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  1. Article ; Online: Structural Analysis of the Plasmodial Proteins ZNHIT3 and NUFIP1 Provides Insights into the Selectivity of a Conserved Interaction.

    Chagot, Marie-Eve / Boutilliat, Alexis / Kriznik, Alexandre / Quinternet, Marc

    Biochemistry

    2022  Volume 61, Issue 7, Page(s) 479–493

    Abstract: Malaria is a widespread and lethal disease caused by ... ...

    Abstract Malaria is a widespread and lethal disease caused by the
    MeSH term(s) Animals ; Anopheles ; Antimalarials/chemistry ; Humans ; Nuclear Proteins/chemistry ; Plasmodium falciparum/chemistry ; Protozoan Proteins/chemistry ; RNA-Binding Proteins/chemistry ; RNA-Binding Proteins/metabolism
    Chemical Substances Antimalarials ; Nuclear Proteins ; Protozoan Proteins ; RNA-Binding Proteins
    Language English
    Publishing date 2022-03-22
    Publishing country United States
    Document type Journal Article
    ZDB-ID 1108-3
    ISSN 1520-4995 ; 0006-2960
    ISSN (online) 1520-4995
    ISSN 0006-2960
    DOI 10.1021/acs.biochem.1c00792
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    In stock of ZB MED Cologne/Königswinter

    Zs.A 217: Show issues Location:
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  2. Article: Structural Analysis of the Plasmodial Proteins ZNHIT3 and NUFIP1 Provides Insights into the Selectivity of a Conserved Interaction

    Chagot, Marie-Eve / Boutilliat, Alexis / Kriznik, Alexandre / Quinternet, Marc

    Biochemistry. 2022 Mar. 22, v. 61, no. 7

    2022  

    Abstract: Malaria is a widespread and lethal disease caused by the Plasmodium parasites that can infect human beings through Anopheles mosquitoes. For that reason, the biology of Plasmodium needs to be studied to develop antimalarial treatments. By determining the ...

    Abstract Malaria is a widespread and lethal disease caused by the Plasmodium parasites that can infect human beings through Anopheles mosquitoes. For that reason, the biology of Plasmodium needs to be studied to develop antimalarial treatments. By determining the three-dimensional structures of macromolecules, structural biology helps to understand the function of proteins and can reveal how interactions occur between biological partners. Here, we studied the ZNHIT3 and NUFIP1 proteins from Plasmodium falciparum, two proteins tightly linked to the ribosome biology. Due to their important functions in post-translational modifications of ribosomal RNAs and in ribophagy, these proteins participate in the survival of cells. In this study, we solved the three-dimensional structure of a thermally stable and species-dependent complex between fragments of these proteins. Our results were compared to the AlphaFold predictions, which motivated the study of the free ZNHIT3 fragment that binds NUFIP1. We showed that the latter fragment multimerized in vitro but also had the inner ability to change its conformation to escape the solvent exposition of key hydrophobic residues involved in the interaction with NUFIP1. Our data could open the gate to selective drug discovery processes involving these two proteins.
    Keywords Anopheles ; Plasmodium falciparum ; antimalarials ; humans ; hydrophobicity ; malaria ; ribosomes ; solvents ; structural biology ; thermal stability
    Language English
    Dates of publication 2022-0322
    Size p. 479-493.
    Publishing place American Chemical Society
    Document type Article
    ZDB-ID 1108-3
    ISSN 1520-4995 ; 0006-2960
    ISSN (online) 1520-4995
    ISSN 0006-2960
    DOI 10.1021/acs.biochem.1c00792
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    In stock of ZB MED Cologne/Königswinter

    Zs.A 217: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
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  3. Article ; Online: Probing the mechanism of the peroxiredoxin decamer interaction with its reductase sulfiredoxin from the single molecule to the solution scale.

    Beaussart, Audrey / Canonico, Florent / Mazon, Hortense / Hidalgo, Jorge / Cianférani, Sarah / Le Cordier, Hélène / Kriznik, Alexandre / Rahuel-Clermont, Sophie

    Nanoscale horizons

    2022  Volume 7, Issue 5, Page(s) 515–525

    Abstract: Peroxiredoxins from the Prx1 subfamily (Prx) are highly regulated multifunctional proteins involved in oxidative stress response, redox signaling and cell protection. Prx is a homodimer that associates into a decamer. The monomer C-terminus plays ... ...

