FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2010018631> ?p ?o ?g. }

• W2010018631 endingPage "60" @default.
• W2010018631 startingPage "60" @default.
• W2010018631 abstract "An attempt has been made to precise the molecular mechanisms of human genetic enzymatic diseases. Starting from the data of bacterial genetics, predictions of the theory are compared to the actual facts.o1.Controller gene abnormalities should now be discussed in the light of positive as well as negative control. Non-functioning of the regulator (regulator-negative mutation) would result in a recessive gain of function in a negative control system, in a recessive loss of function in a positive system. In both cases heterozygotes should show no change of enzymatic activity. A superrepressor mutation in a negative system would produce a dominant loss of function; a constitutive mutation in a positive system would in principle produce a dominant gain.The general case is actually that of a loss of function with a partial deficiency in heterozygotes and does not fit the predictions. Among recessive diseases the only good candidates are thalassemias, which could be explained by operator negative mutations in a negative system, or by regulator mutations in a positive system. Von Willebrand's disease (dominant vascular abnormalities with a deficiency of antihemophilic factor) could be due to a mutation of the superrepressor type. Hepatic porphyria (involving an increase in the enzyme amino-levulinic acid synthetase) would be best explained by a constitutive mutation of the activator in a positive regulatory system.2.Structural gene abnormalities are increasingly being demonstrated despite many difficulties. Investigations are conducted along several lines:–Electrophoresis has been useful in only a few cases, an outstanding example being that of glucose-6-phosphate dehydrogenase.–A decreased affinity towards the substrate or a diminished reactivity with the coenzyme can in a good many examples explain the anomalies. In the latter case this affords a remarkable approach to therapy.–Immunological search for the molecule seems to be presently the best general tool to look for an enzymatically inactive protein. At least in six enzymatic deficiencies the molecule could be recognized showing in addition in each case a genetic heterogeneity. Only in two diseases attempts have been unsuccessful so far. In addition the molecule was found to be present in all six defects of clotting factors which have been investigated.3.Other possible mechanisms are briefly discussed. One possibility is a non-sense mutation. An attempt to demonstrate the biosynthesis of an initial fragment of hemoglobin chain in some cases of thalassemia was unsuccessful.4.In conclusion most of the simple genetic enzymatic deficiencies are probably due to missense mutations in the structural genes.The molecule is being found in an increasing number of diseases. The mechanisms which seem to be at work in most cases are the following:–Instability of the molecule: this is probably the most frequent case when the number of molecules is low in the diseased tissue. The best example is that of many types of red cell glucose-6-phosphate dehydrogenase deficiencies.–Modification of the active site or the overall structure of the molecule, which is probable when the molecule is present in normal amount.–Lack of transformation of a precursor molecule, which could be responsible for some clotting factor defects." @default.
• W2010018631 created "2016-06-24" @default.
• W2010018631 creator A5021742553 @default.
• W2010018631 creator A5027968457 @default.
• W2010018631 creator A5087788813 @default.
• W2010018631 date "2004-05-01" @default.
• W2010018631 modified "2023-09-27" @default.
• W2010018631 title "DEGRADED COLLAGEN FRAGMENTS ACTIVATE NF-KB VIA ALPHAVBETA3 INTEGRINS AND PROTECT SMOOTH MUSCLE CELLS AGAINST APOPTOSIS THROUGH INDUCTION OF INHIBITOR OF APOPTOSIS PROTEINS (IAPS)" @default.
• W2010018631 doi "https://doi.org/10.1016/j.carpath.2004.03.176" @default.
• W2010018631 hasPublicationYear "2004" @default.
• W2010018631 type Work @default.
• W2010018631 sameAs 2010018631 @default.
• W2010018631 citedByCount "0" @default.
• W2010018631 crossrefType "journal-article" @default.
• W2010018631 hasAuthorship W2010018631A5021742553 @default.
• W2010018631 hasAuthorship W2010018631A5027968457 @default.
• W2010018631 hasAuthorship W2010018631A5087788813 @default.
• W2010018631 hasConcept C104317684 @default.
• W2010018631 hasConcept C105951970 @default.
• W2010018631 hasConcept C127716648 @default.
• W2010018631 hasConcept C153471976 @default.
• W2010018631 hasConcept C180754005 @default.
• W2010018631 hasConcept C501734568 @default.
• W2010018631 hasConcept C54355233 @default.
• W2010018631 hasConcept C6929976 @default.
• W2010018631 hasConcept C86803240 @default.
• W2010018631 hasConcept C88045685 @default.
• W2010018631 hasConceptScore W2010018631C104317684 @default.
• W2010018631 hasConceptScore W2010018631C105951970 @default.
• W2010018631 hasConceptScore W2010018631C127716648 @default.
• W2010018631 hasConceptScore W2010018631C153471976 @default.
• W2010018631 hasConceptScore W2010018631C180754005 @default.
• W2010018631 hasConceptScore W2010018631C501734568 @default.
• W2010018631 hasConceptScore W2010018631C54355233 @default.
• W2010018631 hasConceptScore W2010018631C6929976 @default.
• W2010018631 hasConceptScore W2010018631C86803240 @default.
• W2010018631 hasConceptScore W2010018631C88045685 @default.
• W2010018631 hasIssue "3" @default.
• W2010018631 hasLocation W20100186311 @default.
• W2010018631 hasOpenAccess W2010018631 @default.
• W2010018631 hasPrimaryLocation W20100186311 @default.
• W2010018631 hasRelatedWork W1975253683 @default.
• W2010018631 hasRelatedWork W2031464773 @default.
• W2010018631 hasRelatedWork W2078889486 @default.
• W2010018631 hasRelatedWork W2086282504 @default.
• W2010018631 hasRelatedWork W2124025927 @default.
• W2010018631 hasRelatedWork W2125731289 @default.
• W2010018631 hasRelatedWork W2157166663 @default.
• W2010018631 hasRelatedWork W2349400098 @default.
• W2010018631 hasRelatedWork W2982109274 @default.
• W2010018631 hasRelatedWork W3032357680 @default.
• W2010018631 hasVolume "13" @default.
• W2010018631 isParatext "false" @default.
• W2010018631 isRetracted "false" @default.
• W2010018631 magId "2010018631" @default.
• W2010018631 workType "article" @default.