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  1. Article ; Online: All about NASH: disease biology, targets, and opportunities on the road to NASH drugs.

    Xu, H Eric / Guo, Jin-Song

    Acta pharmacologica Sinica

    2022  Volume 43, Issue 5, Page(s) 1101–1102

    MeSH term(s) Biology ; Humans ; Non-alcoholic Fatty Liver Disease/drug therapy
    Language English
    Publishing date 2022-04-04
    Publishing country United States
    Document type Editorial
    ZDB-ID 1360774-1
    ISSN 1745-7254 ; 0253-9756 ; 1671-4083
    ISSN (online) 1745-7254
    ISSN 0253-9756 ; 1671-4083
    DOI 10.1038/s41401-022-00900-y
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    Zs.A 1904: Show issues Location:
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  2. Article ; Online: Cryo-electron microscopy for GPCR research and drug discovery in endocrinology and metabolism.

    Duan, Jia / He, Xin-Heng / Li, Shu-Jie / Xu, H Eric

    Nature reviews. Endocrinology

    2024  Volume 20, Issue 6, Page(s) 349–365

    Abstract: G protein-coupled receptors (GPCRs) are the largest family of cell surface receptors, with many GPCRs having crucial roles in endocrinology and metabolism. Cryogenic electron microscopy (cryo-EM) has revolutionized the field of structural biology, ... ...

    Abstract G protein-coupled receptors (GPCRs) are the largest family of cell surface receptors, with many GPCRs having crucial roles in endocrinology and metabolism. Cryogenic electron microscopy (cryo-EM) has revolutionized the field of structural biology, particularly regarding GPCRs, over the past decade. Since the first pair of GPCR structures resolved by cryo-EM were published in 2017, the number of GPCR structures resolved by cryo-EM has surpassed the number resolved by X-ray crystallography by 30%, reaching >650, and the number has doubled every ~0.63 years for the past 6 years. At this pace, it is predicted that the structure of 90% of all human GPCRs will be completed within the next 5-7 years. This Review highlights the general structural features and principles that guide GPCR ligand recognition, receptor activation, G protein coupling, arrestin recruitment and regulation by GPCR kinases. The Review also highlights the diversity of GPCR allosteric binding sites and how allosteric ligands could dictate biased signalling that is selective for a G protein pathway or an arrestin pathway. Finally, the authors use the examples of glycoprotein hormone receptors and glucagon-like peptide 1 receptor to illustrate the effect of cryo-EM on understanding GPCR biology in endocrinology and metabolism, as well as on GPCR-related endocrine diseases and drug discovery.
    MeSH term(s) Cryoelectron Microscopy/methods ; Humans ; Receptors, G-Protein-Coupled/metabolism ; Receptors, G-Protein-Coupled/chemistry ; Drug Discovery/methods ; Endocrinology/methods ; Animals ; Signal Transduction ; Ligands
    Chemical Substances Receptors, G-Protein-Coupled ; Ligands
    Language English
    Publishing date 2024-02-29
    Publishing country England
    Document type Journal Article ; Review ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
    ZDB-ID 2489381-X
    ISSN 1759-5037 ; 1759-5029
    ISSN (online) 1759-5037
    ISSN 1759-5029
    DOI 10.1038/s41574-024-00957-1
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  3. Article ; Online: ARID3a from the ARID family: structure, role in autoimmune diseases and drug discovery.

    Guo, Cheng-Cen / Xu, H Eric / Ma, Xiong

    Acta pharmacologica Sinica

    2023  Volume 44, Issue 11, Page(s) 2139–2150

    Abstract: The AT-rich interaction domain (ARID) family of DNA-binding proteins is a group of transcription factors and chromatin regulators with a highly conserved ARID domain that recognizes specific AT-rich DNA sequences. Dysfunction of ARID family members has ... ...

