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  • 1990-1994  (576)
  • 1905-1909  (161)
  • 1860-1869  (4)
  • Inorganic Chemistry  (559)
  • Genetics  (182)
  • 1
    Electronic Resource
    Electronic Resource
    Human hexokinase II: localization of the polymorphic gene to chromosome 2 (1993)
    Springer
    Diabetologia 36 (1993), S. 1299-1302 
    Details
    ISSN: 1432-0428
    Keywords: Genetics ; DNA polymorphism ; glucose ; phosphorylation ; glycolysis ; chromosome 2 ; insulin resistance
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Type 2 (non-insulin-dependent) diabetes mellitus is characterized by decreased levels of glucose 6-phosphate in skeletal muscle. It has been suggested that the lower concentrations of glucose 6-phosphate contribute to the defect in glucose metabolism noted in muscle tissue of subjects with Type 2 diabetes or subjects at increased risk of developing Type 2 diabetes. Lower levels of glucose 6-phosphate could be due to a defect in glucose uptake, or phosphorylation, or both. Hexokinase II is the isozyme of hexokinase that is expressed in skeletal muscle and is responsible for catalysing the phosphorylation of glucose in this tissue. The recent demonstration that mutations in another member of this family of glucose phosphorylating enzymes, glucokinase, can lead to the development of Type 2 diabetes prompted us to begin to examine the possible role of hexokinase II in the development of this genetically heterogeneous disorder. As a first step, we have cloned the human hexokinase II gene (HK2) and mapped it to human chromosome 2, band p13.1, by fluorescence in situ hybridization to metaphase chromosomes. In addition, we have identified and characterized a simple tandem repeat DNA polymorphism in HK2 and used this DNA polymorphism to localize this gene within the genetic linkage map of chromosome 2.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00400809
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  • 2
    Electronic Resource
    Electronic Resource
    1,3,4-Oxa- und 1,3,4-Thia-diphospholane aus Diphosphorsubstituierten 2-Oxa- und 2-Thia-propanen (1990)
    Weinheim : Wiley-Blackwell
    Zeitschrift für anorganische Chemie 589 (1990), S. 187-198 
    Details
    ISSN: 0044-2313
    Keywords: Chemistry ; Inorganic Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Description / Table of Contents: 1,3,4-Oxadiphospholanes and 1,3,4-Thiadiphospholanes from Diphosphorus-substituted 2-Oxa- and 2-Thia-propanesThe synthesis of phosphonates and phosphinates of the type (RO)2(O)PCH2ZCH2P(O)(OR)2, R1(RO)(O)PCH2ZCH2P(O)(OR)2 and R1(RO)(O)PCH2ZCH2P(O)(OR)R1 (with Z = O, S; R = Et, Pri; R1 = Me, Ph) is reported. Acyclic diphosphanes, R1(H)PCH2ZCH2P(H)R2 (with Z = O, S; R1 = R2 = H, Me, Ph; R1 = H, R2 = Me), and 1,3,4-Oxadiphospholanes as well as 1,3,4-Thiadiphospholanes are obtained from the esters by reduction.
    Notes: Die Darstellung von Phosphonaten und Phosphinaten der Zusammensetzung (RO)2(O)PCH2ZCH2P(O)(OR)2, R1(RO)(O)PCH2ZCH2P(O)(OR)2, und R1(RO)(O)PCH2ZCH2P(O)(OR)R1 (mit Z = O, S; R = Et, Pri; R1 = Me, Ph) wird beschrieben. Durch Reduktion der Ester sind die acyclischen Diphosphane, R1(H)PCH2ZCH2P(H)R2 (mit Z = O, S; R1 = R2 = H, Me, Ph; R1 = H, R2 = Me) und 1,3,4-Oxadiphospholane bzw. 1,3,4-Thiadiphospholane zugänglich.
