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  1. Article: Cytoreductive surgery with hyperthermic intraperitoneal chemotherapy - perioperative management at Waikato Hospital.

    Davis, Simon J / Byrne, Kelly P

    Anaesthesia and intensive care

    2019  Volume 47, Issue 1, Page(s) 100–101

    MeSH term(s) Combined Modality Therapy ; Cytoreduction Surgical Procedures ; Hospitals ; Humans ; Hyperthermia, Induced ; Peritoneal Neoplasms ; Preoperative Care
    Language English
    Publishing date 2019-02-13
    Publishing country United States
    Document type Journal Article
    ZDB-ID 187524-3
    ISSN 1448-0271 ; 0310-057X
    ISSN (online) 1448-0271
    ISSN 0310-057X
    DOI 10.1177/0310057X18811993
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Combination CD200R/PD-1 blockade in a humanised mouse model.

    Fellermeyer, Martin / Anzilotti, Consuelo / Paluch, Christopher / Cornall, Richard J / Davis, Simon J / Gileadi, Uzi

    Immunotherapy advances

    2023  Volume 3, Issue 1, Page(s) ltad006

    Abstract: There is an increasing number of immune-checkpoint inhibitors being developed and approved for cancer immunotherapy. Most of the new therapies aim to reactivate tumour-infiltrating T cells, which are responsible for tumour killing. However, in many ... ...

    Abstract There is an increasing number of immune-checkpoint inhibitors being developed and approved for cancer immunotherapy. Most of the new therapies aim to reactivate tumour-infiltrating T cells, which are responsible for tumour killing. However, in many tumours, the most abundant infiltrating immune cells are macrophages and myeloid cells, which can be tumour-promoting as well as tumouricidal. CD200R was initially identified as a myeloid-restricted, inhibitory immune receptor, but was subsequently also found to be expressed within the lymphoid lineage. Using a mouse model humanised for CD200R and PD-1, we investigated the potential of a combination therapy comprising nivolumab, a clinically approved PD-1 blocking antibody, and OX108, a CD200R antagonist. We produced nivolumab as a murine IgG1 antibody and validated its binding activity
    Language English
    Publishing date 2023-03-30
    Publishing country England
    Document type Journal Article
    ISSN 2732-4303
    ISSN (online) 2732-4303
    DOI 10.1093/immadv/ltad006
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: The current state and future of T-cell exhaustion research.

    Jenkins, Edward / Whitehead, Toby / Fellermeyer, Martin / Davis, Simon J / Sharma, Sumana

    Oxford open immunology

    2023  Volume 4, Issue 1, Page(s) iqad006

    Abstract: Exhaustion' is a term used to describe a state of native and redirected T-cell hypo-responsiveness resulting from persistent antigen exposure during chronic viral infections or cancer. Although a well-established phenotype across mice and humans, ... ...

    Abstract 'Exhaustion' is a term used to describe a state of native and redirected T-cell hypo-responsiveness resulting from persistent antigen exposure during chronic viral infections or cancer. Although a well-established phenotype across mice and humans, exhaustion at the molecular level remains poorly defined and inconsistent across the literature. This is, in part, due to an overreliance on surface receptors to define these cells and explain exhaustive behaviours, an incomplete understanding of how exhaustion arises, and a lack of clarity over whether exhaustion is the same across contexts, e.g. chronic viral infections versus cancer. With the development of systems-based genetic approaches such as single-cell RNA-seq and CRISPR screens applied to
    Language English
    Publishing date 2023-07-08
    Publishing country England
    Document type Journal Article ; Review
    ISSN 2633-6960
    ISSN (online) 2633-6960
    DOI 10.1093/oxfimm/iqad006
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: LAG-3: a very singular immune checkpoint.

    Lui, Yuan / Davis, Simon J

    Nature immunology

    2018  Volume 19, Issue 12, Page(s) 1278–1279

    MeSH term(s) Antigens, CD ; CD4-Positive T-Lymphocytes ; Programmed Cell Death 1 Receptor
    Chemical Substances Antigens, CD ; Programmed Cell Death 1 Receptor
    Language English
    Publishing date 2018-11-16
    Publishing country United States
    Document type Journal Article ; Comment
    ZDB-ID 2016987-5
    ISSN 1529-2916 ; 1529-2908
    ISSN (online) 1529-2916
    ISSN 1529-2908
    DOI 10.1038/s41590-018-0257-1
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: T-Cell Receptor Ligands: Every which Way They Can.

