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  1. Article ; Online: ONE-GO: Direct detection of context-dependent GPCR activity.

    Raskovalov, Aleksey / Kim, Donggyun / Cherezov, Vadim

    Cell research

    2024  

    Language English
    Publishing date 2024-04-30
    Publishing country England
    Document type Journal Article
    ZDB-ID 1319303-x
    ISSN 1748-7838 ; 1001-0602
    ISSN (online) 1748-7838
    ISSN 1001-0602
    DOI 10.1038/s41422-024-00966-9
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 5283: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
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  2. Article ; Online: Crystallization of Microbial Rhodopsins.

    Kovalev, Kirill / Astashkin, Roman / Gordeliy, Valentin / Cherezov, Vadim

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

    2022  Volume 2501, Page(s) 125–146

    Abstract: Microbial rhodopsins are light-sensitive transmembrane proteins, evolutionary adapted by various organisms like archaea, bacteria, simple eukaryote, and viruses to utilize solar energy for their survival. A complete understanding of functional mechanisms ...

    Abstract Microbial rhodopsins are light-sensitive transmembrane proteins, evolutionary adapted by various organisms like archaea, bacteria, simple eukaryote, and viruses to utilize solar energy for their survival. A complete understanding of functional mechanisms of these proteins is not possible without the knowledge of their high-resolution structures, which can be primarily obtained by X-ray crystallography. This technique, however, requires high-quality crystals, growing of which is a great challenge especially in case of membrane proteins. In this chapter, we summarize methods applied for crystallization of microbial rhodopsins with the emphasis on crystallization in lipidic mesophases, also known as in meso approach. In particular, we describe in detail the methods of crystallization using lipidic cubic phase to grow both large crystals optimized for traditional crystallographic data collection and microcrystals for serial crystallography.
    MeSH term(s) Crystallization/methods ; Crystallography, X-Ray ; Lipids/chemistry ; Membrane Proteins/chemistry ; Rhodopsins, Microbial
    Chemical Substances Lipids ; Membrane Proteins ; Rhodopsins, Microbial
    Language English
    Publishing date 2022-07-20
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 1940-6029
    ISSN (online) 1940-6029
    DOI 10.1007/978-1-0716-2329-9_6
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Serial femtosecond crystallography.

    Barends, Thomas R M / Stauch, Benjamin / Cherezov, Vadim / Schlichting, Ilme

    Nature reviews. Methods primers

    2022  Volume 2

    Abstract: With the advent of X-ray Free Electron Lasers (XFELs), new, high-throughput serial crystallography techniques for macromolecular structure determination have emerged. Serial femtosecond crystallography (SFX) and related methods provide possibilities ... ...

    Abstract With the advent of X-ray Free Electron Lasers (XFELs), new, high-throughput serial crystallography techniques for macromolecular structure determination have emerged. Serial femtosecond crystallography (SFX) and related methods provide possibilities beyond canonical, single-crystal rotation crystallography by mitigating radiation damage and allowing time-resolved studies with unprecedented temporal resolution. This primer aims to assist structural biology groups with little or no experience in serial crystallography planning and carrying out a successful SFX experiment. It discusses the background of serial crystallography and its possibilities. Microcrystal growth and characterization methods are discussed, alongside techniques for sample delivery and data processing. Moreover, it gives practical tips for preparing an experiment, what to consider and do during a beamtime and how to conduct the final data analysis. Finally, the Primer looks at various applications of SFX, including structure determination of membrane proteins, investigation of radiation damage-prone systems and time-resolved studies.
    Language English
    Publishing date 2022-12-26
    Publishing country England
    Document type Journal Article
    ISSN 2662-8449
    ISSN (online) 2662-8449
    DOI 10.1038/s43586-022-00141-7
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  4. Article ; Online: Chemical tools for membrane protein structural biology.

    Zhang, Qinghai / Cherezov, Vadim

    Current opinion in structural biology

    2019  Volume 58, Page(s) 278–285

    Abstract: Solving high-resolution structures of membrane proteins has been an important challenge for decades, still lagging far behind that of soluble proteins even with the recent remarkable technological advances in X-ray crystallography and electron microscopy. ...

    Abstract Solving high-resolution structures of membrane proteins has been an important challenge for decades, still lagging far behind that of soluble proteins even with the recent remarkable technological advances in X-ray crystallography and electron microscopy. Central to this challenge is the necessity to isolate and solubilize membrane proteins in a stable, natively folded and functional state, a process influenced by not only the proteins but also their surrounding chemical environment. This review highlights recent community efforts in the development and characterization of novel membrane agents and ligand tools to stabilize individual proteins and protein complexes, which together have accelerated progress in membrane protein structural biology.
    MeSH term(s) Crystallization ; Detergents/chemistry ; Membrane Proteins/chemistry ; Membrane Proteins/metabolism ; Protein Stability ; Solubility
    Chemical Substances Detergents ; Membrane Proteins
    Language English
    Publishing date 2019-07-05
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Review
    ZDB-ID 1068353-7
    ISSN 1879-033X ; 0959-440X
    ISSN (online) 1879-033X
    ISSN 0959-440X
    DOI 10.1016/j.sbi.2019.06.002
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 3206: 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)
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  5. Article ; Online: Molecular mechanisms of metabotropic GABA

    Shaye, Hamidreza / Stauch, Benjamin / Gati, Cornelius / Cherezov, Vadim

    Science advances

    2021  Volume 7, Issue 22

    Abstract: Metabotropic γ-aminobutyric acid G protein-coupled receptors ( ... ...

