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LitCovid_Glycan-Motif-Structure

{"project":"LitCovid_Glycan-Motif-Structure","denotations":[{"id":"T201","span":{"begin":1371,"end":1382},"obj":"https://glytoucan.org/Structures/Glycans/G43702JT"}],"text":"For glycan interaction, HCoV-NL63 and MHV utilize heparan sulfate proteoglycans (HSPGs) as attachment enhancers [87,124]. Viruses recognize HSPGs as attachment molecules. In the spike (S) protein-deficient virions, the M protein recognizes HSPG. The S proteins generally bind to the viral cellular receptor. However, the M protein also acts as a receptor in the early step of HCoV-NL63 infection. The M membrane protein of HCoV-NL63 recognizes the attachment site of HSPGs. HCoV-NL63 M protein binds to HSPG for the initial attachment of virus to host cells and thereafter, the M and S proteins cooperate for virus entrance into the host cells [125]. HSPGs are glycosaminoglycan (GAG)-carrying proteins frequently used as a secondary receptor for viral entry. HSPGs are composed of covalent-bonded HS chains as a GAG form. The HS GAG linkage structure of tetrasaccharide exhibits GluAβ1,3GlcNAcα1,4Galβ1,3Galβ1,4Xylβ-O-serine. Glycosyltransferases involved in HS GAG synthesis include GlcAT-II (glucuronosyltransferase) and GlcNAcT-II (N-acetylglucosaminyltransferase II) for heparan sulfate synthesis (Figure 9). GAG is used as docking sites for virus interaction with the host cell surface. GAGs contain negatively charged N- and O-sulfated sugars [126]. The biosynthetic pathway and biologic roles in early embryogenic morphogenesis and vulval morphogenesis of HS and chondroitin sulfate GAG have been elucidated in Caenorhabditis elegans [127]. The negative charges mediate the interaction of GAGs and their ligands through electrostatic forces. Interaction of HSPG with ligands potentiates many virus infectious cycles. For examples, adeno-associated virus, human T cell lymphotropic virus type 1, human papilloma virus 16, herpes viruses, hepatitis B and C viruses, Kaposi’s sarcoma-associated herpesvirus, human papilloma viruses and Merkel cell polyoma virus recognize the HSPGs [128,129]. HSPGs increase virulence upon interaction with viral factors required for viral attachment and replication."}

LitCovid-PD-FMA-UBERON

LitCovid-PD-UBERON

{"project":"LitCovid-PD-UBERON","denotations":[{"id":"T32","span":{"begin":448,"end":463},"obj":"Body_part"}],"attributes":[{"id":"A32","pred":"uberon_id","subj":"T32","obj":"http://purl.obolibrary.org/obo/UBERON_4200047"}],"text":"For glycan interaction, HCoV-NL63 and MHV utilize heparan sulfate proteoglycans (HSPGs) as attachment enhancers [87,124]. Viruses recognize HSPGs as attachment molecules. In the spike (S) protein-deficient virions, the M protein recognizes HSPG. The S proteins generally bind to the viral cellular receptor. However, the M protein also acts as a receptor in the early step of HCoV-NL63 infection. The M membrane protein of HCoV-NL63 recognizes the attachment site of HSPGs. HCoV-NL63 M protein binds to HSPG for the initial attachment of virus to host cells and thereafter, the M and S proteins cooperate for virus entrance into the host cells [125]. HSPGs are glycosaminoglycan (GAG)-carrying proteins frequently used as a secondary receptor for viral entry. HSPGs are composed of covalent-bonded HS chains as a GAG form. The HS GAG linkage structure of tetrasaccharide exhibits GluAβ1,3GlcNAcα1,4Galβ1,3Galβ1,4Xylβ-O-serine. Glycosyltransferases involved in HS GAG synthesis include GlcAT-II (glucuronosyltransferase) and GlcNAcT-II (N-acetylglucosaminyltransferase II) for heparan sulfate synthesis (Figure 9). GAG is used as docking sites for virus interaction with the host cell surface. GAGs contain negatively charged N- and O-sulfated sugars [126]. The biosynthetic pathway and biologic roles in early embryogenic morphogenesis and vulval morphogenesis of HS and chondroitin sulfate GAG have been elucidated in Caenorhabditis elegans [127]. The negative charges mediate the interaction of GAGs and their ligands through electrostatic forces. Interaction of HSPG with ligands potentiates many virus infectious cycles. For examples, adeno-associated virus, human T cell lymphotropic virus type 1, human papilloma virus 16, herpes viruses, hepatitis B and C viruses, Kaposi’s sarcoma-associated herpesvirus, human papilloma viruses and Merkel cell polyoma virus recognize the HSPGs [128,129]. HSPGs increase virulence upon interaction with viral factors required for viral attachment and replication."}