    Abstract Peroxiredoxins from the Prx1 subfamily (Prx) are highly regulated multifunctional proteins involved in oxidative stress response, redox signaling and cell protection. Prx is a homodimer that associates into a decamer. The monomer C-terminus plays intricate roles in Prx catalytic functions, decamer stability and interaction with its redox partner, the small reductase sulfiredoxin (Srx), that regulates the switching between Prx cellular functions. As only static structures of covalent Prx-Srx complexes have been reported, whether Srx binding dissociates the decameric assembly and how Prx subunit flexibility impacts complex formation are unknown. Here, we assessed the non-covalent interaction mechanism and dynamics in the solution of
    MeSH term(s) Biophysics ; Catalysis ; Microscopy, Atomic Force ; Oxidoreductases ; Peroxiredoxins
    Chemical Substances Oxidoreductases (EC 1.-) ; Peroxiredoxins (EC 1.11.1.15)
    Language English
    Publishing date 2022-05-03
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 2055-6764
    ISSN (online) 2055-6764
    DOI 10.1039/d2nh00037g
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  4. Article: Ascorbate Peroxidase 2 (APX2) of Chlamydomonas Binds Copper and Modulates the Copper Insertion into Plastocyanin.

    Caccamo, Anna / Vega de Luna, Félix / Wahni, Khadija / Volkov, Alexander N / Przybyla-Toscano, Jonathan / Amelii, Antonello / Kriznik, Alexandre / Rouhier, Nicolas / Messens, Joris / Remacle, Claire

    Antioxidants (Basel, Switzerland)

    2023  Volume 12, Issue 11

    Abstract: Recent phylogenetic studies have unveiled a novel class of ascorbate peroxidases called "ascorbate peroxidase-related" (APX-R). These enzymes, found in green photosynthetic eukaryotes, lack the amino acids necessary for ascorbate binding. This study ... ...

    Abstract Recent phylogenetic studies have unveiled a novel class of ascorbate peroxidases called "ascorbate peroxidase-related" (APX-R). These enzymes, found in green photosynthetic eukaryotes, lack the amino acids necessary for ascorbate binding. This study focuses on the sole APX-R from
    Language English
    Publishing date 2023-10-31
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2704216-9
    ISSN 2076-3921
    ISSN 2076-3921
    DOI 10.3390/antiox12111946
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  5. Article ; Online: Strengthening Peptoid Helicity through Sequence Site-Specific Positioning of Amide

    Rzeigui, Maha / Traikia, Mounir / Jouffret, Laurent / Kriznik, Alexandre / Khiari, Jameleddine / Roy, Olivier / Taillefumier, Claude

    The Journal of organic chemistry

    2020  Volume 85, Issue 4, Page(s) 2190–2201

    Abstract: The synthesis of biomimetic helical secondary structures is sought after for the construction of innovative nanomaterials and applications in medicinal chemistry such as the development of protein-protein interaction modulators. Peptoids, a sequence- ... ...

    Abstract The synthesis of biomimetic helical secondary structures is sought after for the construction of innovative nanomaterials and applications in medicinal chemistry such as the development of protein-protein interaction modulators. Peptoids, a sequence-defined family of oligomers, enable a peptidomimetic strategy, especially considering the easily accessible monomer diversity and peptoid helical folding propensity. However,
    Language English
    Publishing date 2020-01-13
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 123490-0
    ISSN 1520-6904 ; 0022-3263
    ISSN (online) 1520-6904
    ISSN 0022-3263
    DOI 10.1021/acs.joc.9b02916
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    In stock of ZB MED Cologne/Königswinter

    Zs.A 4473: Show issues Location:
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  6. Article: Strengthening Peptoid Helicity through Sequence Site-Specific Positioning of Amide cis-Inducing NtBu Monomers

    Rzeigui, Maha / Traikia, Mounir / Jouffret, Laurent / Kriznik, Alexandre / Khiari, Jameleddine / Roy, Olivier / Taillefumier, Claude

    Journal of organic chemistry. 2019 Dec. 24, v. 85, no. 4

    2019  

    Abstract: The synthesis of biomimetic helical secondary structures is sought after for the construction of innovative nanomaterials and applications in medicinal chemistry such as the development of protein–protein interaction modulators. Peptoids, a sequence- ... ...

