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  1. AU=Narayanan Naveen
  2. AU=Azam Faizul
  3. AU="Özdog˘ru, Asil Ali"
  4. AU="Emami, Hajar"
  5. AU="Cimino, R."
  6. AU="Judith R. Stabel"
  7. AU="Takeuchi, Kazuto"
  8. AU="Mirzaei, Samira"
  9. AU="Carolina Salgado"
  10. AU="Mate, Sebastian"
  11. AU="Hou, Tian-Yang Liu"
  12. AU=Nino Gustavo
  13. AU="Lydon, Myra"
  14. AU="Jain, Nibha"
  15. AU="David A Schwartz"
  16. AU="Swart, Jonathan"
  17. AU="Karol, Agnieszka"
  18. AU="Reilly, Brittni"
  19. AU="Arfaatabar, Maryam"
  20. AU="Kumar Pandey, Anand"

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  1. Artikel ; Online: Half-turned truncal switch operation for dextro-transposition of the great arteries with ventricular septal defect and left ventricular outflow tract obstruction and an abnormal coronary pattern.

    Srinivasan, Naveen / Chandran, Ranjith / Narayanan, Jahnavi / Sasikumar, Divya Kadavanoor / Raju, Vijayakumar

    Multimedia manual of cardiothoracic surgery : MMCTS

    2024  Band 2024

    Abstract: We describe a surgical technique for a half-turned truncal switch operation in a 5-year-old child with dextro-transposition of the great arteries (D-TGA), a ventricular septal defect, a left ventricular outflow tract obstruction and a complex coronary ... ...

    Abstract We describe a surgical technique for a half-turned truncal switch operation in a 5-year-old child with dextro-transposition of the great arteries (D-TGA), a ventricular septal defect, a left ventricular outflow tract obstruction and a complex coronary pattern. The benefit of the half-turned truncal switch is the creation of haemodynamically superior biventricular outflow tracts and the maximal use of an autologous pulmonary valve in the right ventricular outflow tract, thereby avoiding the right ventricular-pulmonary artery conduit.
    Mesh-Begriff(e) Humans ; Transposition of Great Vessels/surgery ; Ventricular Outflow Obstruction/surgery ; Heart Septal Defects, Ventricular/surgery ; Child, Preschool ; Arterial Switch Operation/methods ; Male ; Abnormalities, Multiple/surgery ; Cardiac Surgical Procedures/methods ; Ventricular Outflow Obstruction, Left
    Sprache Englisch
    Erscheinungsdatum 2024-05-16
    Erscheinungsland England
    Dokumenttyp Video-Audio Media ; Case Reports
    ZDB-ID 2280156-X
    ISSN 1813-9175 ; 1813-9175
    ISSN (online) 1813-9175
    ISSN 1813-9175
    DOI 10.1510/mmcts.2024.037
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  2. Artikel ; Online: A mechanistic insight on how Compromised Hydrolysis of Triacylglycerol 7 (CHT7) restrains the involvement of it's CXC domain from quiescence repression.

    Chauhan, Manisha / Arshi, Syeda Amna / Narayanan, Naveen / Arfin, Haseeb Ul / Sharma, Amit

    International journal of biological macromolecules

    2024  Band 265, Heft Pt 1, Seite(n) 130844

    Abstract: CHT7 is a regulator of quiescence repression in Chlamydomonas reinhardtii. Initially, CHT7's repression activity was thought to be managed by its DNA-binding CXC domain. Later, it was found that the CHT7-CXC domain is dispensable for CHT7's activities. ... ...