    Abstract The AT-rich interaction domain (ARID) family of DNA-binding proteins is a group of transcription factors and chromatin regulators with a highly conserved ARID domain that recognizes specific AT-rich DNA sequences. Dysfunction of ARID family members has been implicated in various human diseases including cancers and intellectual disability. Among them, ARID3a has gained increasing attention due to its potential involvement in autoimmunity. In this article we provide an overview of the ARID family, focusing on the structure and biological functions of ARID3a. It explores the role of ARID3a in autoreactive B cells and its contribution to autoimmune diseases such as systemic lupus erythematosus and primary biliary cholangitis. Furthermore, we also discuss the potential for drug discovery targeting ARID3a and present a plan for future research in this field.
    MeSH term(s) Humans ; Transcription Factors/genetics ; Transcription Factors/metabolism ; DNA-Binding Proteins/genetics ; DNA-Binding Proteins/metabolism ; B-Lymphocytes/metabolism ; Autoimmune Diseases/drug therapy ; Autoimmune Diseases/metabolism
    Chemical Substances Transcription Factors ; DNA-Binding Proteins
    Language English
    Publishing date 2023-07-24
    Publishing country United States
    Document type Journal Article ; Review
    ZDB-ID 1360774-1
    ISSN 1745-7254 ; 0253-9756 ; 1671-4083
    ISSN (online) 1745-7254
    ISSN 0253-9756 ; 1671-4083
    DOI 10.1038/s41401-023-01134-2
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    Zs.A 1904: Show issues Location:
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  4. Article ; Online: GABA

    Jiang, Yi / Xu, H Eric

    Cell research

    2020  Volume 30, Issue 8, Page(s) 631–632

    MeSH term(s) Cryoelectron Microscopy ; Receptors, GABA-B ; gamma-Aminobutyric Acid
    Chemical Substances Receptors, GABA-B ; gamma-Aminobutyric Acid (56-12-2)
    Language English
    Publishing date 2020-07-07
    Publishing country England
    Document type Journal Article ; Comment
    ZDB-ID 1319303-x
    ISSN 1748-7838 ; 1001-0602
    ISSN (online) 1748-7838
    ISSN 1001-0602
    DOI 10.1038/s41422-020-0373-y
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    Zs.A 5283: Show issues Location:
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  5. Article: RNA-dependent RNA polymerase: Structure, mechanism, and drug discovery for COVID-19

    Jiang, Yi / Yin, Wanchao / Xu, H. Eric

    Biochemical and biophysical research communications. 2021 Jan. 29, v. 538

    2021  

    Abstract: Coronavirus disease 2019 (COVID-19) caused by severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) has rapidly become a global pandemic. Although great efforts have been made to develop effective therapeutic interventions, only the nucleotide ... ...

    Abstract Coronavirus disease 2019 (COVID-19) caused by severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) has rapidly become a global pandemic. Although great efforts have been made to develop effective therapeutic interventions, only the nucleotide analog remdesivir was approved for emergency use against COVID-19. Remdesivir targets the RNA-dependent RNA polymerase (RdRp), an essential enzyme for viral RNA replication and a promising drug target for COVID-19. Recently, several structures of RdRp in complex with substrate RNA and remdesivir were reported, providing insights into the mechanisms of RNA recognition by RdRp. These structures also reveal the mechanism of RdRp inhibition by nucleotide inhibitors and offer a molecular template for the development of RdRp-targeting drugs. This review discusses the recognition mechanism of RNA and nucleotide inhibitor by RdRp, and its implication in drug discovery.
    Keywords COVID-19 infection ; RNA ; RNA replication ; RNA-directed RNA polymerase ; Severe acute respiratory syndrome coronavirus 2 ; drugs ; pandemic ; research ; therapeutics
    Language English
    Dates of publication 2021-0129
    Size p. 47-53.
    Publishing place Elsevier Inc.
    Document type Article
    Note NAL-AP-2-clean
    ZDB-ID 205723-2
    ISSN 0006-291X ; 0006-291X
    ISSN (online) 0006-291X
    ISSN 0006-291X
    DOI 10.1016/j.bbrc.2020.08.116
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  6. Article ; Online: Family reunion of nuclear hormone receptors: structures, diseases, and drug discovery.