    Abstract The synthesis of biomimetic helical secondary structures is sought after for the construction of innovative nanomaterials and applications in medicinal chemistry such as the development of protein–protein interaction modulators. Peptoids, a sequence-defined family of oligomers, enable a peptidomimetic strategy, especially considering the easily accessible monomer diversity and peptoid helical folding propensity. However, cis–trans isomerization of the backbone tertiary amides may impair the peptoid’s adoption of stable secondary structures, notably the all-cis polyproline I-like helical conformation. Here, we show that cis-inducing NtBu achiral monomers strategically positioned within chiral sequences may reinforce the degree of peptoid helicity, although with a reduced content of chiral side chains. The design principles presented here will undoubtedly help achieve more conformationally stable helical peptoids with desired functions.
    Keywords N-substituted glycines ; amides ; biomimetics ; chemical structure ; cis-trans isomerism ; nanomaterials ; organic chemistry ; protein-protein interactions
    Language English
    Dates of publication 2019-1224
    Size p. 2190-2201.
    Publishing place American Chemical Society
    Document type Article
    ZDB-ID 123490-0
    ISSN 1520-6904 ; 0022-3263
    ISSN (online) 1520-6904
    ISSN 0022-3263
    DOI 10.1021/acs.joc.9b02916
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    In stock of ZB MED Bonn / Germany

    Z 4' 49/42: Show issues
    Z 7.1: Show issues

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  7. Article: Effect of nonenzymatic deamidation on the structure stability of Camelus dromedarius α-lactalbumin

    Si Ahmed Zennia, Saliha / Mati, Abderrahmane / Charron, Christophe / Cakir-Kiefer, Céline / Kriznik, Alexandre / Girardet, Jean-Michel

    Food chemistry. 2019 Sept. 01, v. 291

    2019  

    Abstract: Camelid α-lactalbumin is the only known protein that can undergo nonenzymatic deamidation on two Asn residues. This leads to the generation of a mixture of unusual isoAsp and d-Asp residues that may impact health. The effect of deamidation on camel α- ... ...

    Abstract Camelid α-lactalbumin is the only known protein that can undergo nonenzymatic deamidation on two Asn residues. This leads to the generation of a mixture of unusual isoAsp and d-Asp residues that may impact health. The effect of deamidation on camel α-lactalbumin instability was investigated. Circular dichroism showed that the altered protein acquired secondary structure resulting in an increase in α-helix content. In good agreement, the 3D structure of camel α-lactalbumin determined by X-ray crystallography, displayed a short additional α-helix probably induced by deamidation, compared to the human and bovine counterparts. This α-helix was located in the C-terminal region and included residues 101–106. Differential scanning calorimetry together with the susceptibility to thermolysin showed that the deamidation process reinforced the structural stability of the α-lactalbumin at high temperature and its resistance toward proteolysis.
    Keywords Camelus dromedarius ; X-ray diffraction ; camels ; cattle ; circular dichroism spectroscopy ; deamidation ; differential scanning calorimetry ; lactalbumin ; proteolysis ; temperature ; thermolysin
    Language English
    Dates of publication 2019-0901
    Size p. 207-213.
    Publishing place Elsevier Ltd
    Document type Article
    ZDB-ID 243123-3
    ISSN 1873-7072 ; 0308-8146
    ISSN (online) 1873-7072
    ISSN 0308-8146
    DOI 10.1016/j.foodchem.2019.04.033
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    Z 3634: Show issues

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  8. Article ; Online: Splice variants of protein disulfide isomerase - identification, distribution and functional characterization in the rat.

    Chetot, Thomas / Serfaty, Xavier / Carret, Léna / Kriznik, Alexandre / Sophie-Rahuel-Clermont / Grand, Lucie / Jacolot, Maïwenn / Popowycz, Florence / Benoit, Etienne / Lambert, Véronique / Lattard, Virginie

    Biochimica et biophysica acta. General subjects

    2022  Volume 1867, Issue 2, Page(s) 130280

    Abstract: Background: Protein Disulfide Isomerase (PDI) enzyme is an emerging therapeutic target in oncology and hematology. Although PDI reductase activity has been studied with isolated fragments of the protein, natural structural variations affecting reductase ...

