LIVIVO - The Search Portal for Life Sciences

zur deutschen Oberfläche wechseln
Advanced search

Search results

Result 1 - 10 of total 59

Search options

  1. Book ; Thesis: Immunoglobulins and their fragments on solid surfaces

    Buijs, Jos A. G.

    1995  

    Author's details J. A. G. Buijs
    Keywords Immunglobuline ; Adsorption ; Festkörperoberfläche
    Subject Festkörper ; Adsorbieren ; Gamma-Globuline ; Ig ; Immunoglobuline ; Immunglobulin vom Menschen ; Beriglotin
    Size 126 S. : graph. Darst.
    Publishing country Netherlands
    Document type Book ; Thesis
    Thesis / German Habilitation thesis Wageningen, Landbouwuniv., Diss., 1995
    Note Zsfassung in niederländ. Sprache
    Remark AY 17384 ; Abt. Nussallee/Bereichsbibl. ZBMed: AY 17384
    HBZ-ID HT006779622
    ISBN 90-5651-015-0 ; 978-90-5651-015-2
    Database Catalogue ZB MED Nutrition, Environment, Agriculture

    More links

    Kategorien

  2. Article ; Online: Repurposing the mammalian RNA-binding protein Musashi-1 as an allosteric translation repressor in bacteria.

    Dolcemascolo, Roswitha / Heras-Hernández, María / Goiriz, Lucas / Montagud-Martínez, Roser / Requena-Menéndez, Alejandro / Ruiz, Raúl / Pérez-Ràfols, Anna / Higuera-Rodríguez, R Anahí / Pérez-Ropero, Guillermo / Vranken, Wim F / Martelli, Tommaso / Kaiser, Wolfgang / Buijs, Jos / Rodrigo, Guillermo

    eLife

    2024  Volume 12

    Abstract: The RNA recognition motif (RRM) is the most common RNA-binding protein domain identified in nature. However, RRM-containing proteins are only prevalent in eukaryotic phyla, in which they play central regulatory roles. Here, we engineered an orthogonal ... ...

    Abstract The RNA recognition motif (RRM) is the most common RNA-binding protein domain identified in nature. However, RRM-containing proteins are only prevalent in eukaryotic phyla, in which they play central regulatory roles. Here, we engineered an orthogonal post-transcriptional control system of gene expression in the bacterium
    MeSH term(s) Animals ; Nerve Tissue Proteins/metabolism ; RNA-Binding Proteins/metabolism ; RNA/metabolism ; RNA, Messenger/metabolism ; Escherichia coli/genetics ; Escherichia coli/metabolism ; Mammals/genetics
    Chemical Substances Nerve Tissue Proteins ; RNA-Binding Proteins ; RNA (63231-63-0) ; RNA, Messenger
    Language English
    Publishing date 2024-02-16
    Publishing country England
    Document type Journal Article
    ZDB-ID 2687154-3
    ISSN 2050-084X ; 2050-084X
    ISSN (online) 2050-084X
    ISSN 2050-084X
    DOI 10.7554/eLife.91777
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

  3. Article ; Online: Bivalent binding on cells varies between anti-CD20 antibodies and is dose-dependent.

    Bondza, Sina / Ten Broeke, Toine / Nestor, Marika / Leusen, Jeanette H W / Buijs, Jos

    mAbs

    2020  Volume 12, Issue 1, Page(s) 1792673

    Abstract: Based on their mechanism of action, two types of anti-CD20 antibodies are distinguished: Type I, which efficiently mediate complement-dependent cytotoxicity, and Type II, which instead are more efficient in inducing direct cell death. Several molecular ... ...

