PMC:7795856 / 22035-23327 JSONTXT

{"project":"LitCovid-PubTator","denotations":[{"id":"385","span":{"begin":155,"end":160},"obj":"Gene"},{"id":"386","span":{"begin":165,"end":168},"obj":"Gene"},{"id":"387","span":{"begin":177,"end":180},"obj":"Gene"},{"id":"388","span":{"begin":185,"end":191},"obj":"Gene"},{"id":"389","span":{"begin":500,"end":503},"obj":"Gene"},{"id":"390","span":{"begin":1164,"end":1170},"obj":"Species"},{"id":"391","span":{"begin":1175,"end":1184},"obj":"Species"},{"id":"392","span":{"begin":637,"end":646},"obj":"Species"},{"id":"393","span":{"begin":322,"end":348},"obj":"Chemical"},{"id":"394","span":{"begin":550,"end":554},"obj":"Chemical"},{"id":"395","span":{"begin":647,"end":650},"obj":"Chemical"},{"id":"396","span":{"begin":721,"end":724},"obj":"Chemical"},{"id":"397","span":{"begin":1083,"end":1091},"obj":"Chemical"},{"id":"398","span":{"begin":428,"end":433},"obj":"Disease"},{"id":"399","span":{"begin":513,"end":518},"obj":"Disease"}],"attributes":[{"id":"A385","pred":"tao:has_database_id","subj":"385","obj":"Gene:2641"},{"id":"A386","pred":"tao:has_database_id","subj":"386","obj":"Gene:2695"},{"id":"A387","pred":"tao:has_database_id","subj":"387","obj":"Gene:134864"},{"id":"A388","pred":"tao:has_database_id","subj":"388","obj":"Gene:1437"},{"id":"A389","pred":"tao:has_database_id","subj":"389","obj":"Gene:134864"},{"id":"A390","pred":"tao:has_database_id","subj":"390","obj":"Tax:4932"},{"id":"A391","pred":"tao:has_database_id","subj":"391","obj":"Tax:9606"},{"id":"A392","pred":"tao:has_database_id","subj":"392","obj":"Tax:2005392"},{"id":"A393","pred":"tao:has_database_id","subj":"393","obj":"MESH:C047981"},{"id":"A394","pred":"tao:has_database_id","subj":"394","obj":"MESH:C046274"},{"id":"A395","pred":"tao:has_database_id","subj":"395","obj":"MESH:D011092"},{"id":"A397","pred":"tao:has_database_id","subj":"397","obj":"MESH:D010455"},{"id":"A398","pred":"tao:has_database_id","subj":"398","obj":"MESH:D009369"},{"id":"A399","pred":"tao:has_database_id","subj":"399","obj":"MESH:D009369"}],"namespaces":[{"prefix":"Tax","uri":"https://www.ncbi.nlm.nih.gov/taxonomy/"},{"prefix":"MESH","uri":"https://id.nlm.nih.gov/mesh/"},{"prefix":"Gene","uri":"https://www.ncbi.nlm.nih.gov/gene/"},{"prefix":"CVCL","uri":"https://web.expasy.org/cellosaurus/CVCL_"}],"text":"Furthermore, PASylation can serve as a linker to join two peptides [69]. This is of particular interest if both entities act synergistically, for example, GLP-1 and GIP [70] or Tα1 and GM-CSF [71]. Alternatively, the biologically active protein/peptide can be linked via the PAS sequence to a targeting domain such as the arginylglycylaspartic acid peptide RGD peptide which binds to integrins αVβ3 and αVβ5 in order to enhance tumor penetration and accumulation. In fact, fusion of the short-acting Tα1 with the tumor-targeting iRGD peptide using a Gly4 linker has recently demonstrated enhanced antitumor activity [50]. In contrast to synthetic PEG linkers, which are commonly used for bioconjugations, the recombinant PAS sequence exhibits a precisely defined size and is biodegradable [72]. The PAS polypeptide itself is stable in blood plasma but quickly degraded by intracellular enzymes, thus avoiding organ accumulation [31], a well-known effect for PEGylation [73]. Moreover, PAS sequences are non-immunogenic in animals [31,74] and offer a one-step production of PASylated peptides in various commercially scalable expression systems including bacteria, yeasts, or mammalian cells [35,48], which would even allow the preparation of peptides carrying posttranslational modifications."}