    Abstract Metabotropic γ-aminobutyric acid G protein-coupled receptors (GABA
    MeSH term(s) Brain/metabolism ; Ligands ; Receptors, GABA-B/chemistry ; Receptors, GABA-B/metabolism ; gamma-Aminobutyric Acid/metabolism
    Chemical Substances Ligands ; Receptors, GABA-B ; gamma-Aminobutyric Acid (56-12-2)
    Language English
    Publishing date 2021-05-28
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Review
    ZDB-ID 2810933-8
    ISSN 2375-2548 ; 2375-2548
    ISSN (online) 2375-2548
    ISSN 2375-2548
    DOI 10.1126/sciadv.abg3362
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  6. Article: MicroED structure of the human vasopressin 1B receptor.

    Shiriaeva, Anna / Martynowycz, Michael W / Nicolas, William J / Cherezov, Vadim / Gonen, Tamir

    bioRxiv : the preprint server for biology

    2023  

    Abstract: The small size and flexibility of G protein-coupled receptors (GPCRs) have long posed a significant challenge to determining their structures for research and therapeutic applications. Single particle cryogenic electron microscopy (cryoEM) is often out ... ...

    Abstract The small size and flexibility of G protein-coupled receptors (GPCRs) have long posed a significant challenge to determining their structures for research and therapeutic applications. Single particle cryogenic electron microscopy (cryoEM) is often out of reach due to the small size of the receptor without a signaling partner. Crystallization of GPCRs in lipidic cubic phase (LCP) often results in crystals that may be too small and difficult to analyze using X-ray microcrystallography at synchrotron sources or even serial femtosecond crystallography at X-ray free electron lasers. Here, we determine the previously unknown structure of the human vasopressin 1B receptor (V1BR) using microcrystal electron diffraction (MicroED). To achieve this, we grew V1BR microcrystals in LCP and transferred the material directly onto electron microscopy grids. The protein was labeled with a fluorescent dye prior to crystallization to locate the microcrystals using cryogenic fluorescence microscopy, and then the surrounding material was removed using a plasma-focused ion beam to thin the sample to a thickness amenable to MicroED. MicroED data from 14 crystalline lamellae were used to determine the 3.2 Å structure of the receptor in the crystallographic space group
    Language English
    Publishing date 2023-07-06
    Publishing country United States
    Document type Preprint
    DOI 10.1101/2023.07.05.547888
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article ; Online: Serial Femtosecond Crystallography of G Protein-Coupled Receptors.

    Stauch, Benjamin / Cherezov, Vadim

    Annual review of biophysics

    2018  Volume 47, Page(s) 377–397

    Abstract: G protein-coupled receptors (GPCRs) represent a large superfamily of membrane proteins that mediate cell signaling and regulate a variety of physiological processes in the human body. Structure-function studies of this superfamily were enabled a decade ... ...

    Abstract G protein-coupled receptors (GPCRs) represent a large superfamily of membrane proteins that mediate cell signaling and regulate a variety of physiological processes in the human body. Structure-function studies of this superfamily were enabled a decade ago by multiple breakthroughs in technology that included receptor stabilization, crystallization in a membrane environment, and microcrystallography. The recent emergence of X-ray free-electron lasers (XFELs) has further accelerated structural studies of GPCRs and other challenging proteins by overcoming radiation damage and providing access to high-resolution structures and dynamics using micrometer-sized crystals. Here, we summarize key technology advancements and major milestones of GPCR research using XFELs and provide a brief outlook on future developments in the field.
    MeSH term(s) Crystallography/methods ; Humans ; Lasers ; Receptors, G-Protein-Coupled/chemistry
    Chemical Substances Receptors, G-Protein-Coupled
    Language English
    Publishing date 2018-03-15
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S. ; Review
    ZDB-ID 2434725-5
    ISSN 1936-1238 ; 1936-122X
    ISSN (online) 1936-1238
    ISSN 1936-122X
    DOI 10.1146/annurev-biophys-070317-033239
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Se 190: Show issues Location:
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    ab Jg. 2022: Lesesaal (EG)

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  8. Article ; Online: Lipidic cubic phase technologies for membrane protein structural studies.

    Cherezov, Vadim

    Current opinion in structural biology

    2011  Volume 21, Issue 4, Page(s) 559–566

    Abstract: Lipidic cubic phase (LCP) is a membrane-mimetic matrix suitable for stabilization and crystallization of membrane proteins in lipidic environment. LCP technologies, however, have not been fully embraced by the membrane protein structural biology ... ...