    Abstract Based on their mechanism of action, two types of anti-CD20 antibodies are distinguished: Type I, which efficiently mediate complement-dependent cytotoxicity, and Type II, which instead are more efficient in inducing direct cell death. Several molecular characteristics of these antibodies have been suggested to underlie these different biological functions, one of these being the manner of binding to CD20 expressed on malignant B cells. However, the exact binding model on cells is unclear. In this study, the binding mechanism of the Type I therapeutic antibodies rituximab (RTX) and ofatumumab (OFA) and the Type II antibody obinutuzumab (OBI) were established by real-time interaction analysis on live cells. It was found that the degree of bivalent stabilization differed for the antibodies: OFA was stabilized the most, followed by RTX and then OBI, which had the least amount of bivalent stabilization. Bivalency inversely correlated with binding dynamics for the antibodies, with OBI displaying the most dynamic binding pattern, followed by RTX and OFA. For RTX and OBI, bivalency and binding dynamics were concentration dependent; at higher concentrations the interactions were more dynamic, whereas the percentage of antibodies that bound bivalent was less, resulting in concentration-dependent apparent affinities. This was barely noticeable for OFA, as almost all molecules bound bivalently at the tested concentrations. We conclude that the degree of bivalent binding positively correlates with the complement recruiting capacity of the investigated CD20 antibodies.
    MeSH term(s) Antibodies, Monoclonal, Humanized/immunology ; Antibodies, Monoclonal, Humanized/pharmacology ; B-Lymphocytes/immunology ; B-Lymphocytes/pathology ; Dose-Response Relationship, Drug ; Dose-Response Relationship, Immunologic ; Hematologic Neoplasms/drug therapy ; Hematologic Neoplasms/immunology ; Hematologic Neoplasms/pathology ; Humans ; K562 Cells ; Rituximab/immunology ; Rituximab/pharmacology
    Chemical Substances Antibodies, Monoclonal, Humanized ; Rituximab (4F4X42SYQ6) ; ofatumumab (M95KG522R0) ; obinutuzumab (O43472U9X8)
    Language English
    Publishing date 2020-07-31
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Video-Audio Media
    ZDB-ID 2537838-7
    ISSN 1942-0870 ; 1942-0870
    ISSN (online) 1942-0870
    ISSN 1942-0870
    DOI 10.1080/19420862.2020.1792673
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

  4. Article ; Online: Complement-Dependent Activity of CD20-Specific IgG Correlates With Bivalent Antigen Binding and C1q Binding Strength.

    Bondza, Sina / Marosan, Anita / Kara, Sibel / Lösing, Josephine / Peipp, Matthias / Nimmerjahn, Falk / Buijs, Jos / Lux, Anja

    Frontiers in immunology

    2021  Volume 11, Page(s) 609941

    Abstract: Monoclonal antibodies directed against the CD20 surface antigen on B cells are widely used in the therapy of B cell malignancies. Upon administration, the antibodies bind to CD20 expressing B cells and induce their ... ...

    Abstract Monoclonal antibodies directed against the CD20 surface antigen on B cells are widely used in the therapy of B cell malignancies. Upon administration, the antibodies bind to CD20 expressing B cells and induce their depletion
    MeSH term(s) Antibodies, Monoclonal, Humanized/metabolism ; Antibodies, Monoclonal, Humanized/pharmacology ; Antibody Affinity ; Antibody Specificity ; Antigens, CD20/immunology ; Antigens, CD20/metabolism ; Antineoplastic Agents, Immunological/metabolism ; Antineoplastic Agents, Immunological/pharmacology ; B-Lymphocytes/drug effects ; B-Lymphocytes/immunology ; B-Lymphocytes/metabolism ; B-Lymphocytes/pathology ; Binding Sites, Antibody ; Complement Activation/drug effects ; Complement C1q/metabolism ; Complement C3b/metabolism ; Cytotoxicity, Immunologic/drug effects ; Humans ; K562 Cells ; Kinetics ; Lymphoma, B-Cell/drug therapy ; Lymphoma, B-Cell/immunology ; Lymphoma, B-Cell/metabolism ; Lymphoma, B-Cell/pathology ; Phagocytosis/drug effects ; Protein Binding ; Rituximab/metabolism ; Rituximab/pharmacology
    Chemical Substances Antibodies, Monoclonal, Humanized ; Antigens, CD20 ; Antineoplastic Agents, Immunological ; Rituximab (4F4X42SYQ6) ; Complement C1q (80295-33-6) ; Complement C3b (80295-43-8) ; ofatumumab (M95KG522R0) ; obinutuzumab (O43472U9X8)
    Language English
    Publishing date 2021-01-11
    Publishing country Switzerland
    Document type Comparative Study ; Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2606827-8
    ISSN 1664-3224 ; 1664-3224
    ISSN (online) 1664-3224
    ISSN 1664-3224
    DOI 10.3389/fimmu.2020.609941
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

  5. Article ; Online: Carbon Flux as a Measure of Prostate Cancer Aggressiveness: [

    Regula, Naresh / Honarvar, Hadis / Lubberink, Mark / Jorulf, Håkan / Ladjevardi, Sam / Häggman, Michael / Antoni, Gunnar / Buijs, Jos / Velikyan, Irina / Sörensen, Jens

    International journal of medical sciences

    2020  Volume 17, Issue 2, Page(s) 214–223

    Abstract: ... ...