    Davis, Simon J / O'Brien-Ball, Caitlin

    Biophysical journal

    2020  Volume 118, Issue 12, Page(s) 2867–2869

    MeSH term(s) Ligands ; Receptors, Antigen, T-Cell ; T-Lymphocytes
    Chemical Substances Ligands ; Receptors, Antigen, T-Cell
    Language English
    Publishing date 2020-05-20
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Comment
    ZDB-ID 218078-9
    ISSN 1542-0086 ; 0006-3495
    ISSN (online) 1542-0086
    ISSN 0006-3495
    DOI 10.1016/j.bpj.2020.05.007
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: Macrophages: micromanagers of antagonistic signaling nanoclusters.

    Eggeling, Christian / Davis, Simon J

    The Journal of cell biology

    2017  Volume 216, Issue 4, Page(s) 871–873

    Abstract: How cells integrate antagonistic receptor signaling events is enigmatic. Using superresolution optical microscopy, Lopes et al. (2017. ...

    Abstract How cells integrate antagonistic receptor signaling events is enigmatic. Using superresolution optical microscopy, Lopes et al. (2017.
    MeSH term(s) Humans ; Ligands ; Macrophages/physiology ; Receptors, Cell Surface/metabolism ; Signal Transduction/physiology
    Chemical Substances Ligands ; Receptors, Cell Surface
    Language English
    Publishing date 2017-03-22
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 218154-x
    ISSN 1540-8140 ; 0021-9525
    ISSN (online) 1540-8140
    ISSN 0021-9525
    DOI 10.1083/jcb.201702028
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article ; Online: Measuring GPCR Stoichiometry Using Types-1, -2, and -3 Bioluminescence Resonance Energy Transfer-Based Assays.

    Felce, James H / James, John R / Davis, Simon J

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

    2019  Volume 1947, Page(s) 183–197

    Abstract: How G protein-coupled receptors are assembled is a matter of considerable interest owing in large part to their remarkable pharmacological importance. For determining receptor stoichiometry, resonance energy transfer-based methods offer considerable ... ...

    Abstract How G protein-coupled receptors are assembled is a matter of considerable interest owing in large part to their remarkable pharmacological importance. For determining receptor stoichiometry, resonance energy transfer-based methods offer considerable advantages insofar as they provide the necessary spatial resolution, and because measurements can be made in situ, relatively easily. This chapter describes three complementary stoichiometric assays that rely on measurements of bioluminescence resonance energy transfer. These quantitative approaches make it possible to identify true protein-protein interactions from non-specific associations that inevitably result from constraining proteins in cellular membranes. In our experience, concordant data obtained in two or more of these assays, benchmarked with suitable controls, strongly predict receptor stoichiometry.
    MeSH term(s) Bioluminescence Resonance Energy Transfer Techniques/methods ; Cell Membrane/metabolism ; Fluorescence ; HEK293 Cells ; Humans ; Ligands ; Luciferases, Renilla/metabolism ; Protein Binding ; Protein Conformation ; Receptors, G-Protein-Coupled/chemistry ; Receptors, G-Protein-Coupled/metabolism
    Chemical Substances Ligands ; Receptors, G-Protein-Coupled ; Luciferases, Renilla (EC 1.13.12.5)
    Language English
    Publishing date 2019-04-04
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 1940-6029
    ISSN (online) 1940-6029
    DOI 10.1007/978-1-4939-9121-1_10
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article ; Online: Phagocytes Get Close to Their Enemies.

    Dustin, Michael L / Davis, Simon J

    Developmental cell

    2016  Volume 36, Issue 2, Page(s) 131–132

    Abstract: Phagocytosis is key for many organismal functions. In a recent issue of Cell, Freeman et al. (2016) demonstrate a feed-forward signaling mechanism wherein F-actin and integrin receptors drive contact formation between phagocytes and antibody-coated solid ...

    Abstract Phagocytosis is key for many organismal functions. In a recent issue of Cell, Freeman et al. (2016) demonstrate a feed-forward signaling mechanism wherein F-actin and integrin receptors drive contact formation between phagocytes and antibody-coated solid particles, signaling their engulfment. This mechanism translates nanoscale proximity effects into wider self-propagating signals.
    MeSH term(s) Actin Cytoskeleton/metabolism ; Actins/metabolism ; Animals ; Humans ; Integrins/metabolism ; Phagocytes/cytology ; Phagocytosis/physiology ; Signal Transduction/immunology
    Chemical Substances Actins ; Integrins
    Language English
    Publishing date 2016-01-25
    Publishing country United States
    Document type Journal Article ; Review
    ZDB-ID 2054967-2
    ISSN 1878-1551 ; 1534-5807
    ISSN (online) 1878-1551
    ISSN 1534-5807
    DOI 10.1016/j.devcel.2016.01.004
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article ; Online: Single-cell measurements of two-dimensional binding affinity across cell contacts.

