LIVIVO - The Search Portal for Life Sciences

zur deutschen Oberfläche wechseln
Advanced search

Search results

Result 1 - 10 of total 81

Search options

  1. Article ; Online: Multivalent Calixarene Complexation of a Designed Pentameric Lectin.

    Flood, Ronan J / Cerofolini, Linda / Fragai, Marco / Crowley, Peter B

    Biomacromolecules

    2024  Volume 25, Issue 2, Page(s) 1303–1309

    Abstract: We describe complex formation between a designed pentameric β-propeller and the anionic macrocycle sulfonato-calix[8]arene ( ...

    Abstract We describe complex formation between a designed pentameric β-propeller and the anionic macrocycle sulfonato-calix[8]arene (
    MeSH term(s) Calixarenes/chemistry ; Lectins ; Crystallography, X-Ray ; Magnetic Resonance Spectroscopy ; Binding Sites
    Chemical Substances Calixarenes (130036-26-9) ; Lectins
    Language English
    Publishing date 2024-01-16
    Publishing country United States
    Document type Journal Article
    ISSN 1526-4602
    ISSN (online) 1526-4602
    DOI 10.1021/acs.biomac.3c01280
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

    Inter-library loan at ZB MED

    Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

  2. Article ; Online: Solid-state NMR methods for the characterization of bioconjugations and protein-material interactions.

    Cerofolini, Linda / Parigi, Giacomo / Ravera, Enrico / Fragai, Marco / Luchinat, Claudio

    Solid state nuclear magnetic resonance

    2022  Volume 122, Page(s) 101828

    Abstract: Protein solid-state NMR has evolved dramatically over the last two decades, with the development of new hardware and sample preparation methodologies. This technique is now ripe for complex applications, among which one can count bioconjugation, protein ... ...

    Abstract Protein solid-state NMR has evolved dramatically over the last two decades, with the development of new hardware and sample preparation methodologies. This technique is now ripe for complex applications, among which one can count bioconjugation, protein chemistry and functional biomaterials. In this review, we provide our account on this aspect of protein solid-state NMR.
    MeSH term(s) Magnetic Resonance Spectroscopy/methods ; Proteins/chemistry ; Magnetic Resonance Imaging
    Chemical Substances Proteins
    Language English
    Publishing date 2022-09-24
    Publishing country Netherlands
    Document type Review ; Journal Article
    ZDB-ID 1122088-0
    ISSN 1527-3326 ; 0926-2040
    ISSN (online) 1527-3326
    ISSN 0926-2040
    DOI 10.1016/j.ssnmr.2022.101828
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 4368: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  3. Article ; Online: Integration of NMR Spectroscopy in an Analytical Workflow to Evaluate the Effects of Oxidative Stress on Abituzumab: Beyond the Fingerprint of mAbs

    Cerofolini, Linda / Ravera, Enrico / Fischer, Christian / Trovato, Andrea / Sacco, Francesca / Palinsky, Wolf / Angiuoni, Gabriella / Fragai, Marco / Baroni, Fabio

    Analytical Chemistry. 2023 June 06, v. 95, no. 24 p.9199-9206

    2023  

    Abstract: The assessment of the higher-order structure (HOS) by NMR is a powerful methodology to characterize the structural features of biologics. Forced oxidative stress studies are used to investigate the stability profile, to develop pharmaceutical ... ...

    Abstract The assessment of the higher-order structure (HOS) by NMR is a powerful methodology to characterize the structural features of biologics. Forced oxidative stress studies are used to investigate the stability profile, to develop pharmaceutical formulations and analytical methods. Here, the effects of forced oxidative stress by H₂O₂ on the monoclonal antibody Abituzumab have been characterized by a multianalytical approach combining NMR spectroscopy, mass spectrometry, differential scanning calorimetry, surface plasmon resonance, computational tools, and bioassays. This integrated strategy has provided qualitative and semiquantitative characterization of the samples and information at residue level of the effects that oxidation has on the HOS of Abituzumab, correlating them to the loss of the biological activity.
    Keywords analytical chemistry ; bioactive properties ; calorimetry ; mass spectrometry ; monoclonal antibodies ; nuclear magnetic resonance spectroscopy ; oxidation ; oxidative stress ; surface plasmon resonance
    Language English
    Dates of publication 2023-0606
    Size p. 9199-9206.
    Publishing place American Chemical Society
    Document type Article ; Online
    ZDB-ID 1508-8
    ISSN 1520-6882 ; 0003-2700
    ISSN (online) 1520-6882
    ISSN 0003-2700
    DOI 10.1021/acs.analchem.3c00317
    Database NAL-Catalogue (AGRICOLA)