LitCovid-PD-MONDO

{"project":"LitCovid-PD-MONDO","denotations":[{"id":"T245","span":{"begin":386,"end":395},"obj":"Disease"},{"id":"T246","span":{"begin":1606,"end":1616},"obj":"Disease"},{"id":"T247","span":{"begin":1709,"end":1718},"obj":"Disease"},{"id":"T248","span":{"begin":1745,"end":1756},"obj":"Disease"},{"id":"T249","span":{"begin":1745,"end":1754},"obj":"Disease"},{"id":"T250","span":{"begin":1772,"end":1788},"obj":"Disease"},{"id":"T251","span":{"begin":1781,"end":1788},"obj":"Disease"},{"id":"T252","span":{"begin":1819,"end":1828},"obj":"Disease"}],"attributes":[{"id":"A245","pred":"mondo_id","subj":"T245","obj":"http://purl.obolibrary.org/obo/MONDO_0005550"},{"id":"A246","pred":"mondo_id","subj":"T246","obj":"http://purl.obolibrary.org/obo/MONDO_0005550"},{"id":"A247","pred":"mondo_id","subj":"T247","obj":"http://purl.obolibrary.org/obo/MONDO_0002363"},{"id":"A248","pred":"mondo_id","subj":"T248","obj":"http://purl.obolibrary.org/obo/MONDO_0005344"},{"id":"A249","pred":"mondo_id","subj":"T249","obj":"http://purl.obolibrary.org/obo/MONDO_0002251"},{"id":"A250","pred":"mondo_id","subj":"T250","obj":"http://purl.obolibrary.org/obo/MONDO_0005055"},{"id":"A251","pred":"mondo_id","subj":"T251","obj":"http://purl.obolibrary.org/obo/MONDO_0005089"},{"id":"A252","pred":"mondo_id","subj":"T252","obj":"http://purl.obolibrary.org/obo/MONDO_0002363"}],"text":"For glycan interaction, HCoV-NL63 and MHV utilize heparan sulfate proteoglycans (HSPGs) as attachment enhancers [87,124]. Viruses recognize HSPGs as attachment molecules. In the spike (S) protein-deficient virions, the M protein recognizes HSPG. The S proteins generally bind to the viral cellular receptor. However, the M protein also acts as a receptor in the early step of HCoV-NL63 infection. The M membrane protein of HCoV-NL63 recognizes the attachment site of HSPGs. HCoV-NL63 M protein binds to HSPG for the initial attachment of virus to host cells and thereafter, the M and S proteins cooperate for virus entrance into the host cells [125]. HSPGs are glycosaminoglycan (GAG)-carrying proteins frequently used as a secondary receptor for viral entry. HSPGs are composed of covalent-bonded HS chains as a GAG form. The HS GAG linkage structure of tetrasaccharide exhibits GluAβ1,3GlcNAcα1,4Galβ1,3Galβ1,4Xylβ-O-serine. Glycosyltransferases involved in HS GAG synthesis include GlcAT-II (glucuronosyltransferase) and GlcNAcT-II (N-acetylglucosaminyltransferase II) for heparan sulfate synthesis (Figure 9). GAG is used as docking sites for virus interaction with the host cell surface. GAGs contain negatively charged N- and O-sulfated sugars [126]. The biosynthetic pathway and biologic roles in early embryogenic morphogenesis and vulval morphogenesis of HS and chondroitin sulfate GAG have been elucidated in Caenorhabditis elegans [127]. The negative charges mediate the interaction of GAGs and their ligands through electrostatic forces. Interaction of HSPG with ligands potentiates many virus infectious cycles. For examples, adeno-associated virus, human T cell lymphotropic virus type 1, human papilloma virus 16, herpes viruses, hepatitis B and C viruses, Kaposi’s sarcoma-associated herpesvirus, human papilloma viruses and Merkel cell polyoma virus recognize the HSPGs [128,129]. HSPGs increase virulence upon interaction with viral factors required for viral attachment and replication."}

