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    Recombinant ACE2-Ig Fusion Protein Neutralizes SARS-CoV-2

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    https://www.riss.kr/link?id=A108081002

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    다국어 초록 (Multilingual Abstract) kakao i 다국어 번역

    A novel coronavirus (SARS-CoV-2) is the causative agent for the COVID-19 pandemic, and needs for effective antiviral drugs have been demanded. Angiotensin-converting enzyme 2 (ACE2) has been shown to be a cellular receptor for SARS-CoV and SARS-CoV-2. For the therapeutic validation of ACE2, a recombinant protein consisting of the ACE2 extracellular domain fused to the IgG1 Fc domain (ACE2-Ig) was generated. ACE2-Ig exhibits proper pharmacological properties and binds with a high affinity to SARS-CoV and SARS-CoV-2 receptor-binding domain. Further, it neutralizes virus with SARS-CoV and SARS-CoV-2 spike proteins. Taken overall, these data suggest that ACE2-Ig has substantial anti-SARS-CoV-2 properties and warrant further study concerning its potential applications for the treatment of SARS-CoV-2.ㅍㅍㅍㅍㅍㅍ
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    A novel coronavirus (SARS-CoV-2) is the causative agent for the COVID-19 pandemic, and needs for effective antiviral drugs have been demanded. Angiotensin-converting enzyme 2 (ACE2) has been shown to be a cellular receptor for SARS-CoV and SARS-CoV-2....

    A novel coronavirus (SARS-CoV-2) is the causative agent for the COVID-19 pandemic, and needs for effective antiviral drugs have been demanded. Angiotensin-converting enzyme 2 (ACE2) has been shown to be a cellular receptor for SARS-CoV and SARS-CoV-2. For the therapeutic validation of ACE2, a recombinant protein consisting of the ACE2 extracellular domain fused to the IgG1 Fc domain (ACE2-Ig) was generated. ACE2-Ig exhibits proper pharmacological properties and binds with a high affinity to SARS-CoV and SARS-CoV-2 receptor-binding domain. Further, it neutralizes virus with SARS-CoV and SARS-CoV-2 spike proteins. Taken overall, these data suggest that ACE2-Ig has substantial anti-SARS-CoV-2 properties and warrant further study concerning its potential applications for the treatment of SARS-CoV-2.ㅍㅍㅍㅍㅍㅍ

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    다국어 초록 (Multilingual Abstract) kakao i 다국어 번역

    A novel coronavirus (SARS-CoV-2) is the causative agent for the COVID-19 pandemic, and needs for effective antiviral drugs have been demanded. Angiotensin-converting enzyme 2 (ACE2) has been shown to be a cellular receptor for SARS-CoV and SARS-CoV-2. For the therapeutic validation of ACE2, a recombinant protein consisting of the ACE2 extracellular domain fused to the IgG1 Fc domain (ACE2-Ig) was generated. ACE2-Ig exhibits proper pharmacological properties and binds with a high affinity to SARS-CoV and SARS-CoV-2 receptor-binding domain. Further, it neutralizes virus with SARS-CoV and SARS-CoV-2 spike proteins. Taken overall, these data suggest that ACE2-Ig has substantial anti-SARS-CoV-2 properties and warrant further study concerning its potential applications for the treatment of SARS-CoV-2.
    번역하기

    A novel coronavirus (SARS-CoV-2) is the causative agent for the COVID-19 pandemic, and needs for effective antiviral drugs have been demanded. Angiotensin-converting enzyme 2 (ACE2) has been shown to be a cellular receptor for SARS-CoV and SARS-CoV-2....