    Abstract CHT7 is a regulator of quiescence repression in Chlamydomonas reinhardtii. Initially, CHT7's repression activity was thought to be managed by its DNA-binding CXC domain. Later, it was found that the CHT7-CXC domain is dispensable for CHT7's activities. Rather, CHT7's predicted protein domains were proposed to be involved in regulation activities by binding to other repressors in the cell. Yet, it remains unclear why and how CHT7 refrains its CXC domain from participating in any transcriptional activities. The question becomes more intriguing, since CXC binding regions are available in promoter regions of some of the misregulated genes in CHT7 mutant (cht7). Through biophysical experiments and molecular dynamics approaches, we studied the DNA recognition behavior of CHT7-CXC. The results indicate that this domain possesses sequence selectivity due to the differential binding abilities of its subdomains. Further, to understand if the case is that CXC loses its DNA binding capabilities in the vicinity of other repressors, we examined CHT7-CXC's DNA binding stability under the spatial constraint conditions created through fusing CHT7-CXC with AsLOV2. The results show limited ability of CHT7-CXC to withstand steric forces and provide insights to why and how algal cells may hold back CHT7-CXC's indulgence in quiescence repression. CLASSIFICATIONS: Biological Sciences, Biophysics and Computational Biology.
    Mesh-Begriff(e) Triglycerides ; Hydrolysis ; Transcription Factors/genetics ; DNA-Binding Proteins/metabolism ; DNA ; Transcription, Genetic
    Chemische Substanzen Triglycerides ; Transcription Factors ; DNA-Binding Proteins ; DNA (9007-49-2)
    Sprache Englisch
    Erscheinungsdatum 2024-03-13
    Erscheinungsland Netherlands
    Dokumenttyp Journal Article
    ZDB-ID 282732-3
    ISSN 1879-0003 ; 0141-8130
    ISSN (online) 1879-0003
    ISSN 0141-8130
    DOI 10.1016/j.ijbiomac.2024.130844
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  3. Artikel: Ritonavir may inhibit exoribonuclease activity of nsp14 from the SARS-CoV-2 virus and potentiate the activity of chain terminating drugs

    Narayanan, Naveen / Nair, Deepak T

    International journal of biological macromolecules. 2021 Jan. 31, v. 168

    2021  

    Abstract: SARS-CoV-2is the causative agent for the ongoing COVID19 pandemic, and this virus belongs to the Coronaviridae family. The nsp14 protein of SARS-CoV-2 houses a 3′ to 5′ exoribonuclease activity responsible for removing mismatches that arise during genome ...

    Abstract SARS-CoV-2is the causative agent for the ongoing COVID19 pandemic, and this virus belongs to the Coronaviridae family. The nsp14 protein of SARS-CoV-2 houses a 3′ to 5′ exoribonuclease activity responsible for removing mismatches that arise during genome duplication. A homology model of nsp10-nsp14 complex was used to carry out in silico screening to identify molecules among natural products, or FDA approved drugs that can potentially inhibit the activity of nsp14. This exercise showed that ritonavir might bind to the exoribonuclease active site of the nsp14 protein. A model of the SARS-CoV-2-nsp10-nsp14 complex bound to substrate RNA showed that the ritonavir binding site overlaps with that of the 3′ nucleotide of substrate RNA. A comparison of the calculated energies of binding for RNA and ritonavir suggested that the drug may bind to the active site of nsp14 with significant affinity. It is, therefore, possible that ritonavir may prevent association with substrate RNA and thus inhibit the exoribonuclease activity of nsp14. Overall, our computational studies suggest that ritonavir may serve as an effective inhibitor of the nsp14 protein. nsp14 is known to attenuate the inhibitory effect of drugs that function through premature termination of viral genome replication. Hence, ritonavir may potentiate the therapeutic properties of drugs such as remdesivir, favipiravir and ribavirin.
    Schlagwörter COVID-19 infection ; RNA ; Severe acute respiratory syndrome coronavirus 2 ; active sites ; antiretroviral agents ; binding sites ; computer simulation ; enzyme activity ; enzyme inhibition ; enzyme inhibitors ; exoribonucleases ; gene duplication ; sequence homology ; viral genome ; viral nonstructural proteins
    Sprache Englisch
    Erscheinungsverlauf 2021-0131
    Umfang p. 272-278.
    Erscheinungsort Elsevier B.V.
    Dokumenttyp Artikel
    Anmerkung golden set
    ZDB-ID 282732-3
    ISSN 1879-0003 ; 0141-8130
    ISSN (online) 1879-0003
    ISSN 0141-8130
    DOI 10.1016/j.ijbiomac.2020.12.038
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  4. Buch ; Online: Ritonavir May Inhibit Exoribonuclease Activity of Nsp14 from the SARS-CoV-2 Virus and Potentiate the Activity of Chain Terminating Drugs

    naveen narayanan / deepak nair

    2020  

    Abstract: SARS-CoV-2 is the causative agent for the ongoing COVID19 pandemic, and this virus belongs to the Coronaviridae family. The nsp14 protein of SARS-CoV-2 houses a 3’ to 5’ exoribonuclease activity responsible for removing mismatches that arise during ... ...