{"project":"LitCovid-PD-HP","denotations":[{"id":"T21","span":{"begin":428,"end":433},"obj":"Phenotype"},{"id":"T22","span":{"begin":513,"end":518},"obj":"Phenotype"}],"attributes":[{"id":"A21","pred":"hp_id","subj":"T21","obj":"http://purl.obolibrary.org/obo/HP_0002664"},{"id":"A22","pred":"hp_id","subj":"T22","obj":"http://purl.obolibrary.org/obo/HP_0002664"}],"text":"Furthermore, PASylation can serve as a linker to join two peptides [69]. This is of particular interest if both entities act synergistically, for example, GLP-1 and GIP [70] or Tα1 and GM-CSF [71]. Alternatively, the biologically active protein/peptide can be linked via the PAS sequence to a targeting domain such as the arginylglycylaspartic acid peptide RGD peptide which binds to integrins αVβ3 and αVβ5 in order to enhance tumor penetration and accumulation. In fact, fusion of the short-acting Tα1 with the tumor-targeting iRGD peptide using a Gly4 linker has recently demonstrated enhanced antitumor activity [50]. In contrast to synthetic PEG linkers, which are commonly used for bioconjugations, the recombinant PAS sequence exhibits a precisely defined size and is biodegradable [72]. The PAS polypeptide itself is stable in blood plasma but quickly degraded by intracellular enzymes, thus avoiding organ accumulation [31], a well-known effect for PEGylation [73]. Moreover, PAS sequences are non-immunogenic in animals [31,74] and offer a one-step production of PASylated peptides in various commercially scalable expression systems including bacteria, yeasts, or mammalian cells [35,48], which would even allow the preparation of peptides carrying posttranslational modifications."}

{"project":"LitCovid-sentences","denotations":[{"id":"T124","span":{"begin":0,"end":72},"obj":"Sentence"},{"id":"T125","span":{"begin":73,"end":197},"obj":"Sentence"},{"id":"T126","span":{"begin":198,"end":463},"obj":"Sentence"},{"id":"T127","span":{"begin":464,"end":621},"obj":"Sentence"},{"id":"T128","span":{"begin":622,"end":794},"obj":"Sentence"},{"id":"T129","span":{"begin":795,"end":974},"obj":"Sentence"},{"id":"T130","span":{"begin":975,"end":1292},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Furthermore, PASylation can serve as a linker to join two peptides [69]. This is of particular interest if both entities act synergistically, for example, GLP-1 and GIP [70] or Tα1 and GM-CSF [71]. Alternatively, the biologically active protein/peptide can be linked via the PAS sequence to a targeting domain such as the arginylglycylaspartic acid peptide RGD peptide which binds to integrins αVβ3 and αVβ5 in order to enhance tumor penetration and accumulation. In fact, fusion of the short-acting Tα1 with the tumor-targeting iRGD peptide using a Gly4 linker has recently demonstrated enhanced antitumor activity [50]. In contrast to synthetic PEG linkers, which are commonly used for bioconjugations, the recombinant PAS sequence exhibits a precisely defined size and is biodegradable [72]. The PAS polypeptide itself is stable in blood plasma but quickly degraded by intracellular enzymes, thus avoiding organ accumulation [31], a well-known effect for PEGylation [73]. Moreover, PAS sequences are non-immunogenic in animals [31,74] and offer a one-step production of PASylated peptides in various commercially scalable expression systems including bacteria, yeasts, or mammalian cells [35,48], which would even allow the preparation of peptides carrying posttranslational modifications."}