    More links

    Kategorien

    In stock of ZB MED Bonn / Germany

    Z 4' 52/94: Show issues
    Z 2.9: Show issues

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

    Inter-library loan at ZB MED

    Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

  4. Article ; Online: NMR of Immobilized Enzymes.

    Cerofolini, Linda / Ravera, Enrico / Fragai, Marco / Luchinat, Claudio

    Methods in molecular biology (Clifton, N.J.)

    2020  Volume 2100, Page(s) 363–383

    Abstract: Solid-state NMR has become the method of choice for the assessment of protein structure for insoluble objects lacking long-range order. In this context, it is apparent that solid-state NMR is also perfectly poised toward the characterization of ... ...

    Abstract Solid-state NMR has become the method of choice for the assessment of protein structure for insoluble objects lacking long-range order. In this context, it is apparent that solid-state NMR is also perfectly poised toward the characterization of immobilized proteins. For these systems, it is possible to understand at the atomic level which perturbations, if any, are occurring as a result of the functionalization. Here we describe how it is possible to accomplish the NMR characterization of enzymes that have been immobilized through different approaches, and we introduce the reader to the choice of the experimental strategy that can be useful in different cases. An outlook on the level of information that can be attained is also given, in view of recent methodological advancements.
    MeSH term(s) Enzymes, Immobilized/chemistry ; Immobilized Proteins/chemistry ; Models, Molecular ; Nuclear Magnetic Resonance, Biomolecular/methods ; Protein Conformation
    Chemical Substances Enzymes, Immobilized ; Immobilized Proteins
    Language English
    Publishing date 2020-01-14
    Publishing country United States
    Document type Journal Article
    ISSN 1940-6029
    ISSN (online) 1940-6029
    DOI 10.1007/978-1-0716-0215-7_24
    Database MEDical Literature Analysis and Retrieval System OnLINE

    Full text online

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

    Inter-library loan at ZB MED

    Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

  5. Article ; Online: Characterization of lanthanoid-binding proteins using NMR spectroscopy.

    Ravera, Enrico / Cerofolini, Linda / Fragai, Marco / Parigi, Giacomo / Luchinat, Claudio

    Methods in enzymology

    2021  Volume 651, Page(s) 103–137

    Abstract: The variety of magnetic properties exhibited by paramagnetic lanthanoids provides outstanding information in NMR-based structural biology and therefore can be a very useful tool for characterizing lanthanoid-binding proteins. Because of their dependence ... ...

    Abstract The variety of magnetic properties exhibited by paramagnetic lanthanoids provides outstanding information in NMR-based structural biology and therefore can be a very useful tool for characterizing lanthanoid-binding proteins. Because of their dependence on the relative positions of the protein nuclei and of the lanthanoid ion, the paramagnetic restraints (PCS, PRDC and PRE) provide information on structure and dynamics of proteins. In this Chapter, we cover the use of lanthanoids in structural biology including protein sample preparation, NMR experiments and data interpretation.
    MeSH term(s) Carrier Proteins ; Lanthanoid Series Elements ; Magnetic Resonance Spectroscopy ; Nuclear Magnetic Resonance, Biomolecular ; Protein Conformation ; Proteins/metabolism
    Chemical Substances Carrier Proteins ; Lanthanoid Series Elements ; Proteins
    Language English
    Publishing date 2021-03-11
    Publishing country United States
    Document type Journal Article
    ISSN 1557-7988
    ISSN (online) 1557-7988
    DOI 10.1016/bs.mie.2021.01.039
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  6. Article ; Online: Integration of NMR Spectroscopy in an Analytical Workflow to Evaluate the Effects of Oxidative Stress on Abituzumab: Beyond the Fingerprint of mAbs.

    Cerofolini, Linda / Ravera, Enrico / Fischer, Christian / Trovato, Andrea / Sacco, Francesca / Palinsky, Wolf / Angiuoni, Gabriella / Fragai, Marco / Baroni, Fabio

    Analytical chemistry

    2023  Volume 95, Issue 24, Page(s) 9199–9206

    Abstract: The assessment of the higher-order structure (HOS) by NMR is a powerful methodology to characterize the structural features of biologics. Forced oxidative stress studies are used to investigate the stability profile, to develop pharmaceutical ... ...