    Abstract Purpose
    MeSH term(s) Acetates/chemistry ; Aged ; Carbon Cycle/physiology ; Humans ; Kinetics ; Male ; Middle Aged ; Positron Emission Tomography Computed Tomography/methods ; Prostatic Neoplasms/diagnostic imaging ; Prostatic Neoplasms/physiopathology
    Chemical Substances Acetates
    Language English
    Publishing date 2020-01-14
    Publishing country Australia
    Document type Journal Article
    ZDB-ID 2151424-0
    ISSN 1449-1907 ; 1449-1907
    ISSN (online) 1449-1907
    ISSN 1449-1907
    DOI 10.7150/ijms.39542
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

  6. Article ; Online: Deferring diagnostic evaluation for suspected deep venous thrombosis using a single dose of anticoagulant: Real-world data from a regionwide care pathway.

    Luu, Inge H Y / Mostard, Guy J M / van Mil, Dominique / van Berlo, Marlon H W / Lobbes, Marc B I / Külcü, Kemal / Cate, Hugo Ten / Peeters, Jos / Palmen, Jan / Buijs, Jacqueline / Jie, Kon-Siong G / van Kampen, Roel J W / van Twist, Daan J L

    European journal of internal medicine

    2023  Volume 122, Page(s) 54–60

    Abstract: Background: Patients with suspected deep venous thrombosis (DVT) are typically referred to the emergency department (ED) for immediate evaluation. However, this often contributes to ED overcrowding and necessitates round-the-clock sonographic ... ...

    Abstract Background: Patients with suspected deep venous thrombosis (DVT) are typically referred to the emergency department (ED) for immediate evaluation. However, this often contributes to ED overcrowding and necessitates round-the-clock sonographic examinations. Therefore, we implemented a regionwide care pathway for deferring diagnostic workup of suspected DVT until the following day. Patients receive a single anticoagulant dose from their general practitioner (GP) to prevent progression of DVT in the interval between referral and diagnostic evaluation. The next day, patients undergo comprehensive evaluation at our outpatient DVT clinic, including venous ultrasound. This retrospective study aims to provide real-world data on the safety of this care pathway regarding the occurrence of bleeding complications and pulmonary embolism (PE).
    Methods: We included all GP-referred patients with suspected DVT in 2018 and 2019. Patients with absolute contraindications to deferred evaluation or anticoagulation were excluded. The primary endpoint was the occurrence of bleeding complications. Secondary endpoints included PE events and all-cause mortality within seven days following DVT evaluation.
    Results: Among 1,024 included patients, DVT was confirmed in 238 patients (23.2%) and superficial thrombophlebitis in 98 patients (9.6%). No bleeding events were recorded in patients in whom DVT was ruled out. PE was confirmed in eight patients on the same day as DVT evaluation (0.8%, 95%CI 0.4-1.6) and in six patients within seven days following DVT evaluation (0.6%, 0.2-1.3%). No deaths occurred during this timeframe.
    Conclusion: This real-world study observed a very low incidence of bleeding complications and PE events, indicating that this care pathway of deferred DVT workup is safe and may offer a more streamlined diagnostic approach for patients with suspected DVT.
    MeSH term(s) Humans ; Anticoagulants/adverse effects ; Venous Thrombosis/diagnostic imaging ; Venous Thrombosis/drug therapy ; Retrospective Studies ; Critical Pathways ; Pulmonary Embolism/complications
    Chemical Substances Anticoagulants
    Language English
    Publishing date 2023-12-26
    Publishing country Netherlands
    Document type Journal Article
    ZDB-ID 1038679-8
    ISSN 1879-0828 ; 0953-6205
    ISSN (online) 1879-0828
    ISSN 0953-6205
    DOI 10.1016/j.ejim.2023.12.021
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

  7. Article ; Online: The CoLab-score rapidly and efficiently excludes COVID-19 at the emergency department without need for SARS-CoV-2 testing: a multicenter case-control study

    Boer, Arjen-Kars / Deneer, Ruben / Maas, Maaike / Ammerlaan, Heidi S. M. / van Balkom, Roland H. H. / Leers, Mathie P. G. / Martens, Remy J.H. / Buijs, Madelon M. / Kerremans, Jos J. / Messchaert, Muriël / van Suijlen, Jeroen D.E. / van Riel, Natal A.W. / Scharnhorst, Volkher

    medRxiv

    Abstract: Background ... Rapid identification of emergency department (ED) patients with a possible COVID-19 infection is needed. PCR-testing all ED patients is neither feasible nor effective in most centers, therefore a rapid, objective, low-cost screening tool ... ...