    Abstract Background: Protein Disulfide Isomerase (PDI) enzyme is an emerging therapeutic target in oncology and hematology. Although PDI reductase activity has been studied with isolated fragments of the protein, natural structural variations affecting reductase activity have not been addressed.
    Methods: In this study, we discovered four coding splice variants of the Pdi pre-mRNA in rats. In vitro Michaelis constants and apparent maximum steady-state rate constants after purification and distribution in different rat tissues were determined.
    Results: The consensus sequence was found to be the most expressed splice variant while the second most expressed variant represents 15 to 35% of total Pdi mRNA. The third variant shows a quasi-null expression profile and the fourth was not quantifiable. The consensus sequence splice variant and the second splice variant are widely expressed (transcription level) in the liver and even more present in males. Measurements of the reductase activity of recombinant PDI indicate that the consensus sequence and third splice variant are fully active variants. The second most expressed variant, differing by a lack of signal peptide, was found active but less than the consensus sequence.
    General significance: Our work emphasizes the importance of taking splice variants into account when studying PDI-like proteins to understand the full biological functionalities of PDI.
    MeSH term(s) Male ; Rats ; Animals ; Protein Disulfide-Isomerases/genetics ; Protein Disulfide-Isomerases/metabolism ; Protein Sorting Signals ; Liver/metabolism ; RNA, Messenger/metabolism ; Oxidoreductases/metabolism
    Chemical Substances Protein Disulfide-Isomerases (EC 5.3.4.1) ; Protein Sorting Signals ; RNA, Messenger ; Oxidoreductases (EC 1.-)
    Language English
    Publishing date 2022-11-22
    Publishing country Netherlands
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 60-7
    ISSN 1872-8006 ; 1879-2596 ; 1879-260X ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    ISSN (online) 1872-8006 ; 1879-2596 ; 1879-260X ; 1879-2642 ; 1879-2618 ; 1879-2650
    ISSN 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    DOI 10.1016/j.bbagen.2022.130280
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    Uc I Zs.247: Show issues Location:
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    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
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  9. Article: Dynamics of a Key Conformational Transition in the Mechanism of Peroxiredoxin Sulfinylation.

    Kriznik, Alexandre / Libiad, Marouane / Le Cordier, Hélène / Boukhenouna, Samia / Toledano, Michel B / Rahuel-Clermont, Sophie

    ACS catalysis

    2020  Volume 10, Issue 5, Page(s) 3326–3339

    Abstract: Peroxiredoxins from the Prx1 subfamily (Prx) are moonlighting peroxidases that operate in peroxide signaling and are regulated by sulfinylation. Prxs offer a major model of protein-thiol oxidative modification. They react with ... ...

    Abstract Peroxiredoxins from the Prx1 subfamily (Prx) are moonlighting peroxidases that operate in peroxide signaling and are regulated by sulfinylation. Prxs offer a major model of protein-thiol oxidative modification. They react with H
    Language English
    Publishing date 2020-01-31
    Publishing country United States
    Document type Journal Article
    ISSN 2155-5435
    ISSN 2155-5435
    DOI 10.1021/acscatal.9b04471
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  10. Article ; Online: Thiol Redox Regulation of Plant β-Carbonic Anhydrase.

    Dreyer, Anna / Schackmann, Alexander / Kriznik, Alexandre / Chibani, Kamel / Wesemann, Corinna / Vogelsang, Lara / Beyer, André / Dietz, Karl-Josef

    Biomolecules

    2020  Volume 10, Issue 8

    Abstract: β-carbonic anhydrases (βCA) accelerate the equilibrium formation between ... ...

    Abstract β-carbonic anhydrases (βCA) accelerate the equilibrium formation between CO
    MeSH term(s) Arabidopsis/metabolism ; Arabidopsis Proteins/metabolism ; Carbonic Anhydrases/metabolism ; Models, Molecular ; Oxidation-Reduction ; Sulfhydryl Compounds/metabolism ; Thioredoxins/metabolism
    Chemical Substances Arabidopsis Proteins ; Sulfhydryl Compounds ; Thioredoxins (52500-60-4) ; Carbonic Anhydrases (EC 4.2.1.1)
    Language English
    Publishing date 2020-07-30
    Publishing country Switzerland
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2701262-1
    ISSN 2218-273X ; 2218-273X
    ISSN (online) 2218-273X
    ISSN 2218-273X
    DOI 10.3390/biom10081125
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