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Article ; Online: Zinc finger proteins in the host-virus interplay: multifaceted functions based on their nucleic acid-binding property.

Wang, Guanming / Zheng, Chunfu

2021 Volume 45, Issue 3

Abstract: Zinc finger proteins (ZFPs) are a huge family comprised of massive, structurally diverse proteins characterized by zinc ion coordinating. They engage in the host-virus interplay in-depth and occupy a significant portion of the host antiviral arsenal. ... ...

Abstract	Zinc finger proteins (ZFPs) are a huge family comprised of massive, structurally diverse proteins characterized by zinc ion coordinating. They engage in the host-virus interplay in-depth and occupy a significant portion of the host antiviral arsenal. Nucleic acid-binding is the basic property of certain ZFPs, which draws increasing attention due to their immense influence on viral infections. ZFPs exert multiple roles on the viral replications and host cell transcription profiles by recognizing viral genomes and host mRNAs. Their roles could be either antiviral or proviral and were separately discussed. Our review covers the recent research progress and provides a comprehensive understanding of ZFPs in antiviral immunity based on their DNA/RNA binding property.
Language	English
Publishing date	2021-05-06
Publishing country	England
Document type	Journal Article
ZDB-ID	283740-7
ISSN	1574-6976 ; 0168-6445
ISSN (online)	1574-6976
ISSN	0168-6445
DOI	10.1093/femsre/fuaa059
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Article ; Online: The therapeutic potential of arctigenin against multiple human diseases: A mechanistic review.

Wang, Guanming / Ge, Li / Liu, Tongyu / Zheng, Zhihui / Chen, Lijun

Phytomedicine : international journal of phytotherapy and phytopharmacology

2023 Volume 110, Page(s) 154647

Abstract: Background: Arctigenin (ATG), a dibenzyl butyrolactone lignan compound, is one of the major bioactive components from the medicinal plant Arctium lappa. ATG possesses remarkable therapeutic potential against a wide range of human diseases, such as ... ...

Abstract	Background: Arctigenin (ATG), a dibenzyl butyrolactone lignan compound, is one of the major bioactive components from the medicinal plant Arctium lappa. ATG possesses remarkable therapeutic potential against a wide range of human diseases, such as cancers, immune disorders and chronical diseases. The molecular mechanisms behind the biological effects of ATG have been intensively studied. Purpose: This review aims to systematically summarize the updated knowledge of the proteins and signaling pathways behind the curative property of ATG, and further analyze the potential connections between them. Method: SciFinder, Pubmed, Web of Science and Cochrane Library databases were queried for publications reporting the therapeutic properties of ATG. "Arctigenin", "disease", "cancer", "inflammation", "organ damage", "infection", "toxicity" and "pharmacokinetics" were used as the searching titles. Result: 625 publications were identified and 95 met the inclusion criteria and exclusion criteria. 42 studies described the molecular mechanisms implicated in ATG treatments. Several proteins including phosphodiesterase subtype 4D (PDE4D), estrogen receptor (ER) β, protein phosphatase 2A (PP2A), phosphoinositide 3-kinase (PI3K) and transmembrane protein 16A (TMEM16A) are targeted by ATG in different settings. The frequently described signaling pathways are TLR4/NF-κB, PI3K/AKT/mTOR, AMP-activated protein kinase (AMPK) and nuclear factor erythroid 2-related factor 2 (Nrf-2) signalings. Conclusion: Inhibition of PI3K/AKT pathway and activation of AMPK signaling play the pivotal roles in the therapeutic effects of ATG. PI3K/AKT and AMPK signaling widely link to other signaling pathways, modulating various biological processes such as anti-inflammation, anti-oxidative stress, anti-fibrosis, anti-ER stress, anti-steatosis and pro-apoptosis, which constitute the curative mechanisms of ATG against multiple human diseases.
MeSH term(s)	Humans ; Phosphatidylinositol 3-Kinases/metabolism ; Proto-Oncogene Proteins c-akt/metabolism ; AMP-Activated Protein Kinases ; Lignans/pharmacology ; Lignans/therapeutic use ; Phosphatidylinositol 3-Kinase ; Neoplasms/drug therapy ; Furans/pharmacology ; Furans/therapeutic use
Chemical Substances	Phosphatidylinositol 3-Kinases (EC 2.7.1.-) ; Proto-Oncogene Proteins c-akt (EC 2.7.11.1) ; AMP-Activated Protein Kinases (EC 2.7.11.31) ; arctigenin (U76MR9VS6M) ; Lignans ; Phosphatidylinositol 3-Kinase (EC 2.7.1.137) ; Furans
Language	English
Publishing date	2023-01-02
Publishing country	Germany
Document type	Journal Article ; Review
ZDB-ID	1205240-1
ISSN	1618-095X ; 0944-7113
ISSN (online)	1618-095X
ISSN	0944-7113
DOI	10.1016/j.phymed.2023.154647
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Article ; Online: Zinc finger proteins in the host-virus interplay: multifaceted functions based on their nucleic acid-binding property.