    Abstract Lipidic cubic phase (LCP) is a membrane-mimetic matrix suitable for stabilization and crystallization of membrane proteins in lipidic environment. LCP technologies, however, have not been fully embraced by the membrane protein structural biology community, primarily because of the difficulties associated with handling viscous materials. Recent developments of pre-crystallization assays and improvements in crystal imaging, successes in obtaining high resolution structures of G protein-coupled receptors (GPCRs), and commercial availability of LCP tools and instruments are beginning to attract structural biologists to integrate LCP technologies in their research. This wider acceptance should translate to an increased number of otherwise difficult-to-crystallize membrane protein structures, shedding light on their functional mechanisms and on structural details of lipid-protein interactions.
    MeSH term(s) Crystallization/methods ; Crystallography, X-Ray ; Humans ; Lipids/chemistry ; Membrane Proteins/chemistry
    Chemical Substances Lipids ; Membrane Proteins
    Language English
    Publishing date 2011-07-19
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Review
    ZDB-ID 1068353-7
    ISSN 1879-033X ; 0959-440X
    ISSN (online) 1879-033X
    ISSN 0959-440X
    DOI 10.1016/j.sbi.2011.06.007
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 3206: Show issues Location:
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  9. Article: Structural insights into melatonin receptors

    Stauch, Benjamin / Johansson, Linda C / Cherezov, Vadim

    FEBS journal. 2020 Apr., v. 287, no. 8

    2020  

    Abstract: The long‐anticipated high‐resolution structures of the human melatonin G protein‐coupled receptors MT₁ and MT₂, involved in establishing and maintaining circadian rhythm, were obtained in complex with two melatonin analogs and two approved anti‐insomnia ... ...

    Abstract The long‐anticipated high‐resolution structures of the human melatonin G protein‐coupled receptors MT₁ and MT₂, involved in establishing and maintaining circadian rhythm, were obtained in complex with two melatonin analogs and two approved anti‐insomnia and antidepression drugs using X‐ray free‐electron laser serial femtosecond crystallography. The structures shed light on the overall conformation and unusual structural features of melatonin receptors, as well as their ligand binding sites and the melatonergic pharmacophore, thereby providing insights into receptor subtype selectivity. The structures revealed an occluded orthosteric ligand binding site with a membrane‐buried channel for ligand entry in both receptors, and an additional putative ligand entry path in MT₂ from the extracellular side. This unexpected ligand entry mode contributes to facilitating the high specificity with which melatonin receptors bind their cognate ligand and exclude structurally similar molecules such as serotonin, the biosynthetic precursor of melatonin. Finally, the MT₂ structure allowed accurate mapping of type 2 diabetes‐related single‐nucleotide polymorphisms, where a clustering of residues in helices I and II on the protein–membrane interface was observed which could potentially influence receptor oligomerization. The role of receptor oligomerization is further discussed in light of the differential interaction of MT₁ and MT₂ with GPR50, a regulatory melatonin coreceptor. The melatonin receptor structures will facilitate design of selective tool compounds to further dissect the specific physiological function of each receptor subtype as well as provide a structural basis for next‐generation sleeping aids and other drugs targeting these receptors with higher specificity and fewer side effects.
    Keywords X-radiation ; biosynthesis ; circadian rhythm ; crystallography ; humans ; ligands ; melatonin ; oligomerization ; pharmacology ; serotonin
    Language English
    Dates of publication 2020-04
    Size p. 1496-1510.
    Publishing place John Wiley & Sons, Ltd
    Document type Article
    Note NAL-AP-2-clean ; REVIEW
    ZDB-ID 2173655-8
    ISSN 1742-4658 ; 1742-464X
    ISSN (online) 1742-4658
    ISSN 1742-464X
    DOI 10.1111/febs.15128
    Database NAL-Catalogue (AGRICOLA)

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  10. Article ; Online: Structural insights into melatonin receptors.

    Stauch, Benjamin / Johansson, Linda C / Cherezov, Vadim

    The FEBS journal

    2019  Volume 287, Issue 8, Page(s) 1496–1510

    Abstract: The long-anticipated high-resolution structures of the human melatonin G protein-coupled receptors ... ...

    Abstract The long-anticipated high-resolution structures of the human melatonin G protein-coupled receptors MT
    MeSH term(s) Animals ; Drug Design ; Humans ; Protein Conformation ; Receptors, Melatonin/chemistry ; Receptors, Melatonin/metabolism ; Sleep Aids, Pharmaceutical
    Chemical Substances Receptors, Melatonin ; Sleep Aids, Pharmaceutical
    Language English
    Publishing date 2019-11-23
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S. ; Review
    ZDB-ID 2173655-8
    ISSN 1742-4658 ; 1742-464X
    ISSN (online) 1742-4658
    ISSN 1742-464X
    DOI 10.1111/febs.15128
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    In stock of ZB MED Cologne/Königswinter

    Zs.A 260: Show issues Location:
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