LitCovid-PD-CLO

LitCovid-PD-CHEBI

LitCovid-PD-GO-BP

{"project":"LitCovid-PD-GO-BP","denotations":[{"id":"T102","span":{"begin":967,"end":976},"obj":"http://purl.obolibrary.org/obo/GO_0009058"},{"id":"T103","span":{"begin":1092,"end":1101},"obj":"http://purl.obolibrary.org/obo/GO_0009058"},{"id":"T104","span":{"begin":1153,"end":1178},"obj":"http://purl.obolibrary.org/obo/GO_0051701"},{"id":"T105","span":{"begin":1322,"end":1335},"obj":"http://purl.obolibrary.org/obo/GO_0009653"},{"id":"T106","span":{"begin":1347,"end":1360},"obj":"http://purl.obolibrary.org/obo/GO_0009653"},{"id":"T107","span":{"begin":1913,"end":1922},"obj":"http://purl.obolibrary.org/obo/GO_0016032"},{"id":"T108","span":{"begin":1913,"end":1922},"obj":"http://purl.obolibrary.org/obo/GO_0009405"}],"text":"For glycan interaction, HCoV-NL63 and MHV utilize heparan sulfate proteoglycans (HSPGs) as attachment enhancers [87,124]. Viruses recognize HSPGs as attachment molecules. In the spike (S) protein-deficient virions, the M protein recognizes HSPG. The S proteins generally bind to the viral cellular receptor. However, the M protein also acts as a receptor in the early step of HCoV-NL63 infection. The M membrane protein of HCoV-NL63 recognizes the attachment site of HSPGs. HCoV-NL63 M protein binds to HSPG for the initial attachment of virus to host cells and thereafter, the M and S proteins cooperate for virus entrance into the host cells [125]. HSPGs are glycosaminoglycan (GAG)-carrying proteins frequently used as a secondary receptor for viral entry. HSPGs are composed of covalent-bonded HS chains as a GAG form. The HS GAG linkage structure of tetrasaccharide exhibits GluAβ1,3GlcNAcα1,4Galβ1,3Galβ1,4Xylβ-O-serine. Glycosyltransferases involved in HS GAG synthesis include GlcAT-II (glucuronosyltransferase) and GlcNAcT-II (N-acetylglucosaminyltransferase II) for heparan sulfate synthesis (Figure 9). GAG is used as docking sites for virus interaction with the host cell surface. GAGs contain negatively charged N- and O-sulfated sugars [126]. The biosynthetic pathway and biologic roles in early embryogenic morphogenesis and vulval morphogenesis of HS and chondroitin sulfate GAG have been elucidated in Caenorhabditis elegans [127]. The negative charges mediate the interaction of GAGs and their ligands through electrostatic forces. Interaction of HSPG with ligands potentiates many virus infectious cycles. For examples, adeno-associated virus, human T cell lymphotropic virus type 1, human papilloma virus 16, herpes viruses, hepatitis B and C viruses, Kaposi’s sarcoma-associated herpesvirus, human papilloma viruses and Merkel cell polyoma virus recognize the HSPGs [128,129]. HSPGs increase virulence upon interaction with viral factors required for viral attachment and replication."}