    Abstract Background
    Rapid identification of emergency department (ED) patients with a possible COVID-19 infection is needed. PCR-testing all ED patients is neither feasible nor effective in most centers, therefore a rapid, objective, low-cost screening tool to triage ED patients is necessary.
    Methods
    Results from all routine lab tests from ED patients at the Catharina Hospital were collected from July 2019 to July 2020 and used in a statistical model to obtain the CoLab-score. The score was validated temporally and externally in three independent centers.
    Results
    The CoLab-score consists of 10 routine lab results and can be used to safely rule-out a COVID-19 infection in more than one third of ED presentations with a negative predictive value of 0.997 (95% CI: 0.994 – 0.999) .
    Conclusions
    The CoLab-score is a valuable tool to rule out COVID-19, guide PCR testing and is available to any center with access to routine laboratory tests.
    Keywords covid19
    Language English
    Publishing date 2024-01-31
    Publisher Cold Spring Harbor Laboratory Press
    Document type Article ; Online
    DOI 10.1101/2024.01.30.24301996
    Database COVID19

    Kategorien

  8. Article ; Online: Novel Real-Time Proximity Assay for Characterizing Multiple Receptor Interactions on Living Cells.

    Bondza, Sina / Björkelund, Hanna / Nestor, Marika / Andersson, Karl / Buijs, Jos

    Analytical chemistry

    2017  Volume 89, Issue 24, Page(s) 13212–13218

    Abstract: Cellular receptor activity is often controlled through complex mechanisms involving interactions with multiple molecules, which can be soluble ligands and/or other cell surface molecules. In this study, we combine a fluorescence-based technology for real- ...

    Abstract Cellular receptor activity is often controlled through complex mechanisms involving interactions with multiple molecules, which can be soluble ligands and/or other cell surface molecules. In this study, we combine a fluorescence-based technology for real-time interaction analysis with fluorescence quenching to create a novel time-resolved proximity assay to study protein-receptor interactions on living cells. This assay extracts the binding kinetics and affinity for two proteins if they bind in proximity on the cell surface. One application of real-time proximity interaction analysis is to study relative levels of receptor dimerization. The method was primarily evaluated using the HER2 binding antibodies Trastuzumab and Pertuzumab and two EGFR binding antibodies including Cetuximab. Using Cetuximab and Trastuzumab, proximity of EGFR and HER2 was investigated before and after treatment of cells with the tyrosine-kinase inhibitor Gefitinib. Treated cells displayed 50% increased proximity signal, whereas the binding characteristics of the two antibodies were not significantly affected, implying an increase in the EGFR-HER2 dimer level. These results demonstrate that real-time proximity interaction analysis enables determination of the interaction rate constants and affinity of two ligands while simultaneously quantifying their relative colocalization on living cells.
    MeSH term(s) Antibodies, Monoclonal, Humanized/chemistry ; Antibodies, Monoclonal, Humanized/pharmacology ; Cell Survival ; Cetuximab/chemistry ; Cetuximab/pharmacology ; ErbB Receptors/analysis ; ErbB Receptors/antagonists & inhibitors ; ErbB Receptors/chemistry ; Gefitinib/chemistry ; Gefitinib/pharmacology ; Humans ; Ligands ; Protein Binding/drug effects ; Protein Kinase Inhibitors/chemistry ; Protein Kinase Inhibitors/pharmacology ; Receptor, ErbB-2/analysis ; Receptor, ErbB-2/antagonists & inhibitors ; Receptor, ErbB-2/chemistry ; Time Factors ; Trastuzumab/chemistry ; Trastuzumab/pharmacology ; Tumor Cells, Cultured
    Chemical Substances Antibodies, Monoclonal, Humanized ; Ligands ; Protein Kinase Inhibitors ; EGFR protein, human (EC 2.7.10.1) ; ERBB2 protein, human (EC 2.7.10.1) ; ErbB Receptors (EC 2.7.10.1) ; Receptor, ErbB-2 (EC 2.7.10.1) ; pertuzumab (K16AIQ8CTM) ; Trastuzumab (P188ANX8CK) ; Cetuximab (PQX0D8J21J) ; Gefitinib (S65743JHBS)
    Language English
    Publishing date 2017-12-05
    Publishing country United States
    Document type Journal Article
    ZDB-ID 1508-8
    ISSN 1520-6882 ; 0003-2700
    ISSN (online) 1520-6882
    ISSN 0003-2700
    DOI 10.1021/acs.analchem.7b02983
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

  9. Article ; Online: Pilot-scale process for magnetic bead purification of antibodies directly from non-clarified CHO cell culture.

