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  • 1
    Electronic Resource
    Electronic Resource
    Core database (1995)
    [s.l.] : Nature Publishing Group
    Nature 374 (1995), S. 402-402 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] SIR - The first single base-pair substitu-tion in a human gene underlying a genetic disorder was reported in 1979: a nonsense mutation in residue Lysl7 in the (3-globin gene resulting in (3-thalassaemia1. Since then, more than 3,300 different point mutations have been identified in approx-imately ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/374402b0
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  • 2
    Electronic Resource
    Electronic Resource
    The molecular genetics of growth hormone deficiency (1998)
    Springer
    Human genetics 〈Berlin〉 103 (1998), S. 255-272 
    Details
    ISSN: 1432-1203
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Although most cases of short stature associated with growth hormone (GH) deficiency are sporadic and idiopathic, some 5-30% have an affected first degree relative consistent with a genetic aetiology for the condition. Several different types of mutational lesion in the pituitary-expressed growth hormone (GH1) gene have been described in affected individuals. This review focuses primarily on the GH1 mutational spectrum and its unusual features, discusses potential mechanisms of mutagenesis and pathogenesis, and examines the correlation between mutant genotype and clinical phenotype. The characterization of pathological lesions in several other pituitary-expressed genes that are epistatic to GH1 (POU1F1, PROP1 and GHRHR) has identified additional causes of GH deficiency, the molecular genetics of which are also explored.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004390050815
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  • 3
    Electronic Resource
    Electronic Resource
    A novel missense mutation (Thr176→IIe) at the putative hinge of the neo N-terminus of activated protein C (1995)
    Springer
    Human genetics 〈Berlin〉 95 (1995), S. 447-450 
    Details
    ISSN: 1432-1203
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract We describe the detection of a novel missense mutation (Thr176→Ile) that is located at the neo N-terminus of activated protein C. The Thr176→Ile substitution leads to a type 1 deficiency state. Evidence is presented suggesting that this residue plays a role in pivoting the N-terminus of protein C to fold into the oxyanion hole.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00208974
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  • 4
    Electronic Resource
    Electronic Resource
    Molecular reconstruction and homology modelling of the catalytic domain of the common ancestor of the haemostatic vitamin-K-dependent serine proteinases (1996)
    Springer
    Human genetics 〈Berlin〉 98 (1996), S. 351-370 
    Details
    ISSN: 1432-1203
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract The vitamin-K-dependent serine proteinases of coagulation have evolved by a process of gene duplication and divergence, acquiring along the way a considerable degree of functional diversity that has equipped them for their different roles in haemostasis. The cDNA sequences encoding the catalytic domains of the early mammalian ancestors of five vitamin-K-dependent factors (factors VII, IX and X, protein C and prothrombin) were reconstructed by employing cDNA sequence data from a range of extant mammals and by using established phylogenies. The cDNA sequence of the putative common ancestor of these early mammalian proteins was then reconstructed from the five sequences by using a deduced phylogeny that was different in a number of respects from those previously proposed. Factor IX is proposed to have branched off early on, followed by protein C and prothrombin and finally factors VII and X. Significant differences in mutation rates were observed between proteins within a species; factor IX exhibited a lower mutation rate than the other proteins, consistent with its early emergence. Differences in mutation rates were also observed between species for a given protein and these exhibited an inverse correlation with generation time. A biophysically plausible structure for the ancestral vitamin-K-dependent factor protein was constructed by comparative methods. Studies of the functional architecture of this model provide new insights into the evolution of protein-binding specificity in this family of proteins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004390050222
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  • 5
    Electronic Resource
    Electronic Resource
    The mutational demography of protein C deficiency (1995)
    Springer
    Human genetics 〈Berlin〉 96 (1995), S. 142-146 
    Details
    ISSN: 1432-1203
