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Article ; Online: Advances in the application of fluorescence correlation spectroscopy to study detergent purified and encapsulated membrane proteins.

Stoddart, Leigh A / Goulding, Joëlle / Briddon, Stephen J

The international journal of biochemistry & cell biology

2022 Volume 146, Page(s) 106210

Abstract: Fluorescence correlation spectroscopy (FCS) is a quantitative spectroscopy technique which could potentially increase throughput and sensitivity of screening for ligand, substrate and inhibitor binding to membrane proteins in solution. However, the ... ...

Abstract	Fluorescence correlation spectroscopy (FCS) is a quantitative spectroscopy technique which could potentially increase throughput and sensitivity of screening for ligand, substrate and inhibitor binding to membrane proteins in solution. However, the purification of membrane proteins in their active forms is complex, as the lipid bilayer provides stability and its removal often causes the protein to become conformationally unstable. This has limited the application of biophysical techniques such as FCS to study the function of membrane proteins. The recent application of native extraction techniques such as styrene maleic acid lipid particles (SMALPs) has resolved this issue and FCS has emerged as a powerful option for studying proteins extracted in this way. This review will discuss the application of FCS to study purified membrane proteins in detergent micelles, nanodiscs and SMALPs and its potential to be used routinely in membrane protein drug discovery.
MeSH term(s)	Detergents ; Fluorescence ; Lipid Bilayers/chemistry ; Membrane Proteins/chemistry ; Polystyrenes/chemistry
Chemical Substances	Detergents ; Lipid Bilayers ; Membrane Proteins ; Polystyrenes
Language	English
Publishing date	2022-04-04
Publishing country	Netherlands
Document type	Journal Article ; Review ; Research Support, Non-U.S. Gov't
ZDB-ID	1228429-4
ISSN	1878-5875 ; 1357-2725
ISSN (online)	1878-5875
ISSN	1357-2725
DOI	10.1016/j.biocel.2022.106210
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Article ; Online: Simple methods for quantifying super-resolved cortical actin.

Garlick, Evelyn / Faulkner, Emma L / Briddon, Stephen J / Thomas, Steven G

Scientific reports

2022 Volume 12, Issue 1, Page(s) 2715

Abstract: Cortical actin plays a key role in cell movement and division, but has also been implicated in the organisation of cell surface receptors such as G protein-coupled receptors. The actin mesh proximal to the inner membrane forms small fenced regions, or ' ... ...

Abstract	Cortical actin plays a key role in cell movement and division, but has also been implicated in the organisation of cell surface receptors such as G protein-coupled receptors. The actin mesh proximal to the inner membrane forms small fenced regions, or 'corrals', in which receptors can be constrained. Quantification of the actin mesh at the nanoscale has largely been attempted in single molecule datasets and electron micrographs. This work describes the development and validation of workflows for analysis of super resolved fixed cortical actin images obtained by Super Resolved Radial Fluctuations (SRRF), Structured Illumination Microscopy (3D-SIM) and Expansion Microscopy (ExM). SRRF analysis was used to show a significant increase in corral area when treating cells with the actin disrupting agent cytochalasin D (increase of 0.31 µm
MeSH term(s)	A549 Cells ; Actin Cytoskeleton/chemistry ; Actin Cytoskeleton/metabolism ; Actins/analysis ; Actins/chemistry ; Actins/drug effects ; Cell Membrane/chemistry ; Cell Membrane/metabolism ; Cytochalasin D/pharmacology ; Humans ; Image Processing, Computer-Assisted/methods ; Microscopy, Fluorescence/methods
Chemical Substances	Actins ; Cytochalasin D (22144-77-0)
Language	English
Publishing date	2022-02-17
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-022-06702-w
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Article ; Online: Fluorescent ligands: Bringing light to emerging GPCR paradigms.

Soave, Mark / Briddon, Stephen J / Hill, Stephen J / Stoddart, Leigh A

British journal of pharmacology

2020 Volume 177, Issue 5, Page(s) 978–991

Abstract: In recent years, several novel aspects of GPCR pharmacology have been described, which are thought to play a role in determining the in vivo efficacy of a compound. Fluorescent ligands have been used to study many of these, which have also required the ... ...

