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  1. AU="Zargarian, Loussiné"
  2. AU=Hascalovici Jacob
  3. AU="Spagnolo, Jennifer B"
  4. AU="Anderloni, Giulia"
  5. AU="Ahmad, Shoaib"
  6. AU="Du, Roujia"
  7. AU="Colmenero-Repiso, Ana"
  8. AU="Alvarez-Carbonell, David"
  9. AU="Phelippeau, Michael"
  10. AU="Lunghi, Laura"
  11. AU=Giersiepen Klaus
  12. AU="Drobyshev, Sergey"
  13. AU="Timme, Kathleen H"
  14. AU=Sfriso Paolo
  15. AU="Kim, John S"
  16. AU=Farkash Evan A AU=Farkash Evan A
  17. AU="Xia, Xueqian"

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  1. Artikel: Investigation of the Low-Populated Excited States of the HIV-1 Nucleocapsid Domain

    Mouhand, Assia / Zargarian, Loussiné / Belfetmi, Anissa / Catala, Marjorie / Pasi, Marco / Lescop, Ewen / Tisné, Carine / Mauffret, Olivier

    Viruses. 2022 Mar. 18, v. 14, no. 3

    2022  

    Abstract: The nucleocapsid domain (NCd), located at the C-terminus of the HIV-1 Gag protein, is involved in numerous stages of the replication cycle, such as the packaging of the viral genome and reverse transcription. It exists under different forms through the ... ...

    Abstract The nucleocapsid domain (NCd), located at the C-terminus of the HIV-1 Gag protein, is involved in numerous stages of the replication cycle, such as the packaging of the viral genome and reverse transcription. It exists under different forms through the viral life cycle, depending on the processing of Gag by the HIV-1 protease. NCd is constituted of two adjacent zinc knuckles (ZK1 and ZK2), separated by a flexible linker and flanked by disordered regions. Here, conformational equilibria between a major and two minor states were highlighted exclusively in ZK2, by using CPMG and CEST NMR experiments. These minor states appear to be temperature dependent, and their populations are highest at physiological temperature. These minor states are present both in NCp7, the mature form of NCd, and in NCp9 and NCp15, the precursor forms of NCd, with increased populations. The role of these minor states in the targeting of NCd by drugs and its binding properties is discussed.
    Schlagwörter nucleocapsid ; proteinases ; reverse transcription ; temperature ; viral genome ; zinc
    Sprache Englisch
    Erscheinungsverlauf 2022-0318
    Erscheinungsort Multidisciplinary Digital Publishing Institute
    Dokumenttyp Artikel
    ZDB-ID 2516098-9
    ISSN 1999-4915
    ISSN 1999-4915
    DOI 10.3390/v14030632
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  2. Artikel ; Online: Investigation of the Low-Populated Excited States of the HIV-1 Nucleocapsid Domain.

    Mouhand, Assia / Zargarian, Loussiné / Belfetmi, Anissa / Catala, Marjorie / Pasi, Marco / Lescop, Ewen / Tisné, Carine / Mauffret, Olivier

    Viruses

    2022  Band 14, Heft 3

    Abstract: The nucleocapsid domain (NCd), located at the C-terminus of the HIV-1 Gag protein, is involved in numerous stages of the replication cycle, such as the packaging of the viral genome and reverse transcription. It exists under different forms through the ... ...

    Abstract The nucleocapsid domain (NCd), located at the C-terminus of the HIV-1 Gag protein, is involved in numerous stages of the replication cycle, such as the packaging of the viral genome and reverse transcription. It exists under different forms through the viral life cycle, depending on the processing of Gag by the HIV-1 protease. NCd is constituted of two adjacent zinc knuckles (ZK1 and ZK2), separated by a flexible linker and flanked by disordered regions. Here, conformational equilibria between a major and two minor states were highlighted exclusively in ZK2, by using CPMG and CEST NMR experiments. These minor states appear to be temperature dependent, and their populations are highest at physiological temperature. These minor states are present both in NCp7, the mature form of NCd, and in NCp9 and NCp15, the precursor forms of NCd, with increased populations. The role of these minor states in the targeting of NCd by drugs and its binding properties is discussed.
    Mesh-Begriff(e) Capsid Proteins/metabolism ; HIV-1/physiology ; Nucleocapsid/metabolism ; RNA, Viral/metabolism ; Virion/metabolism ; gag Gene Products, Human Immunodeficiency Virus/metabolism
    Chemische Substanzen Capsid Proteins ; RNA, Viral ; gag Gene Products, Human Immunodeficiency Virus
    Sprache Englisch
    Erscheinungsdatum 2022-03-18
    Erscheinungsland Switzerland
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2516098-9
    ISSN 1999-4915 ; 1999-4915
    ISSN (online) 1999-4915
    ISSN 1999-4915
    DOI 10.3390/v14030632
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  3. Artikel: Overview of the Nucleic-Acid Binding Properties of the HIV-1 Nucleocapsid Protein in Its Different Maturation States

