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PMC:7544943 / 36579-37229 JSONTXT

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LitCovid-PD-FMA-UBERON

Id Subject Object Predicate Lexical cue fma_id
T50 142-149 Body_part denotes protein http://purl.org/sig/ont/fma/fma67257
T51 161-168 Body_part denotes protein http://purl.org/sig/ont/fma/fma67257
T52 258-266 Body_part denotes backbone http://purl.org/sig/ont/fma/fma13478
T53 280-288 Body_part denotes proteins http://purl.org/sig/ont/fma/fma67257
T54 502-510 Body_part denotes proteins http://purl.org/sig/ont/fma/fma67257
T55 641-649 Body_part denotes proteins http://purl.org/sig/ont/fma/fma67257

LitCovid-PD-MONDO

Id Subject Object Predicate Lexical cue mondo_id
T71 356-359 Disease denotes PC1 http://purl.obolibrary.org/obo/MONDO_0008173
T72 364-367 Disease denotes PC2 http://purl.obolibrary.org/obo/MONDO_0008174

LitCovid-PD-CLO

Id Subject Object Predicate Lexical cue
T171 193-195 http://purl.obolibrary.org/obo/CLO_0007622 denotes MD
T172 394-395 http://purl.obolibrary.org/obo/CLO_0001020 denotes a
T173 396-397 http://purl.obolibrary.org/obo/CLO_0001021 denotes b

LitCovid-PubTator

Id Subject Object Predicate Lexical cue tao:has_database_id
846 364-367 Gene denotes PC2 Gene:3854
847 356-359 Gene denotes PC1 Gene:5167
848 447-451 Gene denotes Mpro Gene:8673700
849 429-442 Chemical denotes Spro-Piperine

LitCovid-sentences

Id Subject Object Predicate Lexical cue
T329 0-89 Sentence denotes The PCA is an essential technique to monitor the conformational dynamics of biomolecules.
T330 90-209 Sentence denotes It is useful in determining the concerted motion of protein as well as protein–ligand complex from the MD trajectories.
T331 210-379 Sentence denotes The diagonalization of the covariance matrix of backbone atoms of the proteins and ligand-bound form were considered for the principal components PC1 and PC2 (Figure 9).
T332 380-556 Sentence denotes From Figure 9(a,b), it is observed that both the Spro-Piperine and Mpro-Piperine are less flexible as compared to unbound proteins since they covered less conformational space.
T333 557-650 Sentence denotes It concludes that the ligand-bound forms are more stable as compared to the unbound proteins.