Wang, Guanming / Zheng, Chunfu

FEMS microbiology reviews

2020 Volume 45, Issue 3

Abstract	Zinc finger proteins (ZFPs) are a huge family comprised of massive, structurally diverse proteins characterized by zinc ion coordinating. They engage in the host-virus interplay in-depth and occupy a significant portion of the host antiviral arsenal. Nucleic acid-binding is the basic property of certain ZFPs, which draws increasing attention due to their immense influence on viral infections. ZFPs exert multiple roles on the viral replications and host cell transcription profiles by recognizing viral genomes and host mRNAs. Their roles could be either antiviral or proviral and were separately discussed. Our review covers the recent research progress and provides a comprehensive understanding of ZFPs in antiviral immunity based on their DNA/RNA binding property.
MeSH term(s)	DNA-Binding Proteins/metabolism ; Gene Expression Regulation/physiology ; Host Microbial Interactions/physiology ; Nucleic Acids/metabolism ; Virus Replication/physiology ; Zinc Fingers
Chemical Substances	DNA-Binding Proteins ; Nucleic Acids
Language	English
Publishing date	2020-11-23
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	283740-7
ISSN	1574-6976 ; 0168-6445
ISSN (online)	1574-6976
ISSN	0168-6445
DOI	10.1093/femsre/fuaa059
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Article ; Online: K63-linked polyubiquitination of LGP2 by Riplet regulates RIG-I-dependent innate immune response.

Kouwaki, Takahisa / Nishimura, Tasuku / Wang, Guanming / Nakagawa, Reiko / Oshiumi, Hiroyuki

EMBO reports

2022 Volume 24, Issue 2, Page(s) e54844

Abstract: Type I interferons (IFNs) exhibit strong antiviral activity and induce the expression of antiviral proteins. Since excessive expression of type I IFNs is harmful to the host, their expression should be turned off at the appropriate time. In this study, ... ...

Abstract	Type I interferons (IFNs) exhibit strong antiviral activity and induce the expression of antiviral proteins. Since excessive expression of type I IFNs is harmful to the host, their expression should be turned off at the appropriate time. In this study, we find that post-translational modification of LGP2, a member of the RIG-I-like receptor family, modulates antiviral innate immune responses. The LGP2 protein undergoes K63-linked polyubiquitination in response to cytoplasmic double-stranded RNAs or viral infection. Our mass spectrometry analysis reveals the K residues ubiquitinated by the Riplet ubiquitin ligase. LGP2 ubiquitination occurs with a delay compared to RIG-I ubiquitination. Interestingly, ubiquitination-defective LGP2 mutations increase the expression of type I IFN at a late phase, whereas the mutant proteins attenuate other antiviral proteins, such as SP100, PML, and ANKRD1. Our data indicate that delayed polyubiquitination of LGP2 fine-tunes RIG-I-dependent antiviral innate immune responses at a late phase of viral infection.
MeSH term(s)	Humans ; Antiviral Agents ; DEAD Box Protein 58/genetics ; DEAD Box Protein 58/metabolism ; DEAD-box RNA Helicases/genetics ; Immunity, Innate ; Interferon Type I/genetics ; Ubiquitin/metabolism ; Ubiquitination ; Virus Diseases
Chemical Substances	Antiviral Agents ; DEAD Box Protein 58 (EC 3.6.4.13) ; DEAD-box RNA Helicases (EC 3.6.4.13) ; Interferon Type I ; Ubiquitin ; RIGI protein, human (EC 3.6.1.-) ; DHX58 protein, human (EC 2.7.7.-)
Language	English
Publishing date	2022-12-14
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2020896-0
ISSN	1469-3178 ; 1469-221X
ISSN (online)	1469-3178
ISSN	1469-221X
DOI	10.15252/embr.202254844
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Zs.A 5433: 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) ab Jg. 2022: Lesesaal (EG)
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Article ; Online: RIG-I-Like Receptor-Mediated Recognition of Viral Genomic RNA of Severe Acute Respiratory Syndrome Coronavirus-2 and Viral Escape From the Host Innate Immune Responses.