    Chouliara, Manto / Junghans, Victoria / Dam, Tommy / Santos, Ana Mafalda / Davis, Simon J / Jönsson, Peter

    Biophysical journal

    2021  Volume 120, Issue 22, Page(s) 5032–5040

    Abstract: The two-dimensional (2D) affinity between protein molecules across contacting cells is a key parameter regulating and initiating several cellular processes. However, measuring 2D affinity can be challenging, and experimental data are limited. In addition, ...

    Abstract The two-dimensional (2D) affinity between protein molecules across contacting cells is a key parameter regulating and initiating several cellular processes. However, measuring 2D affinity can be challenging, and experimental data are limited. In addition, the obtained 2D affinities are typically averaged over the cell population. We here present a method to measure 2D affinity on single cells binding to polyhistidine-tagged fluorescent ligands anchored to a supported lipid bilayer (SLB). By decreasing the density of ligands in the SLB using imidazole, a new steady-state accumulation in the contact is obtained, and from this change, both the 2D affinity and the number of receptors on the cell can be determined. The method was validated on an SLB containing rat CD2 binding to the rat CD48 mutant T92A expressed on Jurkat T cells. The addition of imidazole did not influence the average 2D affinity (1/K
    MeSH term(s) Animals ; CD2 Antigens/metabolism ; Cell Communication ; Humans ; Jurkat Cells ; Ligands ; Lipid Bilayers ; Protein Binding ; Rats
    Chemical Substances CD2 Antigens ; Ligands ; Lipid Bilayers
    Language English
    Publishing date 2021-10-13
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 218078-9
    ISSN 1542-0086 ; 0006-3495
    ISSN (online) 1542-0086
    ISSN 0006-3495
    DOI 10.1016/j.bpj.2021.10.010
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article ; Online: Constraints on GPCR Heterodimerization Revealed by the Type-4 Induced-Association BRET Assay.

    Felce, James H / MacRae, Alasdair / Davis, Simon J

    Biophysical journal

    2018  Volume 116, Issue 1, Page(s) 31–41

    Abstract: G-protein-coupled receptors (GPCRs) comprise the largest and most pharmacologically important family of cell-surface receptors encoded by the human genome. In many instances, the distinct signaling behavior of certain GPCRs has been explained in terms of ...

    Abstract G-protein-coupled receptors (GPCRs) comprise the largest and most pharmacologically important family of cell-surface receptors encoded by the human genome. In many instances, the distinct signaling behavior of certain GPCRs has been explained in terms of the formation of heteromers with, for example, distinct signaling properties and allosteric cross-regulation. Confirmation of this has, however, been limited by the paucity of reliable methods for probing heteromeric GPCR interactions in situ. The most widely used assays for GPCR stoichiometry, based on resonance energy transfer, are unsuited to reporting heteromeric interactions. Here, we describe a targeted bioluminescence resonance energy transfer (BRET) assay, called type-4 BRET, which detects both homo- and heteromeric interactions using induced multimerization of protomers within such complexes, at constant expression. Using type-4 BRET assays, we investigate heterodimerization among known GPCR homodimers: the CXC chemokine receptor 4 and sphingosine-1-phosphate receptors. We observe that CXC chemokine receptor 4 and sphingosine-1-phosphate receptors can form heterodimers with GPCRs from their immediate subfamilies but not with more distantly related receptors. We also show that heterodimerization appears to disrupt homodimeric interactions, suggesting the sharing of interfaces. Broadly, these observations indicate that heterodimerization results from the divergence of homodimeric receptors and will therefore likely be restricted to closely related homodimeric GPCRs.
    MeSH term(s) Fluorescence Resonance Energy Transfer ; HEK293 Cells ; Humans ; Protein Multimerization ; Receptors, CXCR4/chemistry ; Sphingosine-1-Phosphate Receptors/chemistry ; Sphingosine-1-Phosphate Receptors/metabolism
    Chemical Substances CXCR4 protein, human ; Receptors, CXCR4 ; Sphingosine-1-Phosphate Receptors
    Language English
    Publishing date 2018-11-22
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 218078-9
    ISSN 1542-0086 ; 0006-3495
    ISSN (online) 1542-0086
    ISSN 0006-3495
    DOI 10.1016/j.bpj.2018.09.034
    Database MEDical Literature Analysis and Retrieval System OnLINE

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