    Mouhand, Assia / Pasi, Marco / Catala, Marjorie / Zargarian, Loussiné / Belfetmi, Anissa / Barraud, Pierre / Mauffret, Olivier / Tisné, Carine

    Viruses. 2020 Sept. 29, v. 12, no. 10

    2020  

    Abstract: HIV-1 Gag polyprotein orchestrates the assembly of viral particles. Its C-terminus consists of the nucleocapsid (NC) domain that interacts with nucleic acids, and p1 and p6, two unstructured regions, p6 containing the motifs to bind ALIX, the cellular ... ...

    Abstract HIV-1 Gag polyprotein orchestrates the assembly of viral particles. Its C-terminus consists of the nucleocapsid (NC) domain that interacts with nucleic acids, and p1 and p6, two unstructured regions, p6 containing the motifs to bind ALIX, the cellular ESCRT factor TSG101 and the viral protein Vpr. The processing of Gag by the viral protease subsequently liberates NCp15 (NC-p1-p6), NCp9 (NC-p1) and NCp7, NCp7 displaying the optimal chaperone activity of nucleic acids. This review focuses on the nucleic acid binding properties of the NC domain in the different maturation states during the HIV-1 viral cycle.
    Schlagwörter Human immunodeficiency virus 1 ; binding properties ; nucleic acids ; nucleocapsid ; nucleocapsid proteins ; polyproteins ; proteinases ; virion
    Sprache Englisch
    Erscheinungsverlauf 2020-0929
    Erscheinungsort Multidisciplinary Digital Publishing Institute
    Dokumenttyp Artikel
    ZDB-ID 2516098-9
    ISSN 1999-4915
    ISSN 1999-4915
    DOI 10.3390/v12101109
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  4. Artikel ; Online: Structure and Function of Adsorbed Hemoglobin on Silica Nanoparticles: Relationship between the Adsorption Process and the Oxygen Binding Properties.

    Devineau, Stéphanie / Zargarian, Loussiné / Renault, Jean Philippe / Pin, Serge

    Langmuir : the ACS journal of surfaces and colloids

    2017  Band 33, Heft 13, Seite(n) 3241–3252

    Abstract: The connection between the mechanisms of protein adsorption on nanoparticles and the structural and functional properties of the adsorbed protein often remains unclear. We investigate porcine hemoglobin adsorption on silica nanoparticles, and we analyze ... ...

    Abstract The connection between the mechanisms of protein adsorption on nanoparticles and the structural and functional properties of the adsorbed protein often remains unclear. We investigate porcine hemoglobin adsorption on silica nanoparticles, and we analyze the structural and functional modifications of adsorbed hemoglobin by UV-vis spectrophotometry, circular dichroism, and oxygen binding measurement. The structural analysis of adsorbed hemoglobin on silica nanoparticles reveals a significant loss of secondary structure and a preservation of the heme electronic structure. However, adsorbed hemoglobin retains its quaternary structure and exhibits an enhanced oxygen affinity with cooperative binding. Moreover, the structural and functional modifications are fully reversible after complete desorption from silica nanoparticles at pH 8.7. The tunable adsorption and desorption of hemoglobin on SNPs with pH change, and the full control of hemoglobin activity by pH, temperature, and the addition of inorganic phosphate effectors opens the way to an interesting system whereby protein adsorption on nanoparticles can allow for full control over hemoglobin oxygen binding activity. Our results suggest that adsorption of hemoglobin on silica nanoparticles leads to a new structural, functional, and dynamic state with full reversibility in a way that significantly differs from protein denaturation.
    Mesh-Begriff(e) Adsorption ; Binding Sites ; Hemoglobins/chemistry ; Hydrogen-Ion Concentration ; Models, Molecular ; Molecular Structure ; Nanoparticles/chemistry ; Oxygen/chemistry ; Silicon Dioxide/chemistry
    Chemische Substanzen Hemoglobins ; Silicon Dioxide (7631-86-9) ; Oxygen (S88TT14065)
    Sprache Englisch
    Erscheinungsdatum 2017-03-23
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2005937-1
    ISSN 1520-5827 ; 0743-7463
    ISSN (online) 1520-5827
    ISSN 0743-7463
    DOI 10.1021/acs.langmuir.6b04281
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  5. Artikel ; Online: Overview of the Nucleic-Acid Binding Properties of the HIV-1 Nucleocapsid Protein in Its Different Maturation States.