Kouwaki, Takahisa / Nishimura, Tasuku / Wang, Guanming / Oshiumi, Hiroyuki

Frontiers in immunology

2021 Volume 12, Page(s) 700926

Abstract: RIG-I-like receptors (RLR), RIG-I and MDA5, are cytoplasmic viral RNA sensors that recognize viral double-stranded RNAs and trigger signals to induce antiviral responses, including type I interferon production. Severe acute respiratory syndrome ... ...

Abstract	RIG-I-like receptors (RLR), RIG-I and MDA5, are cytoplasmic viral RNA sensors that recognize viral double-stranded RNAs and trigger signals to induce antiviral responses, including type I interferon production. Severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) caused the coronavirus disease 2019 pandemic. However, the RLR role in innate immune response to SARS-CoV-2 has not been fully elucidated. Here, we studied the roles of RLR in cytokine expression responding to SARS-CoV-2 and found that not only MDA5 but also RIG-I are involved in innate immune responses in some types of human cells. Transfection of total RNAs extracted from SARS-CoV-2-infected cells into epithelial cells induced IFN-β, IP-10, and Ccl5 mRNA expression. The cytokine expression was reduced by knockout of either RIG-I or MDA5, suggesting that both proteins are required for appropriate innate immune response to SARS-CoV-2. Two viral genomic RNA regions strongly induced type I IFN expression, and a 200-base fragment of viral RNA preferentially induced type I IFN in a RIG-I-dependent manner. In contrast, SARS-CoV-2 infectious particles hardly induced cytokine expression, suggesting viral escape from the host response. Viral 9b protein inhibited RIG-I and MAVS interaction, and viral 7a protein destabilized the TBK1 protein, leading to attenuated IRF-3 phosphorylation required for type I IFN expression. Our data elucidated the mechanism underlying RLR-mediated response to SARS-CoV-2 infection and viral escape from the host innate immune response.
MeSH term(s)	COVID-19/immunology ; Gene Knockdown Techniques ; HEK293 Cells ; Host-Pathogen Interactions ; Humans ; Immune Evasion ; Immunity, Innate ; Interferon Regulatory Factor-3/metabolism ; Interferon Type I/metabolism ; Interferon-Induced Helicase, IFIH1/genetics ; Interferon-Induced Helicase, IFIH1/metabolism ; Phosphorylation ; RNA, Viral/immunology ; Receptors, Retinoic Acid/genetics ; Receptors, Retinoic Acid/metabolism ; SARS-CoV-2/physiology ; Severe Acute Respiratory Syndrome/immunology ; Signal Transduction ; Viral Matrix Proteins/metabolism
Chemical Substances	IRF3 protein, human ; Interferon Regulatory Factor-3 ; Interferon Type I ; PLAAT4 protein, human ; RNA, Viral ; Receptors, Retinoic Acid ; Viral Matrix Proteins ; sars7a protein, SARS virus ; IFIH1 protein, human (EC 3.6.1.-) ; Interferon-Induced Helicase, IFIH1 (EC 3.6.4.13)
Language	English
Publishing date	2021-06-25
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2606827-8
ISSN	1664-3224 ; 1664-3224
ISSN (online)	1664-3224
ISSN	1664-3224
DOI	10.3389/fimmu.2021.700926
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Article ; Online: Attenuation of the Innate Immune Response against Viral Infection Due to ZNF598-Promoted Binding of FAT10 to RIG-I.

Wang, Guanming / Kouwaki, Takahisa / Okamoto, Masaaki / Oshiumi, Hiroyuki

Cell reports

2019 Volume 28, Issue 8, Page(s) 1961–1970.e4

Abstract: Excessive innate immune response is harmful to the host, and aberrant activation of the cytoplasmic viral RNA sensors RIG-I and MDA5 leads to autoimmune disorders. ZNF598 is an E3 ubiquitin ligase involved in the ribosome quality control pathway. It is ... ...