    Brechmann, Nils A / Eriksson, Per-Olov / Eriksson, Kristofer / Oscarsson, Sven / Buijs, Jos / Shokri, Atefeh / Hjälm, Göran / Chotteau, Véronique

    Biotechnology progress

    2019  Volume 35, Issue 3, Page(s) e2775

    Abstract: High capacity magnetic protein A agarose beads, LOABeads PrtA, were used in the development of a new process for affinity purification of monoclonal antibodies (mAbs) from non-clarified CHO cell broth using a pilot-scale magnetic separator. The LOABeads ... ...

    Abstract High capacity magnetic protein A agarose beads, LOABeads PrtA, were used in the development of a new process for affinity purification of monoclonal antibodies (mAbs) from non-clarified CHO cell broth using a pilot-scale magnetic separator. The LOABeads had a maximum binding capacity of 65 mg/mL and an adsorption capacity of 25-42 mg IgG/mL bead in suspension for an IgG concentration of 1 to 8 g/L. Pilot-scale separation was initially tested in a mAb capture step from 26 L clarified harvest. Small-scale experiments showed that similar mAb adsorptions were obtained in cell broth containing 40 × 10
    MeSH term(s) Adsorption ; Animals ; Antibodies, Monoclonal/chemistry ; Antibodies, Monoclonal/metabolism ; CHO Cells/metabolism ; Chromatography, Affinity/instrumentation ; Chromatography, Affinity/methods ; Cricetulus ; Hydrogen-Ion Concentration ; Magnetics/instrumentation ; Magnetics/methods ; Staphylococcal Protein A/chemistry
    Chemical Substances Antibodies, Monoclonal ; Staphylococcal Protein A
    Language English
    Publishing date 2019-01-30
    Publishing country United States
    Document type Evaluation Study ; Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 165657-0
    ISSN 1520-6033 ; 8756-7938
    ISSN (online) 1520-6033
    ISSN 8756-7938
    DOI 10.1002/btpr.2775
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

  10. Article ; Online: Human Growth Hormone Adsorption Kinetics and Conformation on Self-Assembled Monolayers.

    Buijs, Jos / Britt, David W / Hlady, Vladimir

    Langmuir : the ACS journal of surfaces and colloids

    2014  Volume 14, Issue 2, Page(s) 335–341

    Abstract: The adsorption process of the recombinant human growth hormone on organic films, created by self-assembly of octadecyltrichlorosilane, arachidic acid, and dipalmitoylphosphatidylcholine, is investigated and compared to adsorption on silica and methylated ...

    Abstract The adsorption process of the recombinant human growth hormone on organic films, created by self-assembly of octadecyltrichlorosilane, arachidic acid, and dipalmitoylphosphatidylcholine, is investigated and compared to adsorption on silica and methylated silica substrates. Information on the adsorption process of human growth hormone (hGH) is obtained by using total internal reflection fluorescence (TIRF). The intensity, spectra, and quenching of the intrinsic fluorescence emitted by the growth hormone's single tryptophan are monitored and related to adsorption kinetics and protein conformation. For the various alkylated hydrophobic surfaces with differences in surface density and conformational freedom it is observed that the adsorbed amount of growth hormone is relatively large if the alkyl chains are in an ordered structure while the amounts adsorbed are considerably lower for adsorption onto less ordered alkyl chains of fatty acid and phospholipid layers. Adsorption on methylated surfaces results in a relatively large conformational change in the growth hormone's structure, as displayed by a 7 nm blue shift in emission wavelength and a large increase in the effectiveness of fluorescence quenching. Conformational changes are less evident for hGH adsorption onto the fatty acid and phospholipid alkyl chains. Adsorption kinetics on the hydrophilic head groups of the self-assembled monolayers are similar to those on solid hydrophilic surfaces. The relatively small conformational changes in the hGH structure observed for adsorption on silica are even further reduced for adsorption on fatty acid head groups.
    Language English
    Publishing date 2014-08-14
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2005937-1
    ISSN 1520-5827 ; 0743-7463
    ISSN (online) 1520-5827
    ISSN 0743-7463
    DOI 10.1021/la970669s
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

To top