    Mouhand, Assia / Pasi, Marco / Catala, Marjorie / Zargarian, Loussiné / Belfetmi, Anissa / Barraud, Pierre / Mauffret, Olivier / Tisné, Carine

    Viruses

    2020  Band 12, Heft 10

    Abstract: HIV-1 Gag polyprotein orchestrates the assembly of viral particles. Its C-terminus consists of the nucleocapsid (NC) domain that interacts with nucleic acids, and p1 and p6, two unstructured regions, p6 containing the motifs to bind ALIX, the cellular ... ...

    Abstract HIV-1 Gag polyprotein orchestrates the assembly of viral particles. Its C-terminus consists of the nucleocapsid (NC) domain that interacts with nucleic acids, and p1 and p6, two unstructured regions, p6 containing the motifs to bind ALIX, the cellular ESCRT factor TSG101 and the viral protein Vpr. The processing of Gag by the viral protease subsequently liberates NCp15 (NC-p1-p6), NCp9 (NC-p1) and NCp7, NCp7 displaying the optimal chaperone activity of nucleic acids. This review focuses on the nucleic acid binding properties of the NC domain in the different maturation states during the HIV-1 viral cycle.
    Mesh-Begriff(e) DNA-Binding Proteins ; Endosomal Sorting Complexes Required for Transport ; HIV-1/genetics ; HIV-1/metabolism ; Nucleic Acids/chemistry ; Nucleocapsid/metabolism ; Nucleocapsid Proteins/metabolism ; Protein Binding ; RNA, Viral ; Transcription Factors ; Virion/metabolism ; gag Gene Products, Human Immunodeficiency Virus/chemistry ; gag Gene Products, Human Immunodeficiency Virus/metabolism
    Chemische Substanzen DNA-Binding Proteins ; Endosomal Sorting Complexes Required for Transport ; NCP7 protein, Human immunodeficiency virus 1 ; Nucleic Acids ; Nucleocapsid Proteins ; RNA, Viral ; Transcription Factors ; Tsg101 protein ; gag Gene Products, Human Immunodeficiency Virus ; p15 gag protein, Human immunodeficiency virus 1
    Sprache Englisch
    Erscheinungsdatum 2020-09-29
    Erscheinungsland Switzerland
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2516098-9
    ISSN 1999-4915 ; 1999-4915
    ISSN (online) 1999-4915
    ISSN 1999-4915
    DOI 10.3390/v12101109
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  6. Artikel: Structure and Function of Adsorbed Hemoglobin on Silica Nanoparticles: Relationship between the Adsorption Process and the Oxygen Binding Properties

    Devineau, Stéphanie / Pin Serge / Renault Jean Philippe / Zargarian Loussiné

    Langmuir. 2017 Apr. 04, v. 33, no. 13

    2017  

    Abstract: The connection between the mechanisms of protein adsorption on nanoparticles and the structural and functional properties of the adsorbed protein often remains unclear. We investigate porcine hemoglobin adsorption on silica nanoparticles, and we analyze ... ...

    Abstract The connection between the mechanisms of protein adsorption on nanoparticles and the structural and functional properties of the adsorbed protein often remains unclear. We investigate porcine hemoglobin adsorption on silica nanoparticles, and we analyze the structural and functional modifications of adsorbed hemoglobin by UV–vis spectrophotometry, circular dichroism, and oxygen binding measurement. The structural analysis of adsorbed hemoglobin on silica nanoparticles reveals a significant loss of secondary structure and a preservation of the heme electronic structure. However, adsorbed hemoglobin retains its quaternary structure and exhibits an enhanced oxygen affinity with cooperative binding. Moreover, the structural and functional modifications are fully reversible after complete desorption from silica nanoparticles at pH 8.7. The tunable adsorption and desorption of hemoglobin on SNPs with pH change, and the full control of hemoglobin activity by pH, temperature, and the addition of inorganic phosphate effectors opens the way to an interesting system whereby protein adsorption on nanoparticles can allow for full control over hemoglobin oxygen binding activity. Our results suggest that adsorption of hemoglobin on silica nanoparticles leads to a new structural, functional, and dynamic state with full reversibility in a way that significantly differs from protein denaturation.
    Schlagwörter adsorption ; binding properties ; circular dichroism spectroscopy ; desorption ; heme ; hemoglobin ; nanoparticles ; oxygen ; pH ; phosphates ; protein denaturation ; silica ; swine ; temperature ; ultraviolet-visible spectroscopy
    Sprache Englisch
    Erscheinungsverlauf 2017-0404
    Umfang p. 3241-3252.
    Erscheinungsort American Chemical Society
    Dokumenttyp Artikel
    ZDB-ID 2005937-1
    ISSN 1520-5827 ; 0743-7463
    ISSN (online) 1520-5827
    ISSN 0743-7463
    DOI 10.1021%2Facs.langmuir.6b04281
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  7. Artikel ; Online: 1

