> top > docs > PubMed:17897951 > annotations

PubMed:17897951 JSONTXT

Annnotations TAB JSON ListView MergeView

Inflammaging

Id Subject Object Predicate Lexical cue
T1 0-112 Sentence denotes Structural basis for innate immune sensing by M-ficolin and its control by a pH-dependent conformational switch.
T2 113-261 Sentence denotes Ficolins are soluble oligomeric proteins with lectin-like activity, assembled from collagen fibers prolonged by fibrinogen-like recognition domains.
T3 262-459 Sentence denotes They act as innate immune sensors by recognizing conserved molecular markers exposed on microbial surfaces and thereby triggering effector mechanisms such as enhanced phagocytosis and inflammation.
T4 460-601 Sentence denotes In humans, L- and H-ficolins have been characterized in plasma, whereas a third species, M-ficolin, is secreted by monocytes and macrophages.
T5 602-913 Sentence denotes To decipher the molecular mechanisms underlying their recognition properties, we previously solved the structures of the recognition domains of L- and H-ficolins, in complex with various model ligands (Garlatti, V., Belloy, N., Martin, L., Lacroix, M., Matsushita, M., Endo, Y., Fujita, T., Fontecilla-Camps, J.
T6 914-928 Sentence denotes C., Arlaud, G.
T7 929-945 Sentence denotes J., Thielens, N.
T8 946-982 Sentence denotes M., and Gaboriaud, C. (2007) EMBO J.
T9 983-996 Sentence denotes 24, 623-633).
T10 997-1204 Sentence denotes We now report the ligand-bound crystal structures of the recognition domain of M-ficolin, determined at high resolution (1.75-1.8 A), which provides the first structural insights into its binding properties.
T11 1205-1303 Sentence denotes Interaction with acetylated carbohydrates differs from the one previously described for L-ficolin.
T12 1304-1471 Sentence denotes This study also reveals the structural determinants for binding to sialylated compounds, a property restricted to human M-ficolin and its mouse counterpart, ficolin B.
T13 1472-1662 Sentence denotes Finally, comparison between the ligand-bound structures obtained at neutral pH and nonbinding conformations observed at pH 5.6 reveals how the ligand binding site is dislocated at acidic pH.
T14 1663-1764 Sentence denotes This means that the binding function of M-ficolin is subject to a pH-sensitive conformational switch.
T15 1765-1868 Sentence denotes Considering that the homologous ficolin B is found in the lysosomes of activated macrophages (Runza, V.
T16 1869-1932 Sentence denotes L., Hehlgans, T., Echtenacher, B., Zahringer, U., Schwaeble, W.
T17 1933-1951 Sentence denotes J., and Mannel, D.
T18 1952-1964 Sentence denotes N. (2006) J.
T19 1965-1979 Sentence denotes Endotoxin Res.
T20 1980-2082 Sentence denotes 12, 120-126), we propose that this switch could play a physiological role in such acidic compartments.
T1 0-112 Sentence denotes Structural basis for innate immune sensing by M-ficolin and its control by a pH-dependent conformational switch.
T2 113-261 Sentence denotes Ficolins are soluble oligomeric proteins with lectin-like activity, assembled from collagen fibers prolonged by fibrinogen-like recognition domains.
T3 262-459 Sentence denotes They act as innate immune sensors by recognizing conserved molecular markers exposed on microbial surfaces and thereby triggering effector mechanisms such as enhanced phagocytosis and inflammation.
T4 460-601 Sentence denotes In humans, L- and H-ficolins have been characterized in plasma, whereas a third species, M-ficolin, is secreted by monocytes and macrophages.
T5 602-913 Sentence denotes To decipher the molecular mechanisms underlying their recognition properties, we previously solved the structures of the recognition domains of L- and H-ficolins, in complex with various model ligands (Garlatti, V., Belloy, N., Martin, L., Lacroix, M., Matsushita, M., Endo, Y., Fujita, T., Fontecilla-Camps, J.
T6 914-928 Sentence denotes C., Arlaud, G.
T7 929-945 Sentence denotes J., Thielens, N.
T8 946-982 Sentence denotes M., and Gaboriaud, C. (2007) EMBO J.
T9 983-996 Sentence denotes 24, 623-633).
T10 997-1204 Sentence denotes We now report the ligand-bound crystal structures of the recognition domain of M-ficolin, determined at high resolution (1.75-1.8 A), which provides the first structural insights into its binding properties.
T11 1205-1303 Sentence denotes Interaction with acetylated carbohydrates differs from the one previously described for L-ficolin.
T12 1304-1471 Sentence denotes This study also reveals the structural determinants for binding to sialylated compounds, a property restricted to human M-ficolin and its mouse counterpart, ficolin B.
T13 1472-1662 Sentence denotes Finally, comparison between the ligand-bound structures obtained at neutral pH and nonbinding conformations observed at pH 5.6 reveals how the ligand binding site is dislocated at acidic pH.
T14 1663-1764 Sentence denotes This means that the binding function of M-ficolin is subject to a pH-sensitive conformational switch.
T15 1765-1868 Sentence denotes Considering that the homologous ficolin B is found in the lysosomes of activated macrophages (Runza, V.
T16 1869-1932 Sentence denotes L., Hehlgans, T., Echtenacher, B., Zahringer, U., Schwaeble, W.
T17 1933-1951 Sentence denotes J., and Mannel, D.
T18 1952-1964 Sentence denotes N. (2006) J.
T19 1965-1979 Sentence denotes Endotoxin Res.
T20 1980-2082 Sentence denotes 12, 120-126), we propose that this switch could play a physiological role in such acidic compartments.