Abstract	In recent years, several novel aspects of GPCR pharmacology have been described, which are thought to play a role in determining the in vivo efficacy of a compound. Fluorescent ligands have been used to study many of these, which have also required the development of new experimental approaches. Fluorescent ligands offer the potential to use the same fluorescent probe to perform a broad range of experiments, from single-molecule microscopy to in vivo BRET. This review provides an overview of the in vitro use of fluorescent ligands in further understanding emerging pharmacological paradigms within the GPCR field, including ligand-binding kinetics, allosterism and intracellular signalling, along with the use of fluorescent ligands to study physiologically relevant therapeutic agents.
MeSH term(s)	Fluorescent Dyes ; Kinetics ; Ligands ; Receptors, G-Protein-Coupled ; Signal Transduction
Chemical Substances	Fluorescent Dyes ; Ligands ; Receptors, G-Protein-Coupled
Language	English
Publishing date	2020-02-06
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	80081-8
ISSN	1476-5381 ; 0007-1188
ISSN (online)	1476-5381
ISSN	0007-1188
DOI	10.1111/bph.14953
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Article: Advances in the application of fluorescence correlation spectroscopy to study detergent purified and encapsulated membrane proteins

Stoddart, Leigh A / Goulding, Joëlle / Briddon, Stephen J

international journal of biochemistry & cell biology. 2022 May, v. 146

2022

Abstract	Fluorescence correlation spectroscopy (FCS) is a quantitative spectroscopy technique which could potentially increase throughput and sensitivity of screening for ligand, substrate and inhibitor binding to membrane proteins in solution. However, the purification of membrane proteins in their active forms is complex, as the lipid bilayer provides stability and its removal often causes the protein to become conformationally unstable. This has limited the application of biophysical techniques such as FCS to study the function of membrane proteins. The recent application of native extraction techniques such as styrene maleic acid lipid particles (SMALPs) has resolved this issue and FCS has emerged as a powerful option for studying proteins extracted in this way. This review will discuss the application of FCS to study purified membrane proteins in detergent micelles, nanodiscs and SMALPs and its potential to be used routinely in membrane protein drug discovery.
Keywords	detergents ; drugs ; encapsulation ; fluorescence correlation spectroscopy ; ligands ; lipid bilayers ; maleic acid ; membrane proteins ; micelles ; styrene
Language	English
Dates of publication	2022-05
Publishing place	Elsevier Ltd
Document type	Article
ZDB-ID	1228429-4
ISSN	1878-5875 ; 1357-2725
ISSN (online)	1878-5875
ISSN	1357-2725
DOI	10.1016/j.biocel.2022.106210
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: Efficient G protein coupling is not required for agonist-mediated internalization and membrane reorganization of the adenosine A

Stoddart, Leigh A / Kilpatrick, Laura E / Corriden, Ross / Kellam, Barrie / Briddon, Stephen J / Hill, Stephen J

FASEB journal : official publication of the Federation of American Societies for Experimental Biology

2021 Volume 35, Issue 4, Page(s) e21211

Abstract: Organization of G protein-coupled receptors at the plasma membrane has been the focus of much recent attention. Advanced microscopy techniques have shown that these receptors can be localized to discrete microdomains and reorganization upon ligand ... ...

Abstract	Organization of G protein-coupled receptors at the plasma membrane has been the focus of much recent attention. Advanced microscopy techniques have shown that these receptors can be localized to discrete microdomains and reorganization upon ligand activation is crucial in orchestrating their signaling. Here, we have compared the membrane organization and downstream signaling of a mutant (R108A, R3.50A) of the adenosine A
MeSH term(s)	Adenosine/analogs & derivatives ; Adenosine/pharmacology ; Adenosine A3 Receptor Agonists/pharmacology ; Animals ; Arrestin/metabolism ; Boron Compounds/pharmacology ; CHO Cells ; Cricetulus ; GTP-Binding Proteins/metabolism ; Gene Expression Regulation/drug effects ; Mutation ; Protein Binding ; Receptor, Adenosine A3/genetics ; Receptor, Adenosine A3/metabolism
Chemical Substances	ABEA-X-BY630 ; Adenosine A3 Receptor Agonists ; Arrestin ; Boron Compounds ; Receptor, Adenosine A3 ; GTP-Binding Proteins (EC 3.6.1.-) ; Adenosine (K72T3FS567)
Language	English
Publishing date	2021-03-12
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	639186-2
ISSN	1530-6860 ; 0892-6638
ISSN (online)	1530-6860
ISSN	0892-6638
DOI	10.1096/fj.202001729RR
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Zs.A 2266: 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)
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Article: Small Molecule Fluorescent Ligands for the Atypical Chemokine Receptor 3 (ACKR3).