    Abstract The assessment of the higher-order structure (HOS) by NMR is a powerful methodology to characterize the structural features of biologics. Forced oxidative stress studies are used to investigate the stability profile, to develop pharmaceutical formulations and analytical methods. Here, the effects of forced oxidative stress by H
    MeSH term(s) Hydrogen Peroxide ; Workflow ; Antibodies, Monoclonal/chemistry ; Magnetic Resonance Spectroscopy
    Chemical Substances Abituzumab (724QD330RD) ; Hydrogen Peroxide (BBX060AN9V) ; Antibodies, Monoclonal
    Language English
    Publishing date 2023-06-06
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1508-8
    ISSN 1520-6882 ; 0003-2700
    ISSN (online) 1520-6882
    ISSN 0003-2700
    DOI 10.1021/acs.analchem.3c00317
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 4033: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  7. Article ; Online: Orientation of immobilized antigens on common surfaces by a simple computational model: Exposition of SARS-CoV-2 Spike protein RBD epitopes.

    Cerofolini, Linda / Fragai, Marco / Luchinat, Claudio / Ravera, Enrico

    Biophysical chemistry

    2020  Volume 265, Page(s) 106441

    Abstract: The possibility of immobilizing a protein with antigenic properties on a solid support offers significant possibilities in the development of immunosensors and vaccine formulations. For both applications, the orientation of the antigen should ensure ... ...

    Abstract The possibility of immobilizing a protein with antigenic properties on a solid support offers significant possibilities in the development of immunosensors and vaccine formulations. For both applications, the orientation of the antigen should ensure ready accessibility of the antibodies to the epitope. However, an experimental assessment of the orientational preferences necessarily proceeds through the preparation/isolation of the antigen, the immobilization on different surfaces and one or more biophysical characterization steps. To predict a priori whether favorable orientations can be achieved or not would allow one to select the most promising experimental routes, partly mitigating the time cost towards the final product. In this manuscript, we apply a simple computational model, based on united-residue modelling, to the prediction of the orientation of the receptor binding domain of the SARS-CoV-2 spike protein on surfaces commonly used in lateral-flow devices. These calculations can account for the experimental observation that direct immobilization on gold gives sufficient exposure of the epitope to obtain a response in immunochemical assays.
    MeSH term(s) Antigens/chemistry ; Antigens/immunology ; Antigens/metabolism ; Betacoronavirus/metabolism ; Epitopes/chemistry ; Epitopes/immunology ; Models, Molecular ; Molecular Docking Simulation ; Protein Domains ; SARS-CoV-2 ; Silicon Dioxide/chemistry ; Spike Glycoprotein, Coronavirus/chemistry ; Spike Glycoprotein, Coronavirus/immunology ; Spike Glycoprotein, Coronavirus/metabolism ; Surface Properties
    Chemical Substances Antigens ; Epitopes ; Spike Glycoprotein, Coronavirus ; spike protein, SARS-CoV-2 ; Silicon Dioxide (7631-86-9)
    Keywords covid19
    Language English
    Publishing date 2020-07-29
    Publishing country Netherlands
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 185052-0
    ISSN 1873-4200 ; 0301-4622
    ISSN (online) 1873-4200
    ISSN 0301-4622
    DOI 10.1016/j.bpc.2020.106441
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 1147: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  8. Article ; Online: Automated Determination of Nuclear Magnetic Resonance Chemical Shift Perturbations in Ligand Screening Experiments: The PICASSO Web Server.

    Laveglia, Vincenzo / Giachetti, Andrea / Cerofolini, Linda / Haubrich, Kevin / Fragai, Marco / Ciulli, Alessio / Rosato, Antonio

    Journal of chemical information and modeling

    2021  Volume 61, Issue 12, Page(s) 5726–5733

    Abstract: Nuclear magnetic resonance (NMR) is an effective, commonly used experimental approach to screen small organic molecules against a protein target. A very popular method consists of monitoring the changes of the NMR chemical shifts of the protein nuclei ... ...