    A novel coronavirus (SARS-CoV-2) is the causative agent for the COVID-19 pandemic, and needs for effective antiviral drugs have been demanded. Angiotensin-converting enzyme 2 (ACE2) has been shown to be a cellular receptor for SARS-CoV and SARS-CoV-2. For the therapeutic validation of ACE2, a recombinant protein consisting of the ACE2 extracellular domain fused to the IgG1 Fc domain (ACE2-Ig) was generated. ACE2-Ig exhibits proper pharmacological properties and binds with a high affinity to SARS-CoV and SARS-CoV-2 receptor-binding domain. Further, it neutralizes virus with SARS-CoV and SARS-CoV-2 spike proteins. Taken overall, these data suggest that ACE2-Ig has substantial anti-SARS-CoV-2 properties and warrant further study concerning its potential applications for the treatment of SARS-CoV-2.

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    참고문헌 (Reference)

    1 Yan R, "Structural basis for the recognition of SARS-CoV-2 by full-length human ACE2" 367 : 1444-1448, 2020

    2 Liu P, "Novel ACE2-Fc chimeric fusion provides long-lasting hypertension control and organ protection in mouse models of systemic renin angiotensin system activation" 94 : 114-125, 2018

    3 Lei C, "Neutralization of SARS-CoV-2 spike pseudotyped virus by recombinant ACE2-Ig" 11 : 2070-, 2020

    4 Jackson CB, "Mechanisms of SARS-CoV-2 entry into cells" 23 : 3-20, 2022

    5 Junker F, "Fc gamma receptors and their role in antigen uptake, presentation, and T cell activation" 11 : 1393-, 2020

    6 Wrapp D, "Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation" 367 : 1260-1263, 2020

    7 Huang C, "Clinical features of patients infected with 2019 novel coronavirus in Wuhan, China" 395 : 497-506, 2020

    8 Rice GI, "Circulating activities of angiotensin-converting enzyme, its homolog, angiotensin-converting enzyme 2, and neprilysin in a family study" 48 : 914-920, 2006

    1 Yan R, "Structural basis for the recognition of SARS-CoV-2 by full-length human ACE2" 367 : 1444-1448, 2020

    2 Liu P, "Novel ACE2-Fc chimeric fusion provides long-lasting hypertension control and organ protection in mouse models of systemic renin angiotensin system activation" 94 : 114-125, 2018

    3 Lei C, "Neutralization of SARS-CoV-2 spike pseudotyped virus by recombinant ACE2-Ig" 11 : 2070-, 2020

    4 Jackson CB, "Mechanisms of SARS-CoV-2 entry into cells" 23 : 3-20, 2022

    5 Junker F, "Fc gamma receptors and their role in antigen uptake, presentation, and T cell activation" 11 : 1393-, 2020

    6 Wrapp D, "Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation" 367 : 1260-1263, 2020

    7 Huang C, "Clinical features of patients infected with 2019 novel coronavirus in Wuhan, China" 395 : 497-506, 2020

    8 Rice GI, "Circulating activities of angiotensin-converting enzyme, its homolog, angiotensin-converting enzyme 2, and neprilysin in a family study" 48 : 914-920, 2006

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    학술지 이력

    학술지 이력
    연월일 이력구분 이력상세 등재구분
    2023 평가 해외DB학술지평가 신청대상 (해외등재 학술지 평가)
    2020-01-01 등재 등재학술지 유지 (해외등재 학술지 평가) KCI등재
    2010-01-01 등재 등재학술지 유지 (등재유지) KCI등재
    2008-01-01 등재 등재 1차 FAIL (등재유지) KCI등재
    2006-07-18 학술지명변경 외국어명 : 미등록 -> Journal of Bacteriology and Virology KCI등재
    2006-01-01 등재 등재학술지 유지 (등재유지) KCI등재
    2003-01-01 등재 등재학술지 선정 (등재후보2차) KCI등재
    2002-01-01 등재 등재후보 1차 PASS (등재후보1차) KCI등재후보
    1998-07-01 등재 등재후보학술지 선정 (신규평가) KCI등재후보
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    학술지 인용정보
    기준연도 WOS-KCI 통합IF(2년) KCIF(2년) KCIF(3년)
    2016 0.23 0.23 0.2
    KCIF(4년) KCIF(5년) 중심성지수(3년) 즉시성지수
    0.19 0.18 0.358 0.03
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