Dekkers, Sebastian / Comez, Dehan / Karsai, Noemi / Arimont-Segura, Marta / Canals, Meritxell / Caspar, Birgit / de Graaf, Chris / Kilpatrick, Laura E / Leurs, Rob / Kellam, Barrie / Hill, Stephen J / Briddon, Stephen J / Stocks, Michael J

ACS medicinal chemistry letters

2023 Volume 15, Issue 1, Page(s) 143–148

Abstract: The atypical chemokine receptor 3 (ACKR3) is a receptor that induces cancer progression and metastasis in multiple cell types. Therefore, new chemical tools are required to study the role of ACKR3 in cancer and other diseases. In this study, fluorescent ... ...

Abstract	The atypical chemokine receptor 3 (ACKR3) is a receptor that induces cancer progression and metastasis in multiple cell types. Therefore, new chemical tools are required to study the role of ACKR3 in cancer and other diseases. In this study, fluorescent probes, based on a series of small molecule ACKR3 agonists, were synthesized. Three fluorescent probes, which showed specific binding to ACKR3 through a luminescence-based NanoBRET binding assay (p
Language	English
Publishing date	2023-12-08
Publishing country	United States
Document type	Journal Article
ISSN	1948-5875
ISSN	1948-5875
DOI	10.1021/acsmedchemlett.3c00469
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Article ; Online: Small-Molecule Fluorescent Ligands for the CXCR4 Chemokine Receptor.

Dekkers, Sebastian / Caspar, Birgit / Goulding, Joëlle / Kindon, Nicholas D / Kilpatrick, Laura E / Stoddart, Leigh A / Briddon, Stephen J / Kellam, Barrie / Hill, Stephen J / Stocks, Michael J

Journal of medicinal chemistry

2023 Volume 66, Issue 7, Page(s) 5208–5222

Abstract: The C-X-C chemokine receptor type 4, or CXCR4, is a chemokine receptor found to promote cancer progression and metastasis of various cancer cell types. To investigate the pharmacology of this receptor, and to further elucidate its role in cancer, novel ... ...

Abstract	The C-X-C chemokine receptor type 4, or CXCR4, is a chemokine receptor found to promote cancer progression and metastasis of various cancer cell types. To investigate the pharmacology of this receptor, and to further elucidate its role in cancer, novel chemical tools are a necessity. In the present study, using classic medicinal chemistry approaches, small-molecule-based fluorescent probes were designed and synthesized based on previously reported small-molecule antagonists. Here, we report the development of three distinct chemical classes of fluorescent probes that show specific binding to the CXCR4 receptor in a novel fluorescence-based NanoBRET binding assay (p
MeSH term(s)	Receptors, CXCR4/metabolism ; Ligands ; Fluorescent Dyes/chemistry ; Protein Binding ; Chemokines/metabolism ; Chemokine CXCL12/metabolism
Chemical Substances	Receptors, CXCR4 ; Ligands ; Fluorescent Dyes ; Chemokines ; Chemokine CXCL12
Language	English
Publishing date	2023-03-21
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	218133-2
ISSN	1520-4804 ; 0022-2623
ISSN (online)	1520-4804
ISSN	0022-2623
DOI	10.1021/acs.jmedchem.3c00151
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Zs.B 151: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular ab Jg. 2022: Lesesaal (EG)
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Article ; Online: A time-resolved Förster resonance energy transfer assay to investigate drug and inhibitor binding to ABCG2.

Mitchell-White, James I / Briggs, Deborah A / Mistry, Sarah J / Mbiwan, Hannah A / Kellam, Barrie / Holliday, Nicholas D / Briddon, Stephen J / Kerr, Ian D

Archives of biochemistry and biophysics

2024 Volume 753, Page(s) 109915

Abstract: The human ATP-binding cassette (ABC) transporter, ABCG2, is responsible for multidrug resistance in some tumours. Detailed knowledge of its activity is crucial for understanding drug transport and resistance in cancer, and has implications for wider ... ...

