FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W1982510102> ?p ?o ?g. }

• W1982510102 endingPage "294" @default.
• W1982510102 startingPage "282" @default.
• W1982510102 abstract "Thrombovascular diseases result from imbalanced haemostasis and comprise important health problems in the aging population worldwide. The activity of enzymes pertaining to the coagulation cascade of mammalians exhibit several control mechanisms in order to maintain a proper balance between bleeding and thrombosis. For instance, human coagulation serine proteases carrying a F225 or Y225 are allosteric modulated by the binding of Na+ in a water-filled channel connected to the primary specificity pocket (S1 subsite) of these enzymes. We have characterized the structure, topography and lipophilicity of this channel in the ligand-free fast (sodium-bound) and slow (sodium-free) forms of thrombin, in the sole available structure of activated protein C and in several structures of the coagulation factors VIIa, IXa and Xa, differing in the nature of the bound inhibitor and in the occupancy of exosite-I as well as the Ca2+ and Na+ binding sites. Opposite to thrombin, the aqueous channels in all other coagulation enzymes sheltering a Na+ binding site do not have an aperture on the enzyme surface opposite to the S1 subsite entrance. In these enzymes, the lack of the three-residue insertion in loop 1 (183-189) as found in thrombin allied to compensatory mutations in the positions 187-185 and 222 effects a constriction in the water-filled channel that ends up by segregating the ion binding site from the S1 subsite. We also disclosed major topographical changes on the thrombin's surface upon sodium release and transition to the slow form that culminate in the narrowing of the S1 subsite entrance and, strikingly, in the loss of communication between the primary specificity pocket and the exosite-I. Such observation is in accordance with existing experimental data demonstrating thermodynamic linkage between these distant regions on the thrombin surface. Conformational changes in F34, L40, R73 and T74 were the main responsible for this effect. A path by which these changes in the vicinity of exosite-I could be transmitted to the S1 subsite and, consequently, to the sodium binding site is proposed." @default.
• W1982510102 created "2016-06-24" @default.
• W1982510102 creator A5020834458 @default.
• W1982510102 creator A5044492580 @default.
• W1982510102 creator A5047392255 @default.
• W1982510102 creator A5086942190 @default.
• W1982510102 date "2006-02-01" @default.
• W1982510102 modified "2023-09-25" @default.
• W1982510102 title "The Na+ binding channel of human coagulation proteases: Novel insights on the structure and allosteric modulation revealed by molecular surface analysis" @default.
• W1982510102 cites W110482318 @default.
• W1982510102 cites W1497924644 @default.
• W1982510102 cites W1507164076 @default.
• W1982510102 cites W1964127780 @default.
• W1982510102 cites W1969847251 @default.
• W1982510102 cites W1977881358 @default.
• W1982510102 cites W1985407614 @default.
• W1982510102 cites W1995070983 @default.
• W1982510102 cites W1995886976 @default.
• W1982510102 cites W2002262647 @default.
• W1982510102 cites W2006813007 @default.
• W1982510102 cites W2010303722 @default.
• W1982510102 cites W2017569531 @default.
• W1982510102 cites W2017946980 @default.
• W1982510102 cites W2029428222 @default.
• W1982510102 cites W2029510213 @default.
• W1982510102 cites W2032329162 @default.
• W1982510102 cites W2036359252 @default.
• W1982510102 cites W2043324858 @default.
• W1982510102 cites W2045225337 @default.
• W1982510102 cites W2049753237 @default.
• W1982510102 cites W2052918960 @default.
• W1982510102 cites W2063342065 @default.
• W1982510102 cites W2063609829 @default.
• W1982510102 cites W2076086429 @default.
• W1982510102 cites W2078803528 @default.
• W1982510102 cites W2082841654 @default.
• W1982510102 cites W2083226596 @default.
• W1982510102 cites W2083831568 @default.
• W1982510102 cites W2086179867 @default.
• W1982510102 cites W2088545776 @default.
• W1982510102 cites W2089935734 @default.
• W1982510102 cites W2108508060 @default.
• W1982510102 cites W2109906659 @default.
• W1982510102 cites W2130327095 @default.
• W1982510102 cites W2133679578 @default.
• W1982510102 cites W2160439330 @default.
• W1982510102 cites W2171229523 @default.
• W1982510102 doi "https://doi.org/10.1016/j.bpc.2005.10.001" @default.
• W1982510102 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/16288954" @default.
• W1982510102 hasPublicationYear "2006" @default.
• W1982510102 type Work @default.
• W1982510102 sameAs 1982510102 @default.
• W1982510102 citedByCount "10" @default.
• W1982510102 countsByYear W19825101022019 @default.
• W1982510102 countsByYear W19825101022020 @default.
• W1982510102 countsByYear W19825101022021 @default.
• W1982510102 crossrefType "journal-article" @default.
• W1982510102 hasAuthorship W1982510102A5020834458 @default.
• W1982510102 hasAuthorship W1982510102A5044492580 @default.
• W1982510102 hasAuthorship W1982510102A5047392255 @default.
• W1982510102 hasAuthorship W1982510102A5086942190 @default.
• W1982510102 hasConcept C107824862 @default.
• W1982510102 hasConcept C118552586 @default.
• W1982510102 hasConcept C12554922 @default.
• W1982510102 hasConcept C144024400 @default.
• W1982510102 hasConcept C149923435 @default.
• W1982510102 hasConcept C15744967 @default.
• W1982510102 hasConcept C166342909 @default.
• W1982510102 hasConcept C181199279 @default.
• W1982510102 hasConcept C182220744 @default.
• W1982510102 hasConcept C185592680 @default.
• W1982510102 hasConcept C203014093 @default.
• W1982510102 hasConcept C2777292125 @default.
• W1982510102 hasConcept C2778382381 @default.
• W1982510102 hasConcept C2908647359 @default.
• W1982510102 hasConcept C55493867 @default.
• W1982510102 hasConcept C71240020 @default.
• W1982510102 hasConcept C86803240 @default.
• W1982510102 hasConcept C89560881 @default.
• W1982510102 hasConceptScore W1982510102C107824862 @default.
• W1982510102 hasConceptScore W1982510102C118552586 @default.
• W1982510102 hasConceptScore W1982510102C12554922 @default.
• W1982510102 hasConceptScore W1982510102C144024400 @default.
• W1982510102 hasConceptScore W1982510102C149923435 @default.
• W1982510102 hasConceptScore W1982510102C15744967 @default.
• W1982510102 hasConceptScore W1982510102C166342909 @default.
• W1982510102 hasConceptScore W1982510102C181199279 @default.
• W1982510102 hasConceptScore W1982510102C182220744 @default.
• W1982510102 hasConceptScore W1982510102C185592680 @default.
• W1982510102 hasConceptScore W1982510102C203014093 @default.
• W1982510102 hasConceptScore W1982510102C2777292125 @default.
• W1982510102 hasConceptScore W1982510102C2778382381 @default.
• W1982510102 hasConceptScore W1982510102C2908647359 @default.
• W1982510102 hasConceptScore W1982510102C55493867 @default.
• W1982510102 hasConceptScore W1982510102C71240020 @default.
• W1982510102 hasConceptScore W1982510102C86803240 @default.
• W1982510102 hasConceptScore W1982510102C89560881 @default.
• W1982510102 hasIssue "3" @default.

• next