    Abstract SARS-CoV-2 is the causative agent for the ongoing COVID19 pandemic, and this virus belongs to the Coronaviridae family. The nsp14 protein of SARS-CoV-2 houses a 3’ to 5’ exoribonuclease activity responsible for removing mismatches that arise during genome duplication. A homology model of nsp10-nsp14 complex was used to carry out in silico screening to identify molecules among natural products, or FDA approved drugs that can potentially inhibit the activity of nsp14. This exercise showed that ritonavir might bind to the exoribonuclease active site of the nsp14 protein. A model of the SCV2-nsp10-nsp14 complex bound to substrate RNA showed that the ritonavir binding site overlaps with that of the 3’ nucleotide of substrate RNA. A comparison of the calculated energies of binding for RNA and ritonavir suggested that the drug may bind to the active site of nsp14 with significant affinity. It is, therefore, possible that ritonavir may prevent association with substrate RNA and thus inhibit the exoribonuclease activity of nsp14. Overall, our computational studies suggest that ritonavir may serve as an effective inhibitor of the nsp14 protein. nsp14 is known to attenuate the inhibitory effect of drugs that function through premature termination of viral genome replication. Hence, ritonavir may potentiate the therapeutic properties of drugs such as remdesivir, favipiravir and ribavirin.
    Schlagwörter Biochemistry ; Bioinformatics and Computational Biology ; nsp14 ; exoribonuclease ; SARS-CoV-2 ; inhibitor ; ritonavir ; covid19
    Erscheinungsdatum 2020-05-13T05:42:40Z
    Dokumenttyp Buch ; Online
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  5. Artikel ; Online: Vitamin B12 may inhibit RNA-dependent-RNA polymerase activity of nsp12 from the SARS-CoV-2 virus.

    Narayanan, Naveen / Nair, Deepak T

    IUBMB life

    2020  Band 72, Heft 10, Seite(n) 2112–2120

    Abstract: SARS-CoV-2 is the causative agent for the ongoing COVID19 pandemic, and this virus belongs to the Coronaviridae family. Like other members of this family, the virus possesses a positive-sense single-stranded RNA genome. The genome encodes for the nsp12 ... ...

