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PubMed:9822649 JSONTXT 41 Projects

Annnotations TAB TSV DIC JSON TextAE Lectin_function

Id Subject Object Predicate Lexical cue
TextSentencer_T1 0-27 Sentence denotes Recombinant procollagen II:
T1 0-27 Sentence denotes Recombinant procollagen II:
TextSentencer_T2 28-186 Sentence denotes Deletion of D period segments identifies sequences that are required for helix stabilization and generates a temperature-sensitive N-proteinase cleavage site.
T2 28-186 Sentence denotes Deletion of D period segments identifies sequences that are required for helix stabilization and generates a temperature-sensitive N-proteinase cleavage site.
TextSentencer_T3 187-399 Sentence denotes A cDNA cassette system was used to synthesize recombinant versions of procollagen II in which one of the four blocks of 234 amino acids that define a repeating D periods of the collagen triple helix were deleted.
T3 187-399 Sentence denotes A cDNA cassette system was used to synthesize recombinant versions of procollagen II in which one of the four blocks of 234 amino acids that define a repeating D periods of the collagen triple helix were deleted.
TextSentencer_T4 400-542 Sentence denotes All the proteins were triple helical and all underwent a helix-to-coil transition between 25 and 42 degreesC as assayed by circular dichroism.
T4 400-542 Sentence denotes All the proteins were triple helical and all underwent a helix-to-coil transition between 25 and 42 degreesC as assayed by circular dichroism.
TextSentencer_T5 543-593 Sentence denotes However, the details of the melting curves varied.
T5 543-593 Sentence denotes However, the details of the melting curves varied.
TextSentencer_T6 594-686 Sentence denotes The procollagen lacking the D1 period unfolded 3 degreesC lower than a full-length molecule.
T6 594-686 Sentence denotes The procollagen lacking the D1 period unfolded 3 degreesC lower than a full-length molecule.
TextSentencer_T7 687-884 Sentence denotes With the procollagen lacking the D4 period, the first 25% of unfolding occurred at a lower temperature than the full-length molecule, but the rest of the structure unfolded at the same temperature.
T7 687-884 Sentence denotes With the procollagen lacking the D4 period, the first 25% of unfolding occurred at a lower temperature than the full-length molecule, but the rest of the structure unfolded at the same temperature.
TextSentencer_T8 885-1133 Sentence denotes With the procollagen lacking the terminal D0.4 period, the protein unfolded 3 degreesC lower than the full-length molecule and a smaller fraction of the protein was secreted by stably transfected clones than with the other recombinant procollagens.
T8 885-1133 Sentence denotes With the procollagen lacking the terminal D0.4 period, the protein unfolded 3 degreesC lower than the full-length molecule and a smaller fraction of the protein was secreted by stably transfected clones than with the other recombinant procollagens.
TextSentencer_T9 1134-1406 Sentence denotes The results confirmed previous suggestions that the collagen triple helix contains regions of varying stability and they demonstrated that the two D periods at the end of the molecule contain sequences that serve as clamps for folding and for stabilizing the triple helix.
T9 1134-1406 Sentence denotes The results confirmed previous suggestions that the collagen triple helix contains regions of varying stability and they demonstrated that the two D periods at the end of the molecule contain sequences that serve as clamps for folding and for stabilizing the triple helix.
TextSentencer_T10 1407-1732 Sentence denotes Reaction of the recombinant procollagens with procollagen N-proteinase indicated that in the procollagen lacking the sequences, the D1 period assumed an unusual temperature-sensitive conformation at 35 degreesC that allowed cleavage at an otherwise resistant Gly-Ala bond between residues 394 and 395 of the alpha1(II) chain.
T10 1407-1732 Sentence denotes Reaction of the recombinant procollagens with procollagen N-proteinase indicated that in the procollagen lacking the sequences, the D1 period assumed an unusual temperature-sensitive conformation at 35 degreesC that allowed cleavage at an otherwise resistant Gly-Ala bond between residues 394 and 395 of the alpha1(II) chain.