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  • 1
    Online Resource
    Online Resource
    Targeting Carbonic Anhydrases. (2014)
    London :Future Science Ltd,
    Details
    Keywords: Carbonic anhydrase. ; Electronic books.
    Description / Table of Contents: This book brings together a series of excellent reviews from world-leading groups in the field of microwave-mediated chemistry.
    Type of Medium: Online Resource
    Pages: 1 online resource (175 pages)
    ISBN: 9781909453906
    URL: https://ebookcentral.proquest.com/lib/geomar/detail.action?docID=5092531
    DDC: 362.29
    Language: English
    Note: Intro -- Targeting carbonic anhydrases -- Overview of carbonic anhydrase families/isoforms -- Classical sulfonamides and their bioisosters as carbonic anhydrase inhibitors -- Next-generation primary sulfonamide carbonic anhydrase inhibitors -- Next-generation secondary/tertiary sulfonamide carbonic anhydrase inhibitors -- Next-generation polyamine human carbonic anhydrase inhibitors -- Next-generation phenol carbonic anhydrase inhibitors -- Coumarins that inhibit carbonic anhydrase -- Next-generation dithiocarbamate carbonic anhydrase inhibitors -- Protozoan, fungal and bacterial carbonic anhydrases targeting for obtaining anti-infectives -- Amine, amino acid and oligopeptide carbonic anhydrase activators -- Targeting carbonic anhydrases in biotechnology -- _GoBack -- _GoBack -- _GoBack -- _ENREF_2 -- _ENREF_3 -- _ENREF_4 -- _ENREF_5 -- _ENREF_6 -- _ENREF_7 -- _ENREF_8 -- _ENREF_9 -- _ENREF_10 -- _ENREF_11 -- _ENREF_14 -- _ENREF_15 -- _ENREF_16 -- _ENREF_17 -- _ENREF_18 -- _ENREF_19 -- _ENREF_20 -- _ENREF_21 -- _ENREF_22 -- _ENREF_23 -- _ENREF_24 -- _ENREF_25 -- _ENREF_26 -- _ENREF_27 -- _ENREF_28 -- _ENREF_29 -- _ENREF_30 -- _ENREF_31 -- _ENREF_32 -- _ENREF_33 -- _ENREF_34 -- _ENREF_35 -- _ENREF_36 -- _ENREF_37 -- _ENREF_38 -- _ENREF_39 -- _ENREF_40 -- _ENREF_41 -- _ENREF_42 -- _GoBack -- _GoBack -- _GoBack -- _GoBack -- _ENREF_2 -- _ENREF_3 -- _ENREF_4 -- _ENREF_5 -- _ENREF_6 -- _ENREF_7 -- _ENREF_8 -- _ENREF_9 -- _ENREF_10 -- _ENREF_11 -- _ENREF_12 -- _ENREF_13 -- _ENREF_14 -- _ENREF_15 -- _ENREF_16 -- _ENREF_17 -- _ENREF_18 -- _ENREF_19 -- _GoBack -- _GoBack -- _ENREF_2 -- _ENREF_3 -- _ENREF_4 -- _ENREF_5 -- _ENREF_6 -- _ENREF_7 -- _ENREF_8 -- _ENREF_9 -- _ENREF_10 -- _ENREF_11 -- _ENREF_12 -- _ENREF_13 -- _ENREF_14 -- _ENREF_15 -- _ENREF_16 -- _ENREF_17 -- _ENREF_18 -- _ENREF_19 -- _ENREF_20 -- _GoBack -- _ENREF_2 -- _ENREF_3 -- _ENREF_4. , _ENREF_5 -- _ENREF_6 -- _ENREF_7 -- _ENREF_8 -- _ENREF_9 -- _ENREF_10 -- _ENREF_11 -- _ENREF_12 -- _ENREF_13 -- _ENREF_14 -- _ENREF_15 -- _ENREF_16 -- _ENREF_17 -- _ENREF_18 -- _ENREF_19 -- _ENREF_20.