LitCovid-sentences

{"project":"LitCovid-sentences","denotations":[{"id":"T599","span":{"begin":0,"end":121},"obj":"Sentence"},{"id":"T600","span":{"begin":122,"end":170},"obj":"Sentence"},{"id":"T601","span":{"begin":171,"end":245},"obj":"Sentence"},{"id":"T602","span":{"begin":246,"end":307},"obj":"Sentence"},{"id":"T603","span":{"begin":308,"end":396},"obj":"Sentence"},{"id":"T604","span":{"begin":397,"end":473},"obj":"Sentence"},{"id":"T605","span":{"begin":474,"end":650},"obj":"Sentence"},{"id":"T606","span":{"begin":651,"end":759},"obj":"Sentence"},{"id":"T607","span":{"begin":760,"end":822},"obj":"Sentence"},{"id":"T608","span":{"begin":823,"end":926},"obj":"Sentence"},{"id":"T609","span":{"begin":927,"end":1113},"obj":"Sentence"},{"id":"T610","span":{"begin":1114,"end":1192},"obj":"Sentence"},{"id":"T611","span":{"begin":1193,"end":1256},"obj":"Sentence"},{"id":"T612","span":{"begin":1257,"end":1448},"obj":"Sentence"},{"id":"T613","span":{"begin":1449,"end":1549},"obj":"Sentence"},{"id":"T614","span":{"begin":1550,"end":1624},"obj":"Sentence"},{"id":"T615","span":{"begin":1625,"end":1897},"obj":"Sentence"},{"id":"T616","span":{"begin":1898,"end":2005},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"For glycan interaction, HCoV-NL63 and MHV utilize heparan sulfate proteoglycans (HSPGs) as attachment enhancers [87,124]. Viruses recognize HSPGs as attachment molecules. In the spike (S) protein-deficient virions, the M protein recognizes HSPG. The S proteins generally bind to the viral cellular receptor. However, the M protein also acts as a receptor in the early step of HCoV-NL63 infection. The M membrane protein of HCoV-NL63 recognizes the attachment site of HSPGs. HCoV-NL63 M protein binds to HSPG for the initial attachment of virus to host cells and thereafter, the M and S proteins cooperate for virus entrance into the host cells [125]. HSPGs are glycosaminoglycan (GAG)-carrying proteins frequently used as a secondary receptor for viral entry. HSPGs are composed of covalent-bonded HS chains as a GAG form. The HS GAG linkage structure of tetrasaccharide exhibits GluAβ1,3GlcNAcα1,4Galβ1,3Galβ1,4Xylβ-O-serine. Glycosyltransferases involved in HS GAG synthesis include GlcAT-II (glucuronosyltransferase) and GlcNAcT-II (N-acetylglucosaminyltransferase II) for heparan sulfate synthesis (Figure 9). GAG is used as docking sites for virus interaction with the host cell surface. GAGs contain negatively charged N- and O-sulfated sugars [126]. The biosynthetic pathway and biologic roles in early embryogenic morphogenesis and vulval morphogenesis of HS and chondroitin sulfate GAG have been elucidated in Caenorhabditis elegans [127]. The negative charges mediate the interaction of GAGs and their ligands through electrostatic forces. Interaction of HSPG with ligands potentiates many virus infectious cycles. For examples, adeno-associated virus, human T cell lymphotropic virus type 1, human papilloma virus 16, herpes viruses, hepatitis B and C viruses, Kaposi’s sarcoma-associated herpesvirus, human papilloma viruses and Merkel cell polyoma virus recognize the HSPGs [128,129]. HSPGs increase virulence upon interaction with viral factors required for viral attachment and replication."}