    Additional Material: 2 Tab.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/zaac.19905890120
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  • 3
    Electronic Resource
    Electronic Resource
    The peroxisomal import signal of amine oxidase from the yeast Hansenula polymorpha is not universal (1992)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 8 (1992), S. 243-252 
    Details
    ISSN: 0749-503X
    Keywords: Amine oxidase ; peroxisomes ; Hansenula polymorpha ; Saccharomyces cerevisiae ; targeting signal ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Amine oxidase from the yeast Hansenula polymorpha is a peroxisomal protein. The signal for routing of the protein into peroxisomes has not been identified yet. Expression of a mutant amine oxidase in H. Polymorpha has revealed that the C-terminal sequence, which possesses an internal SRL tripeptide, is not involved in targeting (Faber et al., unpublished). We have explored heterologous expression of the amine oxidase gene (AMO) in Saccharomyces cerevisiae to investigate the conservation of peroxisomal targeting pathways between yeasts. Surprisingly, wide-type amine oxidase is not recognized as a peroxisomal protein by S. cerevisiae. The enzyme, which was fully active and acumulated to levels similar to those found in H. polymorpha, stayed entirely in the cytosol. However, fusing a SKL or a SRL sequence to the C-terminus forced the protein at least partially into peroxisomes of the heterologous host. These data suggest that the functional targeting sequence of amine oxidase may differ from the C-terminal peroxisomal targeting signal S/C/A-K/R/H-L (Gould et al., 1989). Contrary to the established tripeptide motif, the amine oxidase targeting signal appears not to be conserved between the different yeast species.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320080402
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  • 4
    Electronic Resource
    Electronic Resource
    The role of ALA-S and ALA-D in regulating porphyrin biosynthesis in a normal and a HEM R+ mutant strain of Saccharomyces cerevisiaeDedicated to Professor Dr Andres O. M. Stoppani on his 75th Birthday. (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 165-173 
    Details
    ISSN: 0749-503X
    Keywords: δ-Aminolevulinate synthase ; δ-aminoleuvulinate dehydratase ; Saccharomyces cerevisiae HEM R+ mutants ; catabolite repression and derepression ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Catabolite repression and derepression on δ-aminolevulinate synthase (ALA-S) and δ-aminolevulinate dehydratase (ALA-D) in a normal yeast strain, D27, and its derived D27/C6 (HEM R+) were investigated. ALA-S and ALA-D activities and intracellular ALA (I-ALA) at different physiological states of the cells were measured. In YPD medium, under conditions of repression and when glucose was exhausted, both strains behaved identically as if the mutation was not expressed. In YPEt medium, however, both ALA-S and ALA-D activities were higher than in YPD, but the I-ALA content and the enzymic activity profiles shown by the two strains were quite different. It appears, therefore, that the mutation causes a deregulation of ALA-S, so that its activity is kept at a high level throughout the cell cycle. This would explain the increased levels of cytochromes present in the mutant. This mutation may affect some regulatory aspect of ALA formation and renders an ALA-S of high activity; moreover, this enzyme species seems to be more stable than in the normal strain.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320090207
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  • 5
    Electronic Resource
    Electronic Resource
    Sequence of a cytochrome c gene from Kluyveromyces lactis and its upstream region (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 201-204 
    Details
    ISSN: 0749-503X
    Keywords: Kluyveromyces lactis ; cytochrome c gene ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The complete sequence of a cytochrome c gene from Kluyveromyces lactis including its upstream region is reported. Sequence of the translated open reading frame is discussed in terms of cytochrome c structural requirements. Putative regulatory signals in the upstream region are described and compared with reported sequences which modulate the expression of respiratory-related yeast genes.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320090211
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  • 6