Abstract	Excessive innate immune response is harmful to the host, and aberrant activation of the cytoplasmic viral RNA sensors RIG-I and MDA5 leads to autoimmune disorders. ZNF598 is an E3 ubiquitin ligase involved in the ribosome quality control pathway. It is also involved in the suppression of interferon (IFN)-stimulated gene (ISG) expression; however, its underlying mechanism is unclear. In this study, we show that ZNF598 is a negative regulator of the RIG-I-mediated signaling pathway, and endogenous ZNF598 protein binds to RIG-I. ZNF598 ubiquitin ligase activity is dispensable for the suppression of RIG-I signaling. Instead, ZNF598 delivers a ubiquitin-like protein FAT10 to the RIG-I protein, resulting in the inhibition of RIG-I polyubiquitination, which is required for triggering downstream signaling to produce type I IFN. Moreover, ZNF598-mediated suppression is abrogated by FAT10 knockout. Our data elucidate the mechanism by which ZNF598 inhibits RIG-I-mediated innate immune response.
MeSH term(s)	Carrier Proteins/metabolism ; Cell Line ; Cytokines/metabolism ; DEAD Box Protein 58/metabolism ; Humans ; Immunity, Innate ; Protein Binding ; Receptors, Immunologic ; Signal Transduction ; Ubiquitin/metabolism ; Ubiquitination ; Ubiquitins/metabolism ; Virus Diseases/immunology
Chemical Substances	Carrier Proteins ; Cytokines ; Receptors, Immunologic ; UBD protein, human ; Ubiquitin ; Ubiquitins ; ZNF598 protein, human ; RIGI protein, human (EC 3.6.1.-) ; DEAD Box Protein 58 (EC 3.6.4.13)
Language	English
Publishing date	2019-08-21
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2649101-1
ISSN	2211-1247 ; 2211-1247
ISSN (online)	2211-1247
ISSN	2211-1247
DOI	10.1016/j.celrep.2019.07.081
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Article ; Online: Ubiquitin ligase RIPLET mediates polyubiquitination of RIG-I and LGP2 and regulates the innate immune responses to SARS-CoV-2 infection

Kouwaki, Takahisa / Nishimura, Tasuku / Wang, Guanming / Nakagawa, Reiko / Oshiumi, Hiroyuki

bioRxiv

Abstract: RIG-I, a cytoplasmic viral RNA sensor, is crucial for innate antiviral immune responses; however, there are controversies about the regulatory mechanism of RIG-I by several ubiquitin ligases and LGP2. This study revealed that the RIPLET ubiquitin ligase ... ...

Abstract	RIG-I, a cytoplasmic viral RNA sensor, is crucial for innate antiviral immune responses; however, there are controversies about the regulatory mechanism of RIG-I by several ubiquitin ligases and LGP2. This study revealed that the RIPLET ubiquitin ligase is a general activating factor for RIG-I signaling. In contrast, another ubiquitin ligase, TRIM25, activated RIG-I in a cell-type-specific manner. RIPLET and TRIM25 functions were modulated by accessory factors, such as ZCCH3C and NLRP12. Interestingly, we found an additional role of RIPLET in innate immune responses. RIPLET induced delayed polyubiquitination of LGP, resulting in the attenuation of excessive cytokine expression at the late phase. Moreover, RIPLET was involved in the innate immune responses against SARS-CoV-2 infection, a cause of the recent COVID-19 pandemic. Our data indicate that RIPLET fine-tunes innate immune responses via polyubiquitination of RIG-I and LGP2 against virus infection, including SARS-CoV-2.
Keywords	covid19
Language	English
Publishing date	2021-01-25
Publisher	Cold Spring Harbor Laboratory
Document type	Article ; Online
DOI	10.1101/2021.01.25.428042
Database	COVID19

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Article ; Online: Megakaryocytes in pulmonary diseases.

Huang, Di-Yun / Wang, Guan-Ming / Ke, Zhuo-Ran / Zhou, Yong / Yang, Hui-Hui / Ma, Tian-Liang / Guan, Cha-Xiang

Life sciences

2022 Volume 301, Page(s) 120602

Abstract: Megakaryocytes (MKs) are typical cellular components in the circulating blood flowing from the heart into the lungs. Physiologically, MKs function as an important regulator of platelet production and immunoregulation. However, dysfunction in MKs is ... ...