    Abstract Nuclear magnetic resonance (NMR) is an effective, commonly used experimental approach to screen small organic molecules against a protein target. A very popular method consists of monitoring the changes of the NMR chemical shifts of the protein nuclei upon addition of the small molecule to the free protein. Multidimensional NMR experiments allow the interacting residues to be mapped along the protein sequence. A significant amount of human effort goes into manually tracking the chemical shift variations, especially when many signals exhibit chemical shift changes and when many ligands are tested. Some computational approaches to automate the procedure are available, but none of them as a web server. Furthermore, some methods require the adoption of a fairly specific experimental setup, such as recording a series of spectra at increasing small molecule:protein ratios. In this work, we developed a tool requesting a minimal amount of experimental data from the user, implemented it as an open-source program, and made it available as a web application. Our tool compares two spectra, one of the free protein and one of the small molecule:protein mixture, based on the corresponding peak lists. The performance of the tool in terms of correct identification of the protein-binding regions has been evaluated on different protein targets, using experimental data from interaction studies already available in the literature. For a total of 16 systems, our tool achieved between 79% and 100% correct assignments, properly identifying the protein regions involved in the interaction.
    MeSH term(s) Algorithms ; Amino Acid Sequence ; Humans ; Ligands ; Magnetic Resonance Spectroscopy/methods ; Nuclear Magnetic Resonance, Biomolecular/methods ; Proteins/chemistry
    Chemical Substances Ligands ; Proteins
    Language English
    Publishing date 2021-11-29
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 190019-5
    ISSN 1549-960X ; 0095-2338
    ISSN (online) 1549-960X
    ISSN 0095-2338
    DOI 10.1021/acs.jcim.1c00871
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 1230: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  9. Article ; Online: Orientation of immobilized antigens on common surfaces by a simple computational model

    Cerofolini, Linda / Fragai, Marco / Luchinat, Claudio / Ravera, Enrico

    Biophysical Chemistry

    Exposition of SARS-CoV-2 Spike protein RBD epitopes

    2020  Volume 265, Page(s) 106441

    Keywords Biophysics ; Organic Chemistry ; Biochemistry ; covid19
    Language English
    Publisher Elsevier BV
    Publishing country us
    Document type Article ; Online
    ZDB-ID 185052-0
    ISSN 1873-4200 ; 0301-4622
    ISSN (online) 1873-4200
    ISSN 0301-4622
    DOI 10.1016/j.bpc.2020.106441
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

    Full text online

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 1147: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  10. Article ; Online: Mechanism and Inhibition of Matrix Metalloproteinases.

    Cerofolini, Linda / Fragai, Marco / Luchinat, Claudio

    Current medicinal chemistry

    2018  Volume 26, Issue 15, Page(s) 2609–2633

    Abstract: Matrix metalloproteinases hydrolyze proteins and glycoproteins forming the extracellular matrix, cytokines and growth factors released in the extracellular space, and membrane-bound receptors on the outer cell membrane. The pathological relevance of MMPs ...

    Abstract Matrix metalloproteinases hydrolyze proteins and glycoproteins forming the extracellular matrix, cytokines and growth factors released in the extracellular space, and membrane-bound receptors on the outer cell membrane. The pathological relevance of MMPs has prompted the structural and functional characterization of these enzymes and the development of synthetic inhibitors as possible drug candidates. Recent studies have provided a better understanding of the substrate preference of the different members of the family, and structural data on the mechanism by which these enzymes hydrolyze the substrates. Here, we report the recent advancements in the understanding of the mechanism of collagenolysis and elastolysis, and we discuss the perspectives of new therapeutic strategies for targeting MMPs.
    MeSH term(s) Amino Acid Sequence ; Animals ; Catalysis ; Collagen/chemistry ; Elastin/chemistry ; HEK293 Cells ; Humans ; Hydrolysis ; Matrix Metalloproteinase Inhibitors/chemistry ; Matrix Metalloproteinase Inhibitors/pharmacology ; Matrix Metalloproteinases/chemistry ; Protein Domains
    Chemical Substances Matrix Metalloproteinase Inhibitors ; Collagen (9007-34-5) ; Elastin (9007-58-3) ; Matrix Metalloproteinases (EC 3.4.24.-)
    Language English
    Publishing date 2018-03-27
    Publishing country United Arab Emirates
    Document type Journal Article ; Review
    ZDB-ID 1319315-6
    ISSN 1875-533X ; 0929-8673
    ISSN (online) 1875-533X
    ISSN 0929-8673
    DOI 10.2174/0929867325666180326163523
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 4432: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

To top