    Abstract SARS-CoV-2 is the causative agent for the ongoing COVID19 pandemic, and this virus belongs to the Coronaviridae family. Like other members of this family, the virus possesses a positive-sense single-stranded RNA genome. The genome encodes for the nsp12 protein, which houses the RNA-dependent-RNA polymerase (RdRP) activity responsible for the replication of the viral genome. A homology model of nsp12 was prepared using the structure of the SARS nsp12 (6NUR) as a model. The model was used to carry out in silico screening to identify molecules among natural products, or Food and Drug Administration-approved drugs that can potentially inhibit the activity of nsp12. This exercise showed that vitamin B12 (methylcobalamin) may bind to the active site of the nsp12 protein. A model of the nsp12 in complex with substrate RNA and incoming NTP showed that vitamin B12 binding site overlaps with that of the incoming nucleotide. A comparison of the calculated energies of binding for RNA plus NTP and methylcobalamin suggested that the vitamin may bind to the active site of nsp12 with significant affinity. It is, therefore, possible that methylcobalamin binding may prevent association with RNA and NTP and thus inhibit the RdRP activity of nsp12. Overall, our computational studies suggest that methylcobalamin form of vitamin B12 may serve as an effective inhibitor of the nsp12 protein.
    Mesh-Begriff(e) Amino Acid Sequence ; Antiviral Agents/chemistry ; Antiviral Agents/pharmacology ; Binding Sites ; Coronavirus RNA-Dependent RNA Polymerase/antagonists & inhibitors ; Coronavirus RNA-Dependent RNA Polymerase/chemistry ; Coronavirus RNA-Dependent RNA Polymerase/genetics ; Coronavirus RNA-Dependent RNA Polymerase/metabolism ; Genome, Viral ; High-Throughput Screening Assays ; Molecular Docking Simulation ; Molecular Dynamics Simulation ; Prescription Drugs/chemistry ; Prescription Drugs/pharmacology ; Protein Binding ; Protein Conformation, alpha-Helical ; Protein Conformation, beta-Strand ; Protein Interaction Domains and Motifs ; SARS-CoV-2/drug effects ; SARS-CoV-2/enzymology ; SARS-CoV-2/genetics ; Sequence Alignment ; Sequence Homology, Amino Acid ; Substrate Specificity ; Thermodynamics ; User-Computer Interface ; Vitamin B 12/chemistry ; Vitamin B 12/pharmacology
    Chemische Substanzen Antiviral Agents ; Prescription Drugs ; Coronavirus RNA-Dependent RNA Polymerase (EC 2.7.7.48) ; NSP12 protein, SARS-CoV-2 (EC 2.7.7.48) ; Vitamin B 12 (P6YC3EG204)
    Schlagwörter covid19
    Sprache Englisch
    Erscheinungsdatum 2020-08-18
    Erscheinungsland England
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1492141-8
    ISSN 1521-6551 ; 1521-6543
    ISSN (online) 1521-6551
    ISSN 1521-6543
    DOI 10.1002/iub.2359
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  6. Artikel ; Online: Ritonavir may inhibit exoribonuclease activity of nsp14 from the SARS-CoV-2 virus and potentiate the activity of chain terminating drugs.

    Narayanan, Naveen / Nair, Deepak T

    International journal of biological macromolecules

    2020  Band 168, Seite(n) 272–278

    Abstract: SARS-CoV-2is the causative agent for the ongoing COVID19 pandemic, and this virus belongs to the Coronaviridae family. The nsp14 protein of SARS-CoV-2 houses a 3' to 5' exoribonuclease activity responsible for removing mismatches that arise during genome ...

    Abstract SARS-CoV-2is the causative agent for the ongoing COVID19 pandemic, and this virus belongs to the Coronaviridae family. The nsp14 protein of SARS-CoV-2 houses a 3' to 5' exoribonuclease activity responsible for removing mismatches that arise during genome duplication. A homology model of nsp10-nsp14 complex was used to carry out in silico screening to identify molecules among natural products, or FDA approved drugs that can potentially inhibit the activity of nsp14. This exercise showed that ritonavir might bind to the exoribonuclease active site of the nsp14 protein. A model of the SARS-CoV-2-nsp10-nsp14 complex bound to substrate RNA showed that the ritonavir binding site overlaps with that of the 3' nucleotide of substrate RNA. A comparison of the calculated energies of binding for RNA and ritonavir suggested that the drug may bind to the active site of nsp14 with significant affinity. It is, therefore, possible that ritonavir may prevent association with substrate RNA and thus inhibit the exoribonuclease activity of nsp14. Overall, our computational studies suggest that ritonavir may serve as an effective inhibitor of the nsp14 protein. nsp14 is known to attenuate the inhibitory effect of drugs that function through premature termination of viral genome replication. Hence, ritonavir may potentiate the therapeutic properties of drugs such as remdesivir, favipiravir and ribavirin.
    Mesh-Begriff(e) Amino Acid Sequence ; Antiviral Agents/administration & dosage ; Antiviral Agents/chemistry ; Antiviral Agents/pharmacology ; COVID-19/drug therapy ; COVID-19/virology ; Catalytic Domain ; Computer Simulation ; Drug Evaluation, Preclinical ; Drug Synergism ; Drug Therapy, Combination ; Exoribonucleases/antagonists & inhibitors ; Exoribonucleases/chemistry ; Exoribonucleases/genetics ; Genome, Viral/drug effects ; Humans ; Molecular Dynamics Simulation ; Pandemics ; Ritonavir/administration & dosage ; Ritonavir/chemistry ; Ritonavir/pharmacology ; SARS-CoV-2/drug effects ; SARS-CoV-2/genetics ; SARS-CoV-2/physiology ; Viral Nonstructural Proteins/antagonists & inhibitors ; Viral Nonstructural Proteins/chemistry ; Viral Nonstructural Proteins/genetics ; Virus Replication/drug effects
    Chemische Substanzen Antiviral Agents ; Viral Nonstructural Proteins ; Exoribonucleases (EC 3.1.-) ; NSP14 protein, SARS-CoV-2 (EC 3.1.-) ; Ritonavir (O3J8G9O825)
    Sprache Englisch
    Erscheinungsdatum 2020-12-09
    Erscheinungsland Netherlands
    Dokumenttyp Journal Article
    ZDB-ID 282732-3
    ISSN 1879-0003 ; 0141-8130
    ISSN (online) 1879-0003
    ISSN 0141-8130
    DOI 10.1016/j.ijbiomac.2020.12.038
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  7. Artikel ; Online: Vitamin B12 may inhibit RNA‐dependent‐RNA polymerase activity of nsp12 from the SARS‐CoV ‐2 virus