LitCovid-PD-GlycoEpitope

{"project":"LitCovid-PD-GlycoEpitope","denotations":[{"id":"T7","span":{"begin":50,"end":65},"obj":"GlycoEpitope"},{"id":"T8","span":{"begin":798,"end":800},"obj":"GlycoEpitope"},{"id":"T9","span":{"begin":827,"end":829},"obj":"GlycoEpitope"},{"id":"T10","span":{"begin":960,"end":962},"obj":"GlycoEpitope"},{"id":"T11","span":{"begin":1076,"end":1091},"obj":"GlycoEpitope"},{"id":"T12","span":{"begin":1364,"end":1366},"obj":"GlycoEpitope"},{"id":"T13","span":{"begin":1371,"end":1382},"obj":"GlycoEpitope"}],"attributes":[{"id":"A7","pred":"glyco_epitope_db_id","subj":"T7","obj":"http://www.glycoepitope.jp/epitopes/EP0086"},{"id":"A8","pred":"glyco_epitope_db_id","subj":"T8","obj":"http://www.glycoepitope.jp/epitopes/EP0086"},{"id":"A9","pred":"glyco_epitope_db_id","subj":"T9","obj":"http://www.glycoepitope.jp/epitopes/EP0086"},{"id":"A10","pred":"glyco_epitope_db_id","subj":"T10","obj":"http://www.glycoepitope.jp/epitopes/EP0086"},{"id":"A11","pred":"glyco_epitope_db_id","subj":"T11","obj":"http://www.glycoepitope.jp/epitopes/EP0086"},{"id":"A12","pred":"glyco_epitope_db_id","subj":"T12","obj":"http://www.glycoepitope.jp/epitopes/EP0086"},{"id":"A13","pred":"glyco_epitope_db_id","subj":"T13","obj":"http://www.glycoepitope.jp/epitopes/EP0081"}],"text":"For glycan interaction, HCoV-NL63 and MHV utilize heparan sulfate proteoglycans (HSPGs) as attachment enhancers [87,124]. Viruses recognize HSPGs as attachment molecules. In the spike (S) protein-deficient virions, the M protein recognizes HSPG. The S proteins generally bind to the viral cellular receptor. However, the M protein also acts as a receptor in the early step of HCoV-NL63 infection. The M membrane protein of HCoV-NL63 recognizes the attachment site of HSPGs. HCoV-NL63 M protein binds to HSPG for the initial attachment of virus to host cells and thereafter, the M and S proteins cooperate for virus entrance into the host cells [125]. HSPGs are glycosaminoglycan (GAG)-carrying proteins frequently used as a secondary receptor for viral entry. HSPGs are composed of covalent-bonded HS chains as a GAG form. The HS GAG linkage structure of tetrasaccharide exhibits GluAβ1,3GlcNAcα1,4Galβ1,3Galβ1,4Xylβ-O-serine. Glycosyltransferases involved in HS GAG synthesis include GlcAT-II (glucuronosyltransferase) and GlcNAcT-II (N-acetylglucosaminyltransferase II) for heparan sulfate synthesis (Figure 9). GAG is used as docking sites for virus interaction with the host cell surface. GAGs contain negatively charged N- and O-sulfated sugars [126]. The biosynthetic pathway and biologic roles in early embryogenic morphogenesis and vulval morphogenesis of HS and chondroitin sulfate GAG have been elucidated in Caenorhabditis elegans [127]. The negative charges mediate the interaction of GAGs and their ligands through electrostatic forces. Interaction of HSPG with ligands potentiates many virus infectious cycles. For examples, adeno-associated virus, human T cell lymphotropic virus type 1, human papilloma virus 16, herpes viruses, hepatitis B and C viruses, Kaposi’s sarcoma-associated herpesvirus, human papilloma viruses and Merkel cell polyoma virus recognize the HSPGs [128,129]. HSPGs increase virulence upon interaction with viral factors required for viral attachment and replication."}

2_test

{"project":"2_test","denotations":[{"id":"32604730-25187545-51944087","span":{"begin":113,"end":115},"obj":"25187545"},{"id":"32604730-17692355-51944088","span":{"begin":116,"end":119},"obj":"17692355"},{"id":"32604730-31315999-51944089","span":{"begin":645,"end":648},"obj":"31315999"},{"id":"32604730-12369092-51944090","span":{"begin":1251,"end":1254},"obj":"12369092"},{"id":"32604730-12761549-51944091","span":{"begin":1443,"end":1446},"obj":"12761549"},{"id":"32604730-11507222-51944092","span":{"begin":1888,"end":1891},"obj":"11507222"},{"id":"32604730-11518721-51944093","span":{"begin":1892,"end":1895},"obj":"11518721"},{"id":"T42843","span":{"begin":113,"end":115},"obj":"25187545"},{"id":"T53854","span":{"begin":116,"end":119},"obj":"17692355"},{"id":"T94580","span":{"begin":645,"end":648},"obj":"31315999"},{"id":"T83893","span":{"begin":1251,"end":1254},"obj":"12369092"},{"id":"T73934","span":{"begin":1443,"end":1446},"obj":"12761549"},{"id":"T91960","span":{"begin":1888,"end":1891},"obj":"11507222"},{"id":"T65288","span":{"begin":1892,"end":1895},"obj":"11518721"}],"text":"For glycan interaction, HCoV-NL63 and MHV utilize heparan sulfate proteoglycans (HSPGs) as attachment enhancers [87,124]. Viruses recognize HSPGs as attachment molecules. In the spike (S) protein-deficient virions, the M protein recognizes HSPG. The S proteins generally bind to the viral cellular receptor. However, the M protein also acts as a receptor in the early step of HCoV-NL63 infection. The M membrane protein of HCoV-NL63 recognizes the attachment site of HSPGs. HCoV-NL63 M protein binds to HSPG for the initial attachment of virus to host cells and thereafter, the M and S proteins cooperate for virus entrance into the host cells [125]. HSPGs are glycosaminoglycan (GAG)-carrying proteins frequently used as a secondary receptor for viral entry. HSPGs are composed of covalent-bonded HS chains as a GAG form. The HS GAG linkage structure of tetrasaccharide exhibits GluAβ1,3GlcNAcα1,4Galβ1,3Galβ1,4Xylβ-O-serine. Glycosyltransferases involved in HS GAG synthesis include GlcAT-II (glucuronosyltransferase) and GlcNAcT-II (N-acetylglucosaminyltransferase II) for heparan sulfate synthesis (Figure 9). GAG is used as docking sites for virus interaction with the host cell surface. GAGs contain negatively charged N- and O-sulfated sugars [126]. The biosynthetic pathway and biologic roles in early embryogenic morphogenesis and vulval morphogenesis of HS and chondroitin sulfate GAG have been elucidated in Caenorhabditis elegans [127]. The negative charges mediate the interaction of GAGs and their ligands through electrostatic forces. Interaction of HSPG with ligands potentiates many virus infectious cycles. For examples, adeno-associated virus, human T cell lymphotropic virus type 1, human papilloma virus 16, herpes viruses, hepatitis B and C viruses, Kaposi’s sarcoma-associated herpesvirus, human papilloma viruses and Merkel cell polyoma virus recognize the HSPGs [128,129]. HSPGs increase virulence upon interaction with viral factors required for viral attachment and replication."}