    Larue, Valéry / Catala, Marjorie / Belfetmi, Anissa / Zargarian, Loussiné / Mauffret, Olivier / Tisné, Carine

    Biomolecular NMR assignments

    2018  Band 12, Heft 1, Seite(n) 139–143

    Abstract: During HIV-1 assembly, the ... ...

    Abstract During HIV-1 assembly, the Pr55
    Mesh-Begriff(e) Nuclear Magnetic Resonance, Biomolecular ; Protein Domains ; Protein Precursors/chemistry
    Chemische Substanzen Protein Precursors ; p55 gag precursor protein, Human immunodeficiency virus 1
    Sprache Englisch
    Erscheinungsdatum 2018-01-13
    Erscheinungsland Netherlands
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2388861-1
    ISSN 1874-270X ; 1874-2718
    ISSN (online) 1874-270X
    ISSN 1874-2718
    DOI 10.1007/s12104-017-9796-x
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  8. Artikel ; Online: Antitumor Activity and Mechanism of Action of Hormonotoxin, an LHRH Analog Conjugated to Dermaseptin-B2, a Multifunctional Antimicrobial Peptide.

    Couty, Mickael / Dusaud, Marie / Miro-Padovani, Mickael / Zhang, Liuhui / Zadigue, Patricia / Zargarian, Loussiné / Lequin, Olivier / de la Taille, Alexandre / Delbe, Jean / Hamma-Kourbali, Yamina / Amiche, Mohamed

    International journal of molecular sciences

    2021  Band 22, Heft 21

    Abstract: Prostate cancer is the most common cancer in men. For patients with advanced or metastatic prostate cancer, available treatments can slow down its progression but cannot cure it. The development of innovative drugs resulting from the exploration of ... ...

    Abstract Prostate cancer is the most common cancer in men. For patients with advanced or metastatic prostate cancer, available treatments can slow down its progression but cannot cure it. The development of innovative drugs resulting from the exploration of biodiversity could open new therapeutic alternatives. Dermaseptin-B2, a natural multifunctional antimicrobial peptide isolated from Amazonian frog skin, has been reported to possess antitumor activity. To improve its pharmacological properties and to decrease its peripheral toxicity and lethality we developed a hormonotoxin molecule composed of dermaseptin-B2 combined with d-Lys
    Mesh-Begriff(e) Amino Acid Sequence ; Amphibian Proteins/metabolism ; Amphibian Proteins/pharmacology ; Animals ; Anti-Bacterial Agents/pharmacology ; Antimicrobial Cationic Peptides/metabolism ; Antimicrobial Cationic Peptides/pharmacology ; Antimicrobial Peptides/metabolism ; Antimicrobial Peptides/pharmacology ; Antineoplastic Agents/pharmacology ; Apoptosis/drug effects ; Cell Line, Tumor/drug effects ; Cell Movement/drug effects ; Cell Survival/drug effects ; Gonadotropin-Releasing Hormone/analogs & derivatives ; Gonadotropin-Releasing Hormone/metabolism ; Gonadotropin-Releasing Hormone/pharmacology ; Humans ; Immunologic Factors/metabolism ; Mice ; Mice, Nude ; Neoplasms/drug therapy ; Neoplasms/metabolism ; Xenograft Model Antitumor Assays
    Chemische Substanzen Amphibian Proteins ; Anti-Bacterial Agents ; Antimicrobial Cationic Peptides ; Antimicrobial Peptides ; Antineoplastic Agents ; Immunologic Factors ; dermaseptin B2, Phyllomedusa bicolor ; dermaseptin (136212-91-4) ; Gonadotropin-Releasing Hormone (33515-09-2)
    Sprache Englisch
    Erscheinungsdatum 2021-10-20
    Erscheinungsland Switzerland
    Dokumenttyp Journal Article
    ZDB-ID 2019364-6
    ISSN 1422-0067 ; 1422-0067 ; 1661-6596
    ISSN (online) 1422-0067
    ISSN 1422-0067 ; 1661-6596
    DOI 10.3390/ijms222111303
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  9. Artikel: NMR Studies of DNA Support the Role of Pre-Existing Minor Groove Variations in Nucleosome Indirect Readout