Abstract	The human ATP-binding cassette (ABC) transporter, ABCG2, is responsible for multidrug resistance in some tumours. Detailed knowledge of its activity is crucial for understanding drug transport and resistance in cancer, and has implications for wider pharmacokinetics. The binding of substrates and inhibitors is a key stage in the transport cycle of ABCG2. Here, we describe a novel binding assay using a high affinity fluorescent inhibitor based on Ko143 and time-resolved Förster resonance energy transfer (TR-FRET) to measure saturation binding to ABCG2. This binding is displaced by Ko143 and other known ABCG2 ligands, and is sensitive to the addition of AMP-PNP, a non-hydrolysable ATP analogue. This assay complements the arsenal of methods for determining drug:ABCG2 interactions and has the possibility of being adaptable for other multidrug pumps.
MeSH term(s)	Humans ; Fluorescence Resonance Energy Transfer ; Drug Resistance, Neoplasm ; ATP-Binding Cassette Transporters/metabolism ; Drug Resistance, Multiple ; Neoplasms ; Adenosine Triphosphate ; ATP Binding Cassette Transporter, Subfamily G, Member 2/metabolism ; Neoplasm Proteins/metabolism
Chemical Substances	ATP-Binding Cassette Transporters ; Adenosine Triphosphate (8L70Q75FXE) ; ABCG2 protein, human ; ATP Binding Cassette Transporter, Subfamily G, Member 2 ; Neoplasm Proteins
Language	English
Publishing date	2024-02-01
Publishing country	United States
Document type	Journal Article
ZDB-ID	523-x
ISSN	1096-0384 ; 0003-9861
ISSN (online)	1096-0384
ISSN	0003-9861
DOI	10.1016/j.abb.2024.109915
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Article ; Online: Subtype selective fluorescent ligands based on ICI 118,551 to study the human β2-adrenoceptor in CRISPR/Cas9 genome-edited HEK293T cells at low expression levels.

Goulding, Joëlle / Mistry, Sarah J / Soave, Mark / Woolard, Jeanette / Briddon, Stephen J / White, Carl W / Kellam, Barrie / Hill, Stephen J

Pharmacology research & perspectives

2021 Volume 9, Issue 3, Page(s) e00779

Abstract: Fluorescent ligand technologies have proved to be powerful tools to improve our understanding of ligand-receptor interactions. Here we have characterized a small focused library of nine fluorescent ligands based on the highly selective ... ...

Abstract	Fluorescent ligand technologies have proved to be powerful tools to improve our understanding of ligand-receptor interactions. Here we have characterized a small focused library of nine fluorescent ligands based on the highly selective β
MeSH term(s)	Adrenergic beta-2 Receptor Antagonists/pharmacology ; CRISPR-Cas Systems ; Fluorescence ; Gene Editing ; HEK293 Cells ; Humans ; Ligands ; Propanolamines/pharmacology ; Receptors, Adrenergic, beta-2/genetics ; Receptors, Adrenergic, beta-2/metabolism
Chemical Substances	ADRB2 protein, human ; Adrenergic beta-2 Receptor Antagonists ; Ligands ; Propanolamines ; Receptors, Adrenergic, beta-2 ; ICI 118551 (46OL1UC10R)
Language	English
Publishing date	2021-05-18
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2740389-0
ISSN	2052-1707 ; 2052-1707
ISSN (online)	2052-1707
ISSN	2052-1707
DOI	10.1002/prp2.779
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Article ; Online: Analysis of Sequence Divergence in Mammalian ABCGs Predicts a Structural Network of Residues That Underlies Functional Divergence.

Mitchell-White, James I / Stockner, Thomas / Holliday, Nicholas / Briddon, Stephen J / Kerr, Ian D

International journal of molecular sciences

2021 Volume 22, Issue 6

Abstract: The five members of the mammalian G subfamily of ATP-binding cassette transporters differ greatly in their substrate specificity. Four members of the subfamily are important in lipid transport and the wide substrate specificity of one of the members, ... ...

Abstract	The five members of the mammalian G subfamily of ATP-binding cassette transporters differ greatly in their substrate specificity. Four members of the subfamily are important in lipid transport and the wide substrate specificity of one of the members, ABCG2, is of significance due to its role in multidrug resistance. To explore the origin of substrate selectivity in members 1, 2, 4, 5 and 8 of this subfamily, we have analysed the differences in conservation between members in a multiple sequence alignment of ABCG sequences from mammals. Mapping sets of residues with similar patterns of conservation onto the resolved 3D structure of ABCG2 reveals possible explanations for differences in function, via a connected network of residues from the cytoplasmic to transmembrane domains. In ABCG2, this network of residues may confer extra conformational flexibility, enabling it to transport a wider array of substrates.
MeSH term(s)	ATP Binding Cassette Transporter, Subfamily G, Member 2/chemistry ; Allosteric Regulation ; Amino Acid Sequence ; Animals ; Conserved Sequence ; Mammals/metabolism ; Models, Molecular ; Phylogeny
Chemical Substances	ATP Binding Cassette Transporter, Subfamily G, Member 2
Language	English
Publishing date	2021-03-16
Publishing country	Switzerland
Document type	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/ijms22063012
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