    Xu, H Eric

    Acta pharmacologica Sinica

    2015  Volume 36, Issue 1, Page(s) 1–2

    MeSH term(s) Drug Discovery/methods ; Hormones/metabolism ; Humans ; Receptors, Cytoplasmic and Nuclear/metabolism
    Chemical Substances Hormones ; Receptors, Cytoplasmic and Nuclear
    Language English
    Publishing date 2015-01
    Publishing country United States
    Document type Editorial ; Introductory Journal Article
    ZDB-ID 1360774-1
    ISSN 1745-7254 ; 0253-9756 ; 1671-4083
    ISSN (online) 1745-7254
    ISSN 0253-9756 ; 1671-4083
    DOI 10.1038/aps.2014.140
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  7. Article ; Online: Structure genomics of SARS-CoV-2 and its Omicron variant: drug design templates for COVID-19.

    Wu, Can-Rong / Yin, Wan-Chao / Jiang, Yi / Xu, H Eric

    Acta pharmacologica Sinica

    2022  Volume 43, Issue 12, Page(s) 3021–3033

    Abstract: Coronavirus disease 2019 (COVID-19), caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), has brought an unprecedented public health crisis and persistently threatens to humanity. With tireless efforts from scientists around the world, ...

    Abstract Coronavirus disease 2019 (COVID-19), caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), has brought an unprecedented public health crisis and persistently threatens to humanity. With tireless efforts from scientists around the world, understanding of the biology of coronavirus has been greatly enhanced over the past 2 years. Structural biology has demonstrated its powerful impact on uncovering structures and functions for the vast majority of SARS-CoV-2 proteins and guided the development of drugs and vaccines against COVID-19. In this review, we summarize current progress in the structural biology of SARS-CoV-2 and discuss important biological issues that remain to be addressed. We present the examples of structure-based design of Pfizer's novel anti-SARS-CoV-2 drug PF-07321332 (Paxlovid), Merck's nucleotide inhibitor molnupiravir (Lagevrio), and VV116, an oral drug candidate for COVID-19. These examples highlight the importance of structure in drug discovery to combat COVID-19. We also discussed the recent variants of Omicron and its implication in immunity escape from existing vaccines and antibody therapies.
    MeSH term(s) Humans ; SARS-CoV-2/genetics ; COVID-19/drug therapy ; COVID-19 Vaccines ; Drug Design ; Genomics
    Chemical Substances nirmatrelvir (7R9A5P7H32) ; COVID-19 Vaccines
    Language English
    Publishing date 2022-01-20
    Publishing country United States
    Document type Journal Article ; Review
    ZDB-ID 1360774-1
    ISSN 1745-7254 ; 0253-9756 ; 1671-4083
    ISSN (online) 1745-7254
    ISSN 0253-9756 ; 1671-4083
    DOI 10.1038/s41401-021-00851-w
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  8. Article ; Online: Cryo-EM structures of adenosine receptor A

    Cai, Hongmin / Guo, Shimeng / Xu, Youwei / Sun, Jun / Li, Junrui / Xia, Zhikan / Jiang, Yi / Xie, Xin / Xu, H Eric

    Nature communications

    2024  Volume 15, Issue 1, Page(s) 3252

    Abstract: The adenosine ... ...

    Abstract The adenosine A
    MeSH term(s) Humans ; Receptor, Adenosine A3/metabolism ; Cryoelectron Microscopy ; Signal Transduction
    Chemical Substances Receptor, Adenosine A3
    Language English
    Publishing date 2024-04-16
    Publishing country England
    Document type Journal Article
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/s41467-024-47207-6
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  9. Article ; Online: AlphaFold: Research accelerator and hypothesis generator.