sentences

Id Subject Object Predicate Lexical cue
T1 0-112 Sentence denotes Structural basis for innate immune sensing by M-ficolin and its control by a pH-dependent conformational switch.
T2 113-261 Sentence denotes Ficolins are soluble oligomeric proteins with lectin-like activity, assembled from collagen fibers prolonged by fibrinogen-like recognition domains.
T3 262-459 Sentence denotes They act as innate immune sensors by recognizing conserved molecular markers exposed on microbial surfaces and thereby triggering effector mechanisms such as enhanced phagocytosis and inflammation.
T4 460-601 Sentence denotes In humans, L- and H-ficolins have been characterized in plasma, whereas a third species, M-ficolin, is secreted by monocytes and macrophages.
T5 602-913 Sentence denotes To decipher the molecular mechanisms underlying their recognition properties, we previously solved the structures of the recognition domains of L- and H-ficolins, in complex with various model ligands (Garlatti, V., Belloy, N., Martin, L., Lacroix, M., Matsushita, M., Endo, Y., Fujita, T., Fontecilla-Camps, J.
T6 914-928 Sentence denotes C., Arlaud, G.
T7 929-945 Sentence denotes J., Thielens, N.
T8 946-982 Sentence denotes M., and Gaboriaud, C. (2007) EMBO J.
T9 983-996 Sentence denotes 24, 623-633).
T10 997-1204 Sentence denotes We now report the ligand-bound crystal structures of the recognition domain of M-ficolin, determined at high resolution (1.75-1.8 A), which provides the first structural insights into its binding properties.
T11 1205-1303 Sentence denotes Interaction with acetylated carbohydrates differs from the one previously described for L-ficolin.
T12 1304-1471 Sentence denotes This study also reveals the structural determinants for binding to sialylated compounds, a property restricted to human M-ficolin and its mouse counterpart, ficolin B.
T13 1472-1662 Sentence denotes Finally, comparison between the ligand-bound structures obtained at neutral pH and nonbinding conformations observed at pH 5.6 reveals how the ligand binding site is dislocated at acidic pH.
T14 1663-1764 Sentence denotes This means that the binding function of M-ficolin is subject to a pH-sensitive conformational switch.
T15 1765-1868 Sentence denotes Considering that the homologous ficolin B is found in the lysosomes of activated macrophages (Runza, V.
T16 1869-1932 Sentence denotes L., Hehlgans, T., Echtenacher, B., Zahringer, U., Schwaeble, W.
T17 1933-1951 Sentence denotes J., and Mannel, D.
T18 1952-1964 Sentence denotes N. (2006) J.
T19 1965-1979 Sentence denotes Endotoxin Res.
T20 1980-2082 Sentence denotes 12, 120-126), we propose that this switch could play a physiological role in such acidic compartments.