Abstract	Megakaryocytes (MKs) are typical cellular components in the circulating blood flowing from the heart into the lungs. Physiologically, MKs function as an important regulator of platelet production and immunoregulation. However, dysfunction in MKs is considered a trigger in various diseases. It has been described that the lung is an important site of platelet biogenesis from extramedullary MKs, which may play an essential role in various pulmonary diseases. With detailed studies, there are different degrees of numerical changes of MKs in coronavirus disease 2019 (COVID-19), acute respiratory distress syndrome (ARDS), chronic obstructive pulmonary disease (COPD), lung cancer, pulmonary fibrosis (PF), and other pulmonary diseases. Also, MKs inhibit or promote the development of pulmonary diseases through various pathways. Here, we summarize the current knowledge of MKs in pulmonary diseases, highlighting the physiological functions and integrated molecular mechanisms. We aim to shine new light on not only the subsequent study of MKs but also the diagnosis and treatment of pulmonary diseases.
MeSH term(s)	Blood Platelets ; COVID-19 ; Humans ; Lung ; Megakaryocytes ; Respiratory Distress Syndrome ; Thrombopoiesis
Language	English
Publishing date	2022-05-01
Publishing country	Netherlands
Document type	Journal Article ; Review
ZDB-ID	3378-9
ISSN	1879-0631 ; 0024-3205
ISSN (online)	1879-0631
ISSN	0024-3205
DOI	10.1016/j.lfs.2022.120602
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Article: Megakaryocytes in pulmonary diseases

Huang, Di-Yun / Wang, Guan-Ming / Ke, Zhuo-Ran / Zhou, Yong / Yang, Hui-Hui / Ma, Tian-Liang / Guan, Cha-Xiang

Life sciences. 2022 July 15, v. 301

2022

Abstract	Megakaryocytes (MKs) are typical cellular components in the circulating blood flowing from the heart into the lungs. Physiologically, MKs function as an important regulator of platelet production and immunoregulation. However, dysfunction in MKs is considered a trigger in various diseases. It has been described that the lung is an important site of platelet biogenesis from extramedullary MKs, which may play an essential role in various pulmonary diseases. With detailed studies, there are different degrees of numerical changes of MKs in coronavirus disease 2019 (COVID-19), acute respiratory distress syndrome (ARDS), chronic obstructive pulmonary disease (COPD), lung cancer, pulmonary fibrosis (PF), and other pulmonary diseases. Also, MKs inhibit or promote the development of pulmonary diseases through various pathways. Here, we summarize the current knowledge of MKs in pulmonary diseases, highlighting the physiological functions and integrated molecular mechanisms. We aim to shine new light on not only the subsequent study of MKs but also the diagnosis and treatment of pulmonary diseases.
Keywords	COVID-19 infection ; acute respiratory distress syndrome ; biogenesis ; blood ; heart ; immunomodulation ; lung neoplasms ; lungs ; megakaryocytes ; pulmonary fibrosis
Language	English
Dates of publication	2022-0715
Publishing place	Elsevier Inc.
Document type	Article
ZDB-ID	3378-9
ISSN	1879-0631 ; 0024-3205
ISSN (online)	1879-0631
ISSN	0024-3205
DOI	10.1016/j.lfs.2022.120602
Database	NAL-Catalogue (AGRICOLA)

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Article: Mitochondrial citrate accumulation triggers senescence of alveolar epithelial cells contributing to pulmonary fibrosis in mice.

Hong, Jie-Ru / Jin, Ling / Zhang, Chen-Yu / Zhong, Wen-Jing / Yang, Hui-Hui / Wang, Guan-Ming / Ma, Sheng-Chao / Guan, Cha-Xiang / Li, Qing / Zhou, Yong

Heliyon

2023 Volume 9, Issue 6, Page(s) e17361

Abstract: Alveolar epithelial cell (AEC) senescence is implicated in the pathogenesis of pulmonary fibrosis (PF). However, the exact mechanism underlying AEC senescence during PF remains poorly understood. Here, we reported an unrecognized mechanism for AEC ... ...

Abstract	Alveolar epithelial cell (AEC) senescence is implicated in the pathogenesis of pulmonary fibrosis (PF). However, the exact mechanism underlying AEC senescence during PF remains poorly understood. Here, we reported an unrecognized mechanism for AEC senescence during PF. We found that, in bleomycin (BLM)-induced PF mice, the expressions of isocitrate dehydrogenase 3α (Idh3α) and citrate carrier (CIC) were significantly down-regulated in the lungs, which could result in mitochondria citrate (citrate
Language	English
Publishing date	2023-06-19
Publishing country	England
Document type	Journal Article
ZDB-ID	2835763-2
ISSN	2405-8440
ISSN	2405-8440
DOI	10.1016/j.heliyon.2023.e17361
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