation demonstrates the importance of peptide length and composition in interpreting sequence/activity relationships. Based on the results, we conclude that the relationship between caspase-3/-7 and their substrates containing phosphorylated amino acids might depend on the steric conditions and not be directly connected with ionic interactions. Thus, the precise effect of phospho-amino acid residues located in the vicinity of the cleaved bond on the regulation of the substrate specificity of caspases remains difficult to predict. Our observations allow to predict that natural phosphorylated proteins may be cleaved by caspases, but only when extended substrate binding site interactions are satisfied.
    MeSH term(s) Adaptor Proteins, Signal Transducing/chemistry ; Binding Sites ; Caspase 3/genetics ; Caspase 3/metabolism ; Caspase 7/genetics ; Caspase 7/metabolism ; Humans ; Kinetics ; Models, Molecular ; Peptide Fragments/metabolism ; Phosphorylation ; Proteolysis ; Serine/chemistry ; Serine/metabolism ; Substrate Specificity ; Transcription Factors/chemistry ; Vimentin/chemistry
    Chemical Substances Adaptor Proteins, Signal Transducing ; Peptide Fragments ; Transcription Factors ; VIM protein, human ; Vimentin ; YAP1 protein, human ; Serine (452VLY9402) ; CASP3 protein, human (EC 3.4.22.-) ; CASP7 protein, human (EC 3.4.22.-) ; Caspase 3 (EC 3.4.22.-) ; Caspase 7 (EC 3.4.22.-)
    Language English
    Publishing date 2021-06-07
    Publishing country England
    Document type Evaluation Study ; Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2969-5
    ISSN 1470-8728 ; 0006-2936 ; 0306-3275 ; 0264-6021
    ISSN (online) 1470-8728
    ISSN 0006-2936 ; 0306-3275 ; 0264-6021
    DOI 10.1042/BCJ20210255
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Uc I Zs.110: Show issues Location:
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  3. Article ; Online: Re-emerging Aspartic Protease Targets: Examining

    Kryštůfek, Robin / Šácha, Pavel / Starková, Jana / Brynda, Jiří / Hradilek, Martin / Tloušt'ová, Eva / Grzymska, Justyna / Rut, Wioletta / Boucher, Michael J / Drąg, Marcin / Majer, Pavel / Hájek, Miroslav / Řezáčová, Pavlína / Madhani, Hiten D / Craik, Charles S / Konvalinka, Jan

    Journal of medicinal chemistry

    2021  Volume 64, Issue 10, Page(s) 6706–6719

    Abstract: Cryptococcosis is an invasive infection that accounts for 15% of AIDS-related fatalities. Still, treating cryptococcosis remains a significant challenge due to the poor availability of effective antifungal therapies and emergence of drug resistance. ... ...

    Abstract Cryptococcosis is an invasive infection that accounts for 15% of AIDS-related fatalities. Still, treating cryptococcosis remains a significant challenge due to the poor availability of effective antifungal therapies and emergence of drug resistance. Interestingly, protease inhibitor components of antiretroviral therapy regimens have shown some clinical benefits in these opportunistic infections. We investigated Major aspartyl peptidase 1 (May1), a secreted
    MeSH term(s) Antifungal Agents/chemistry ; Antifungal Agents/metabolism ; Antifungal Agents/pharmacology ; Aspartic Acid Proteases/antagonists & inhibitors ; Aspartic Acid Proteases/genetics ; Aspartic Acid Proteases/metabolism ; Binding Sites ; Catalytic Domain ; Cryptococcus neoformans/enzymology ; Crystallography, X-Ray ; Drug Evaluation, Preclinical ; Fungal Proteins/antagonists & inhibitors ; Fungal Proteins/genetics ; Fungal Proteins/metabolism ; Fungi/drug effects ; HIV/enzymology ; HIV Protease/chemistry ; HIV Protease/metabolism ; Molecular Dynamics Simulation ; Recombinant Proteins/biosynthesis ; Recombinant Proteins/chemistry ; Recombinant Proteins/isolation & purification ; Structure-Activity Relationship ; Substrate Specificity
    Chemical Substances Antifungal Agents ; Fungal Proteins ; Recombinant Proteins ; Aspartic Acid Proteases (EC 3.4.-) ; HIV Protease (EC 3.4.23.-)
    Language English
    Publishing date 2021-05-18
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 218133-2
    ISSN 1520-4804 ; 0022-2623
    ISSN (online) 1520-4804
    ISSN 0022-2623
    DOI 10.1021/acs.jmedchem.0c02177
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.B 151: Show issues Location:
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