    Narayanan, Naveen / Nair, Deepak T.

    IUBMB Life

    2020  Band 72, Heft 10, Seite(n) 2112–2120

    Schlagwörter Clinical Biochemistry ; Genetics ; Cell Biology ; Biochemistry ; Molecular Biology ; covid19
    Sprache Englisch
    Verlag Wiley
    Erscheinungsland us
    Dokumenttyp Artikel ; Online
    ZDB-ID 1492141-8
    ISSN 1521-6551 ; 1521-6543
    ISSN (online) 1521-6551
    ISSN 1521-6543
    DOI 10.1002/iub.2359
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  8. Buch ; Online: Ritonavir may inhibit exoribonuclease activity of nsp14 from the SARS-CoV-2 virus and potentiate the activity of chain terminating drugs

    narayanan, naveen / nair, deepak t

    2020  

    Abstract: SARS-CoV-2 is the causative agent for the ongoing COVID19 pandemic, and this virus belongs to the Coronaviridae family. The nsp14 protein of SARS-CoV-2 houses a 3’ to 5’exoribonuclease activity responsible for removing mismatches that arise during genome ...

    Abstract SARS-CoV-2 is the causative agent for the ongoing COVID19 pandemic, and this virus belongs to the Coronaviridae family. The nsp14 protein of SARS-CoV-2 houses a 3’ to 5’exoribonuclease activity responsible for removing mismatches that arise during genome duplication. A homology model of nsp10-nsp14 complex was used to carry out in silico screening to identify molecules among natural products, or FDA approved drugs that can potentially inhibit the activity of nsp14. This exercise showed that ritonavir might bind to the exoribonuclease active site of the nsp14 protein. A model of the SCV2-nsp10-nsp14 complex bound to substrate RNA showed that the ritonavir binding site overlaps with that of the 3’nucleotide of substrate RNA. A comparison of the calculated energies of binding for RNA and ritonavir suggested that the drug may bind to the active site of nsp14 with significant affinity. It is, therefore, possible that ritonavir may prevent association with substrate RNA and thus inhibit the exoribonuclease activity of nsp14. Overall, our computational studies suggest that ritonavirmay serve as an effective inhibitor of the nsp14 protein. nsp14 is known to attenuate the inhibitory effect of drugs that function through premature termination of viral genome replication. Hence, ritonavir may potentiate the therapeutic properties of drugs such as remdesivir, favipiravir and ribavirin.
    Schlagwörter covid19
    Verlag Center for Open Science
    Erscheinungsland us
    Dokumenttyp Buch ; Online
    DOI 10.35543/osf.io/f5gnq
    Datenquelle BASE - Bielefeld Academic Search Engine (Lebenswissenschaftliche Auswahl)

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  9. Buch ; Online: Vitamin B12 may inhibit RNA-dependent-RNA polymerase activity of nsp12 from the COVID-19 Virus

    nair, deepak t / narayanan, naveen

    2020  

    Abstract: COVID-19 is the causative agent for the ongoing pandemic, and this virus belongs to the Coronaviridae family. Like other members of this family, the virus possesses a positive-sense single-stranded RNA genome. The genome encodes for the nsp12 protein, ... ...