PubmedHPO

Id Subject Object Predicate Lexical cue
T1 1638-1648 HP_0001373 denotes dislocated

mondo_disease

Id Subject Object Predicate Lexical cue mondo_id
T1 446-458 Disease denotes inflammation http://purl.obolibrary.org/obo/MONDO_0021166

Lectin-Jamboree-Sentence

Id Subject Object Predicate Lexical cue
T1 0-112 Sentence denotes Structural basis for innate immune sensing by M-ficolin and its control by a pH-dependent conformational switch.
T2 113-261 Sentence denotes Ficolins are soluble oligomeric proteins with lectin-like activity, assembled from collagen fibers prolonged by fibrinogen-like recognition domains.
T3 262-459 Sentence denotes They act as innate immune sensors by recognizing conserved molecular markers exposed on microbial surfaces and thereby triggering effector mechanisms such as enhanced phagocytosis and inflammation.
T4 460-601 Sentence denotes In humans, L- and H-ficolins have been characterized in plasma, whereas a third species, M-ficolin, is secreted by monocytes and macrophages.
T5 602-996 Sentence denotes To decipher the molecular mechanisms underlying their recognition properties, we previously solved the structures of the recognition domains of L- and H-ficolins, in complex with various model ligands (Garlatti, V., Belloy, N., Martin, L., Lacroix, M., Matsushita, M., Endo, Y., Fujita, T., Fontecilla-Camps, J. C., Arlaud, G. J., Thielens, N. M., and Gaboriaud, C. (2007) EMBO J. 24, 623-633).
T6 997-1204 Sentence denotes We now report the ligand-bound crystal structures of the recognition domain of M-ficolin, determined at high resolution (1.75-1.8 A), which provides the first structural insights into its binding properties.
T7 1205-1303 Sentence denotes Interaction with acetylated carbohydrates differs from the one previously described for L-ficolin.
T8 1304-1662 Sentence denotes This study also reveals the structural determinants for binding to sialylated compounds, a property restricted to human M-ficolin and its mouse counterpart, ficolin B. Finally, comparison between the ligand-bound structures obtained at neutral pH and nonbinding conformations observed at pH 5.6 reveals how the ligand binding site is dislocated at acidic pH.
T9 1663-1764 Sentence denotes This means that the binding function of M-ficolin is subject to a pH-sensitive conformational switch.
T10 1765-2082 Sentence denotes Considering that the homologous ficolin B is found in the lysosomes of activated macrophages (Runza, V. L., Hehlgans, T., Echtenacher, B., Zahringer, U., Schwaeble, W. J., and Mannel, D. N. (2006) J. Endotoxin Res. 12, 120-126), we propose that this switch could play a physiological role in such acidic compartments.

NCBITAXON

Id Subject Object Predicate Lexical cue db_id
T1 893-903 OrganismTaxon denotes Fontecilla 375848
T2 1418-1423 OrganismTaxon denotes human 9606
T3 1442-1447 OrganismTaxon denotes mouse 10088|10090

Anatomy-UBERON

Id Subject Object Predicate Lexical cue uberon_id
T1 516-522 Body_part denotes plasma http://purl.obolibrary.org/obo/UBERON_0001969
T2 575-584 Body_part denotes monocytes http://purl.obolibrary.org/obo/CL_0000576|http://purl.obolibrary.org/obo/CL_0001054
T4 589-600 Body_part denotes macrophages http://purl.obolibrary.org/obo/CL_0000235
T5 1823-1832 Body_part denotes lysosomes http://purl.obolibrary.org/obo/GO_0005764
T6 1846-1857 Body_part denotes macrophages http://purl.obolibrary.org/obo/CL_0000235

CL-cell

Id Subject Object Predicate Lexical cue cl_id
T1 575-584 Cell denotes monocytes http://purl.obolibrary.org/obo/CL:0000576|http://purl.obolibrary.org/obo/CL:0001054
T3 589-600 Cell denotes macrophages http://purl.obolibrary.org/obo/CL:0000235|http://purl.obolibrary.org/obo/CL:0000394
T5 1846-1857 Cell denotes macrophages http://purl.obolibrary.org/obo/CL:0000235|http://purl.obolibrary.org/obo/CL:0000394