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  • 2
    Electronic Resource
    Electronic Resource
    Tissue-specific regulation of metallothionein and metallothionein mRNA accumulation in the Antarctic notothenioid, Notothenia coriiceps (2000)
    Springer
    Polar biology 23 (2000), S. 17-23 
    Details
    ISSN: 1432-2056
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The distribution of metallothionein and metallothionein mRNA was examined in brain, liver and kidney of the red-blooded Antarctic fish Notothenia coriiceps. Basal levels of metallothionein were detected by silver saturation assay; the analysis showed large differences in the metallothionein content, with an increasing amount in kidney, liver and brain, respectively. Reverse transcriptase-mediated polymerase chain reaction was used to amplify two distinct metallothionein cDNA species from RNA extracted from the three tissues examined. Northern blot analysis revealed a high constitutive expression of metallothionein mRNA in kidney, in spite of the low metallothionein content found in this tissue. The analysis of the distribution of the two metallothionein transcripts, termed MT-1 and MT-2, in the tissues showed that the MT-2 transcript was the major form of the metallothionein mRNA in kidney and brain, whilst in liver the expression levels of the two metallothionein transcripts were comparable. This tissue-specific expression of isometallothioneins in the Antarctic fish suggests the presence of an organ-specific regulation of the metallothionein genes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s003000050003
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    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Susceptibility to Heavy Metals and Cadmium Accumulation in Aerobic and Anaerobic Thermophilic Microorganisms Isolated from Deep-Sea Hydrothermal Vents (2000)
    Springer
    Current microbiology 41 (2000), S. 201-205 
    Details
    ISSN: 1432-0991
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Thirty thermophilic strains isolated from heavy metal-rich hydrothermal vent sites at Lau Basin were tested for their susceptibility to cadmium, zinc, cobalt, and nickel. The 14 aerobic spore formers belonging to the genus Bacillus, 6 anaerobic fermenters from the order Thermotogales, and 10 anaerobic sulfur reducers from the order Thermococcales could be clearly distinguished according to their metal susceptibilities. The Thermococcales were found to exhibit the highest resistance to cadmium and zinc, whereas Thermotogales were highly sensitive to these metals. In contrast, the Thermotogales displayed the highest resistance to cobalt ions. No clear distinction could be established between the metal susceptibilities of these strains and seven reference organisms used for comparative studies. Cadmium resistance, slightly inducible in some cadmium-resistant bacilli, was not plasmid mediated. The amount of cadmium immobilized by the Thermotogales was related to their level of resistance to this metal.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s00284431056
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    Paper (German National Licenses)
    Fulltext
  • 4
    Electronic Resource
    Electronic Resource
    Crystal structure of the bovine α-chymotrypsin:kunitz inhibitor complex. An example of multiple protein:protein recognition sitesThis paper is dedicated to Professor A. Ballio on the occasion of his 75th birthday. (1997)
    Chicester [u.a.] : Wiley-Blackwell
    Journal of Molecular Recognition 10 (1997), S. 26-35 
    Details
    ISSN: 0952-3499
    Keywords: bovine α-chymotrypsin ; bovine basic pancreatic trypsin inhibitor (Kunitz-type inhibitor) ; serine proteinase:Kunitz inhibitor complex ; crystal structure ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: The crystal structure of bovine α-chymotrypsin (α-CHT) in complex with the bovine basic pancreatic trypsin inhibitor (BPTI) has been solved and refined at 2.8 Å resolution (R-factor=0.18). The proteinase:inhibitor complex forms a compact dimer (two α-CHT and two BPTI molecules), which may be stabilized by surface-bound sulphate ions, in the crystalline state. Each BPTI molecule, at opposite ends, is contacting both proteinase molecules in the dimer, through the reactive site loop and through residues next to the inhibitor's C-terminal region. Specific recognition between α-CHT and BPTI occurs at the (re)active site interface according to structural rules inferred from the analysis of homologous serine proteinase:inhibitor complexes. Lys15, the P1 residue of BPTI, however, does not occupy the α-CHT S1 specificity pocket, being hydrogen bonded to backbone atoms of the enzyme surface residues Gly216 and Ser217. © 1997 John Wiley & Sons, Ltd.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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    Paper (German National Licenses)
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