    Abstract COVID-19 is the causative agent for the ongoing pandemic, and this virus belongs to the Coronaviridae family. Like other members of this family, the virus possesses a positive-sense single-stranded RNA genome. The genome encodes for the nsp12 protein, which houses the RNA-dependent-RNA polymerase (RdRP) activity responsible for the replication of the viral genome. A homology model of nsp12 was prepared using the structure of the SARS nsp12 (6NUR) as a model. The model was used to carry out in silico screening to identify molecules among natural products, or FDA approved drugs that can potentially inhibit the activity of nsp12. This exercise showed that vitamin B12 (methylcobalamin) may bind to the active site of the nsp12 protein. A model of the nsp12 in complex with substrate RNA and incoming NTP showed that Vitamin B12 binding site overlaps with that of the incoming nucleotide. A comparison of the calculated energies of binding for RNA plus NTP and methylcobalamin suggested that the vitamin may bind to the active site of nsp12 with significant affinity. It is, therefore, possible that methylcobalamin binding may prevent association with RNA and NTP and thus inhibit the RdRP activity of nsp12. Overall, our computational studies suggest that methylcobalamin form of vitamin B12 may serve as an effective inhibitor of the nsp12 protein.
    Schlagwörter covid19
    Verlag Center for Open Science
    Erscheinungsland us
    Dokumenttyp Buch ; Online
    DOI 10.35543/osf.io/p48fa
    Datenquelle BASE - Bielefeld Academic Search Engine (Lebenswissenschaftliche Auswahl)

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  10. Artikel ; Online: The proofreading activity of Pfprex from Plasmodium falciparum can prevent mutagenesis of the apicoplast genome by oxidized nucleotides

    Minakshi Sharma / Naveen Narayanan / Deepak T. Nair

    Scientific Reports, Vol 10, Iss 1, Pp 1-

    2020  Band 14

    Abstract: Abstract The DNA polymerase module of the Pfprex enzyme (PfpPol) is responsible for duplication of the genome of the apicoplast organelle in the malaria parasite. We show that PfpPol can misincorporate oxidized nucleotides such as 8oxodGTP opposite dA. ... ...

    Abstract Abstract The DNA polymerase module of the Pfprex enzyme (PfpPol) is responsible for duplication of the genome of the apicoplast organelle in the malaria parasite. We show that PfpPol can misincorporate oxidized nucleotides such as 8oxodGTP opposite dA. This event gives rise to transversion mutations that are known to lead to adverse physiological outcomes. The apicoplast genome is particularly vulnerable to the harmful effects of 8oxodGTP due to very high AT content (~ 87%). We show that the proofreading activity of PfpPol has the unique ability to remove the oxidized nucleotide from the primer terminus. Due to this property, the proofreading domain of PfpPol is able to prevent mutagenesis of the AT-rich apicoplast genome and neutralize the deleterious genotoxic effects of ROS generated in the apicoplast due to normal metabolic processes. The proofreading activity of the Pfprex enzyme may, therefore, represent an attractive target for therapeutic intervention. Also, a survey of DNA repair pathways shows that the observed property of Pfprex constitutes a novel form of dynamic error correction wherein the repair of promutagenic damaged nucleotides is concomitant with DNA replication.
    Schlagwörter Medicine ; R ; Science ; Q
    Thema/Rubrik (Code) 572
    Sprache Englisch
    Erscheinungsdatum 2020-07-01T00:00:00Z
    Verlag Nature Portfolio
    Dokumenttyp Artikel ; Online
    Datenquelle BASE - Bielefeld Academic Search Engine (Lebenswissenschaftliche Auswahl)

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