    Electronic Resource
    Electronic Resource
    Development and tissue-specific distribution of mouse small heat shock protein hsp25 (1993)
    Chichester [u.a.] : Wiley-Blackwell
    Developmental Genetics 14 (1993), S. 103-111 
    Details
    ISSN: 0192-253X
    Keywords: Mouse ; development ; small heat shock protein ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: We have investigated the developmental and tissue-specific distribution of the mouse small hsp25 by immunohistology using an antibody that specifically identifies hsp25. Our analysis shows that the relative amount of hsp25 increases during embryogenesis. Through days 13-20 of embryogenesis, hsp25 accumulation is predominant in the various muscle tissues, including the heart, the bladder, and the back muscles. hsp25 is detectable also in neurons of the spinal cord and the purkinje cells. Furthermore analysis of the closely related α, B-crystallin shows that in several tissues, including the bladder, the notochordal sheath and the eye lens both proteins are coexpressed. Our studies demonstrate that mammalian hsp25 accumulation is developmentally regulated during mouse embryogenesis and support the view of an important functional role of small heat shock proteins in normal cell metabolism. © 1993Wiley-Liss, Inc.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/dvg.1020140204
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  • 7
    Electronic Resource
    Electronic Resource
    Mitochondrial gene defects in patients with NIDDM (1994)
    Springer
    Diabetologia 37 (1994), S. 372-376 
    Details
    ISSN: 1432-0428
    Keywords: Genetics ; diabetes mellitus ; mitochondria ; maternal ; deafness
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Non-insulin-dependent diabetes mellitus (NIDDM) has a strong genetic component and maternal factors have recently been implicated in disease inheritance. The mitochondrial myopathies are a group of diseases which often show maternal inheritance as a result of mtDNA defects; some patients have impaired glucose tolerance. Occasional families with maternally inherited diabetes and deafness associated with a deletion or point mutation of mtDNA have been reported. To assess the importance of mitochondrial gene defects in NIDDM, 150 unrelated diabetic subjects from Wales, UK and 68 unrelated patients with diabetes and at least one affected sibling from England, UK were studied. Southern blot analysis did not show any large mtDNA deletions or duplications. One patient had a mutation in the mitochondrial tRNAleu(UUR) gene at bp 3243. This mutation is commonly associated with the syndrome of mitochondrial encephalomyopathy, lactic acidosis and stroke like episodes (MELAS). Study of this patient and his siblings showed a distinct form of late-onset diabetes associated with nerve deafness but no clinical features of the MELAS syndrome. No diabetic subject was shown to have the mtDNA mutation at position 8344 (tRNAlys) which has previously been described in the syndrome of mitochondrial encephalomyopathy and red-ragged fibres (MERRF). The role of other mitochondrial gene defects in diabetes and the pathophysiological basis of glucose intolerance in patients with the MELAS mutation requires further elucidation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00408473
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  • 8
    Electronic Resource
    Electronic Resource
    Radiological “metamorphosis” in a patient with severe congenital osteogenesis imperfecta (1990)
    Springer
    European journal of pediatrics 149 (1990), S. 403-405 
    Details
    ISSN: 1432-1076
    Keywords: Osteogenesis imperfecta ; Collagen type I ; Radiology, classification ; Genetics
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Congenital osteogenesis imperfecta (OI) was diagnosed by ultrasound in a 31-week-old fetus, and the diagnosis confirmed after delivery by caesarean section at week 36. The baby survived the neonatal period, but failed to thrive, had recurrent respiratory infections and ultimately died at 8 months. Cultured fibroblasts synthesized both normal type I collagen and unstable type I collagen harbouring a structural defect in the α1(I) cyanogen bromide-derived peptide number 8 (CB8) region of the molecule, indicating a heterozygous dominant mutation. A+ birth, the radiological picture was that of the “thin bone”-type of congenital OI (OI type IIB/III in the Sillence classification); at the age of 12 weeks ribs and long bones had undergone a marked expansion giving a very different picture, that of the “thick bone”-type congenital OI (OI type IIA). The mechanism responsible for this change in bone structure is not known, but fractures and callus formation are unlikely to be the only factors. Caution is needed in the interpretation of radiographs of newborns with OI for prognostic or genetic purposes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02009659