    Campbell, Elizabeth A / Walden, Helen / Walter, Johannes C / Shukla, Arun K / Beck, Martin / Passmore, Lori A / Xu, H Eric

    Molecular cell

    2024  Volume 84, Issue 3, Page(s) 404–408

    Abstract: To celebrate the 50th anniversary of Cell Press and the Cell focus issue on structural biology, we discussed with scientists working across diverse fields how AlphaFold has changed their research and brought structural biology to the masses. ...

    Abstract To celebrate the 50th anniversary of Cell Press and the Cell focus issue on structural biology, we discussed with scientists working across diverse fields how AlphaFold has changed their research and brought structural biology to the masses.
    MeSH term(s) Molecular Biology ; Anniversaries and Special Events
    Language English
    Publishing date 2024-02-01
    Publishing country United States
    Document type Journal Article
    ZDB-ID 1415236-8
    ISSN 1097-4164 ; 1097-2765
    ISSN (online) 1097-4164
    ISSN 1097-2765
    DOI 10.1016/j.molcel.2023.12.035
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    Zs.A 5055: Show issues Location:
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  10. Article ; Online: RNA-dependent RNA polymerase: Structure, mechanism, and drug discovery for COVID-19.

    Jiang, Yi / Yin, Wanchao / Xu, H Eric

    Biochemical and biophysical research communications

    2020  Volume 538, Page(s) 47–53

    Abstract: Coronavirus disease 2019 (COVID-19) caused by severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) has rapidly become a global pandemic. Although great efforts have been made to develop effective therapeutic interventions, only the nucleotide ... ...

    Abstract Coronavirus disease 2019 (COVID-19) caused by severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) has rapidly become a global pandemic. Although great efforts have been made to develop effective therapeutic interventions, only the nucleotide analog remdesivir was approved for emergency use against COVID-19. Remdesivir targets the RNA-dependent RNA polymerase (RdRp), an essential enzyme for viral RNA replication and a promising drug target for COVID-19. Recently, several structures of RdRp in complex with substrate RNA and remdesivir were reported, providing insights into the mechanisms of RNA recognition by RdRp. These structures also reveal the mechanism of RdRp inhibition by nucleotide inhibitors and offer a molecular template for the development of RdRp-targeting drugs. This review discusses the recognition mechanism of RNA and nucleotide inhibitor by RdRp, and its implication in drug discovery.
    MeSH term(s) Adenosine Monophosphate/analogs & derivatives ; Adenosine Monophosphate/chemistry ; Adenosine Monophosphate/pharmacology ; Alanine/analogs & derivatives ; Alanine/chemistry ; Alanine/pharmacology ; Antiviral Agents/chemistry ; Antiviral Agents/pharmacology ; COVID-19/drug therapy ; Catalytic Domain ; Coronavirus RNA-Dependent RNA Polymerase ; Drug Discovery ; Humans ; Nucleic Acid Synthesis Inhibitors/chemistry ; Nucleic Acid Synthesis Inhibitors/pharmacology ; Protein Conformation ; RNA, Viral/biosynthesis ; SARS-CoV-2/drug effects ; SARS-CoV-2/enzymology ; SARS-CoV-2/genetics ; Virus Replication/drug effects
    Chemical Substances Antiviral Agents ; Nucleic Acid Synthesis Inhibitors ; RNA, Viral ; remdesivir (3QKI37EEHE) ; Adenosine Monophosphate (415SHH325A) ; Coronavirus RNA-Dependent RNA Polymerase (EC 2.7.7.48) ; NSP12 protein, SARS-CoV-2 (EC 2.7.7.48) ; Alanine (OF5P57N2ZX)
    Keywords covid19
    Language English
    Publishing date 2020-09-04
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 205723-2
    ISSN 1090-2104 ; 0006-291X ; 0006-291X
    ISSN (online) 1090-2104 ; 0006-291X
    ISSN 0006-291X
    DOI 10.1016/j.bbrc.2020.08.116
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    Zs.A 116: Show issues Location:
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