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract The geographical distribution and prevalence of 256 single base-pair substitutions (105 of them being different) within the coding region of the human protein C (PROC) gene were correlated with their initial likelihoods of generation. A significant positive correlation was observed between these “mutational likelihoods” and the geographical dispersal of the PROC gene lesions within and between 16 different countries. This relationship could be attributed to the fact that, with few exceptions, high dispersal was only exhibited by CG→TG and CG→CA transitions, i.e. those substitutions that are known to arise de novo at the highest frequency. The statistical distribution of mutational likelihoods was as predicted on the basis of the PROC cDNA sequence alone, allowing however for the redundancy of the genetic code. These findings suggest (1) that genetic drift and lesion-specific selection have been of relatively minor importance in determining the mutational spectrum observed in the PROC gene and (2) that most multiple reports of particular substitutions in different geographical locations appear to reflect recurrent mutation rather than identity-by-descent.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00207369
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  • 6
    Electronic Resource
    Electronic Resource
    Mutational and functional analysis of the neurofibromatosis type 1 (NF1) gene (1996)
    Springer
    Human genetics 〈Berlin〉 99 (1996), S. 88-92 
    Details
    ISSN: 1432-1203
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Neurofibromatosis type 1 (NF1) is one of the most common autosomal dominant disorders. It is caused by mutations in the NF1 gene which comprises 60 exons and is located on chromosome 17q. The NF1 gene product, neurofibromin, displays partial homology to GTPase-activating protein (GAP). The GAP-related domain (GRD), encoded by exons 20–27a, is the only region of neurofibromin to which a biological function has been ascribed. A total of 320 unrelated NF1 patients were screened for mutations in the GRD-encoding region of the NF1 gene. Sixteen different lesions in the NF1 GRD region were identified in a total of 20 patients. Of these lesions, 14 are novel and together comprise three missense, two nonsense and three splice site mutations plus six deletions of between 1 and 4 bp. The effect of one of the missense mutations (R1391S) was studied by in vitro expression of a site-directed mutant and GAP activity assay. The mutant protein, R1391S, was found to be some 300-fold less active than wild-type NF1 GRD. The mutations reported in this study therefore provide further material for the functional analysis of neurofibromin as well as an insight into the mutational spectrum of the NF1 GRD.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004390050317
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  • 7
    Electronic Resource
    Electronic Resource
    Prothrombin cleavage by human vascular smooth muscle cells: A potential alternative pathway to the coagulation cascade (1995)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 59 (1995), S. 514-528 
    Details
    ISSN: 0730-2312
    Keywords: prothrombin ; prethrombin 2 ; fragment 1.2 ; α-thrombin ; prothrombin activation ; serine proteinase ; human vascular smooth muscle cells ; mitogenic activity ; enzymatic activity ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Thrombin is a potent mitogen for human vascular smooth muscle cells (HVSMC) and its enzymatic activity is required for this function. The present study demonstrates that prothrombin is also mitogenic for HVSMC due to the generation of enzymatically active thrombin which occurs upon incubation of prothrombin with the cells. Analysis by SDS-PAGE, immunoblotting, and amino acid sequencing revealed that prothrombin incubated with HVSMC undergoes limited proteolysis. Prethrombin 1 was formed through cleavage at R155-S156. Cleavage at R271-T272 generated fragment 1.2 and prethrombin 2 whilst cleavage at R284-T285 yielded truncated prothrombin 2 (prethrombin 2′). However, cleavage at R320-I321 which, during prothrombin activation produces two-chain α-thrombin, was not detectable. Studies on HVSMC-conditioned medium revealed that a similar pattern of prothrombin cleavage occurred by a cell-secreted factor(s). Amidolytic activity analysis indicated that 1-3% catalytically active thrombin-like activity was generated upon incubation of prothrombin with HVSMC-conditioned medium. By treating conditioned medium with various classes of proteinase inhibitors or hirudin, it was determined that prothrombin is cleaved by a cell-derived serine proteinase-like factor(s) at R271-S272 and by α-thrombin at R155-S156 and R284-T285. Antibodies neutralising the activity of either urokinase, tissue plasminogen activator, or factor Xa failed to alter the prothrombin cleaving activity of conditioned medium. This activity which may catalyse an alternative pathway for the generation of thrombin, was eluted from a gel filtration column as a single peak with apparent molecular mass of 30-40 kDa. © 1995 Wiley-Liss, Inc.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240590411
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