    Xu, Xiaoqian / Ben Imeddourene Akli / Zargarian Loussiné / Foloppe Nicolas / Mauffret Olivier / Hartmann Brigitte

    Biochemistry. 2014 Sept. 09, v. 53, no. 35

    2014  

    Abstract: We investigated how the intrinsic sequence-dependent properties probed via the phosphate linkages (BI ↔ BII equilibrium) influence the preferred shape of free DNA, and how this affects the nucleosome formation. First, this exploits NMR solution studies ...

    Abstract We investigated how the intrinsic sequence-dependent properties probed via the phosphate linkages (BI ↔ BII equilibrium) influence the preferred shape of free DNA, and how this affects the nucleosome formation. First, this exploits NMR solution studies of four B-DNA dodecamers that together cover 39 base pairs of the 5′ half of the sequence 601, of special interest for nucleosome formation. The results validate our previous prediction of a systematic, general sequence effect on the intrinsic backbone BII propensities. NMR provides new evidence that the backbone behavior is intimately coupled to the minor groove width. Second, application of the backbone behavior predictions to the full sequence 601 and other relevant sequences demonstrates that alternation of intrinsic low and high BII propensities, coupled to intrinsic narrow and wide minor grooves, largely coincides with the sinusoidal variations of the DNA minor groove width observed in crystallographic structures of the nucleosome. This correspondence is much poorer with low affinity sequences. Overall, the results indicate that nucleosome formation involves an indirect readout process implicating pre-existing DNA minor groove conformations. It also illustrates how the prediction of the intrinsic structural DNA behavior offers a powerful framework to gain explanatory insight on how proteins read DNA.
    Schlagwörter B-DNA ; nuclear magnetic resonance spectroscopy ; nucleosomes ; phosphates ; prediction
    Sprache Englisch
    Erscheinungsverlauf 2014-0909
    Umfang p. 5601-5612.
    Erscheinungsort American Chemical Society
    Dokumenttyp Artikel
    ZDB-ID 1108-3
    ISSN 1520-4995 ; 0006-2960
    ISSN (online) 1520-4995
    ISSN 0006-2960
    DOI 10.1021%2Fbi500504y
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  10. Artikel ; Online: Identification of acylation products in SHAPE chemistry.

    Lin, Chaoqi / Poyer, Salomé / Zargarian, Loussiné / Salpin, Jean-Yves / Fossé, Philippe / Mauffret, Olivier / Xie, Juan

    Bioorganic & medicinal chemistry letters

    2017  Band 27, Heft 11, Seite(n) 2506–2509

    Abstract: SHAPE chemistry (selective 2'-hydroxyl acylation analyzed by primer extension) has been developed to specifically target flexible nucleotides (often unpaired nucleotides) independently to their purine or pyrimidine nature for RNA secondary structure ... ...

    Abstract SHAPE chemistry (selective 2'-hydroxyl acylation analyzed by primer extension) has been developed to specifically target flexible nucleotides (often unpaired nucleotides) independently to their purine or pyrimidine nature for RNA secondary structure determination. However, to the best of our knowledge, the structure of 2'-O-acylation products has never been confirmed by NMR or X-ray data. We have realized the acylation reactions between cNMP and NMIA under SHAPE chemistry conditions and identified the acylation products using standard NMR spectroscopy and LC-MS/MS experiments. For cAMP and cGMP, the major acylation product is the 2'-O-acylated compound (>99%). A trace amount of N-acylated cAMP has also been identified by LC-UV-MS
    Mesh-Begriff(e) Acylation ; Magnetic Resonance Spectroscopy ; Nitrosamines/chemistry ; Nucleic Acid Conformation ; Nucleotides/chemistry ; RNA/chemistry ; Tandem Mass Spectrometry
    Chemische Substanzen Nitrosamines ; Nucleotides ; methylisoamylnitrosamine (35606-38-3) ; RNA (63231-63-0)
    Sprache Englisch
    Erscheinungsdatum 2017--01
    Erscheinungsland England
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1063195-1
    ISSN 1464-3405 ; 0960-894X
    ISSN (online) 1464-3405
    ISSN 0960-894X
    DOI 10.1016/j.bmcl.2017.03.096
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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