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  • 9
    Electronic Resource
    Electronic Resource
    A gene in the HLA class I region contributes to susceptibility to IDDM in the Finnish population (1994)
    Springer
    Diabetologia 37 (1994), S. 937-944 
    Details
    ISSN: 1432-0428
    Keywords: Genetics ; haplotype ; HLA-A ; HLA-DQ ; HLA-DR ; tumour necrosis factor ; diabetes mellitus
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary In Finland the haplotype A2, Cw1, B56, DR4, DQ8 is the third most common haplotype in insulin-dependent diabetic (IDDM) patients and has the highest haplotype-specific absolute risk for IDDM. Cw1, B56, DR4, DQ8 haplotypes containing HLA-A alleles other than A2 are infrequent in the population and are not associated with IDDM. Comparison of the A2 and non-A2 haplotypes at the DNA level showed that they were identical at HLA-B,-DR, and -DQ loci. Evidence that class I alleles confer susceptibility to IDDM was obtained from the two HLA-C, -B, -DR and -DQ haplotypes most frequently found in IDDM patients in Finland. A24, A3 and A2 on the Cw3, B62, DR4, DQ8 haplotype, and A28, A2 and A1 on the Cw7, B8, DR3, DQ2 were all found to be associated with IDDM. In Finland these seven haplotypes, including A2, Cw1, B56, DR4, DQ8, account for 33% of diabetic haplotypes and 10.3% of non-diabetic haplotypes (p〈0.00001). The contribution of the class I region to IDDM susceptibility was also apparent in those IDDM patients lacking the disease-predisposing class II alleles. Significantly more non-DR3/non-DR4 IDDM patients (47 of 55) possessed two of the IDDM-associated HLA-A alleles compared to non-DR3/non-DR4 control subjects (40 of 58; p=0.038). Moreover, IDDM patients confirmed by oligotyping as unable to form a ‘diabetes-susceptibility’ DQ heterodimer, tended to possess two diabetes-associated HLA-A alleles (12 of 13) compared to control subjects (12 of 20; p=0.056).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00400951
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  • 10
    Electronic Resource
    Electronic Resource
    HLA class II genes and antibodies against recombinant U1-nRNP proteins in patients with systemic lupus erythematosus (1994)
    Springer
    Rheumatology international 14 (1994), S. 63-69 
    Details
    ISSN: 1437-160X
    Keywords: Systemic lupus erythematosus ; Recombinant U1-nRNP proteins ; Genetics
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract To investigate a possible involvement of HLA-class II alleles in the genetic predisposition for the formation of anti-U1-nRNP antibody in systemic lupus erythematosus (SLE), genomic DNA of 178 patients was typed for the DRB1, DQA1 and DQB1 alleles using a polymerase chain reaction (PCR) and non-radioactive-oligonucleotide typing. Antibodies against recombinant U1-nRNP proteins (U1-A- U1-C-and 70K-protein) were determined by ELISA. Anti-U1-C antibody was found in 26 (14.7%), anti-U1-A in 34 (19.2%) and anti-70K in 17 (9.6%) patients. A joint occurrence was observed for these antibodies against the recombinant U1-nRNP proteins: anti-U1-C and anti-U1-A antibodies occurred together more frequently than alone and than together with anti-U1-70K antibodies. The frequency of DRB1 * 04 was slightly increased in the patients with anti-U1-C as compared to the patients without anti-U1-C (P〈0.05, Pcorr=n.s., RR=2.4). The DQA1 * 0301 allele, which is in linkage disequilibrium with DRB1 * 04, is found more frequently in anti-U1-C-positive than in antibody-negative patients. The DQB1 * 0303 allele, detected in 12 of 176 SLE patients, was absent in the patients with any of the antibodies against the U1-nRNP proteins. All these deviations may be due to chance alone. We concluded that the presence of antibodies against recombinant U1-nRNP proteins was not significantly associated with any HLA DRB1, DQA1 and DQB1 allele in our group of SLE patients.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00300249
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