LitCovid-PD-HP

{"project":"LitCovid-PD-HP","denotations":[{"id":"T20","span":{"begin":1709,"end":1718},"obj":"Phenotype"},{"id":"T21","span":{"begin":1745,"end":1754},"obj":"Phenotype"},{"id":"T22","span":{"begin":1772,"end":1788},"obj":"Phenotype"},{"id":"T23","span":{"begin":1819,"end":1828},"obj":"Phenotype"}],"attributes":[{"id":"A20","pred":"hp_id","subj":"T20","obj":"http://purl.obolibrary.org/obo/HP_0012740"},{"id":"A21","pred":"hp_id","subj":"T21","obj":"http://purl.obolibrary.org/obo/HP_0012115"},{"id":"A22","pred":"hp_id","subj":"T22","obj":"http://purl.obolibrary.org/obo/HP_0100726"},{"id":"A23","pred":"hp_id","subj":"T23","obj":"http://purl.obolibrary.org/obo/HP_0012740"}],"text":"For glycan interaction, HCoV-NL63 and MHV utilize heparan sulfate proteoglycans (HSPGs) as attachment enhancers [87,124]. Viruses recognize HSPGs as attachment molecules. In the spike (S) protein-deficient virions, the M protein recognizes HSPG. The S proteins generally bind to the viral cellular receptor. However, the M protein also acts as a receptor in the early step of HCoV-NL63 infection. The M membrane protein of HCoV-NL63 recognizes the attachment site of HSPGs. HCoV-NL63 M protein binds to HSPG for the initial attachment of virus to host cells and thereafter, the M and S proteins cooperate for virus entrance into the host cells [125]. HSPGs are glycosaminoglycan (GAG)-carrying proteins frequently used as a secondary receptor for viral entry. HSPGs are composed of covalent-bonded HS chains as a GAG form. The HS GAG linkage structure of tetrasaccharide exhibits GluAβ1,3GlcNAcα1,4Galβ1,3Galβ1,4Xylβ-O-serine. Glycosyltransferases involved in HS GAG synthesis include GlcAT-II (glucuronosyltransferase) and GlcNAcT-II (N-acetylglucosaminyltransferase II) for heparan sulfate synthesis (Figure 9). GAG is used as docking sites for virus interaction with the host cell surface. GAGs contain negatively charged N- and O-sulfated sugars [126]. The biosynthetic pathway and biologic roles in early embryogenic morphogenesis and vulval morphogenesis of HS and chondroitin sulfate GAG have been elucidated in Caenorhabditis elegans [127]. The negative charges mediate the interaction of GAGs and their ligands through electrostatic forces. Interaction of HSPG with ligands potentiates many virus infectious cycles. For examples, adeno-associated virus, human T cell lymphotropic virus type 1, human papilloma virus 16, herpes viruses, hepatitis B and C viruses, Kaposi’s sarcoma-associated herpesvirus, human papilloma viruses and Merkel cell polyoma virus recognize the HSPGs [128,129]. HSPGs increase virulence upon interaction with viral factors required for viral attachment and replication."}

PMC:7352545 / 62180-64185 JSONTXT

Annnotations TAB JSON ListView MergeView

PMC:7352545 / 62180-64185 JSON TXT