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  • Springer  (37)
  • American Society of Hematology  (16)
  • Nature Publishing Group  (5)
  • 1
    Electronic Resource
    Electronic Resource
    Hypersensitivity to nonsteroidal anti-inflammatory drugs (1995)
    [s.l.] : Nature Publishing Group
    Nature medicine 1 (1995), S. 2-4 
    Details
    ISSN: 1546-170X
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Medicine
    Notes: [Auszug] To the editor — Nonsteroidal anti-inflammatory drugs (NSAIDs) are a widely used class of compounds that are prescribed as analgesic, antipyretic and anti-inflammatory agents1. NSAIDs can elicit potentially fatal hypersensitivity reactions (including anaphylaxis, bronchospasm and ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/nm0195-2b
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  • 2
    Electronic Resource
    Electronic Resource
    Molecular weights of antihaemophilic factor and von Willebrand factor proteins in human plasma (1976)
    [s.l.] : Nature Publishing Group
    Nature 263 (1976), S. 612-613 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] These interpretations do not adequately explain certain clinical and laboratory observations. For example, von Willebrand patients infused with factor VIII preparations show a secondary rise in AHF activity when no measurable VWF activity or factor VIII-related antigen is present10. The molecular ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/263612a0
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  • 3
    Electronic Resource
    Electronic Resource
    Ant navigation Priming of visual route memories (2005)
    [s.l.] : Nature Publishing Group
    Nature 438 (2005), S. 302-302 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Ants travelling to and fro between their nest and a foraging area may follow stereotyped foodward and homeward routes that are guided by different visual and directional memory sequences. Honeybees are known to fly a feeder-to-hive or hive-to-feeder vector according to whether or not they have ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/438302a
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  • 4
    Electronic Resource
    Electronic Resource
    Enzymatic Release of Phosphate from Rat Molar Enamel by Phosphoprotein Phosphatase (1969)
    [s.l.] : Nature Publishing Group
    Nature 223 (1969), S. 520-521 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] From the investigations of Glimcher1 and Veis2 it is now clear that mineralized tissue, both embryonic and mature, whether bone, dentin or enamel, all share a common feature: a phosphoprotein matrix. These specialized proteins, in common with casein and other phosphoproteins, can be phosphorylated ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/223520a0
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  • 5
    Electronic Resource
    Electronic Resource
    Laboratory Colonization of the Horn Fly, Hæmatobia irritans (L.) (1962)
    [s.l.] : Nature Publishing Group
    Nature 196 (1962), S. 191-192 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] For each test diet, 480 ml. of blood was drawn from a steer into a vacuum transfusion bottle containing 120 ml. of ACD* anticoagulant solution. The blood was mixed immediately with the other ingredients and the unused portion stored under refrigeration. For each test diet, 10 male and 10 female ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/196191b0
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  • 6
    Electronic Resource
    Electronic Resource
    Gm-3.2, A new granulocyte/macrophage alloantigen (1985)
    Springer
    Immunogenetics 21 (1985), S. 61-70 
    Details
    ISSN: 1432-1211
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract A monoclonal antibody defining a unique mouse neutrophil cell-surface antigen, Gm-3.2, is described. Gm-3.2 is found on all neutrophils in peritoneal exudates and in bone marrow, and is also present on macrophages activated by thioglycolate but is absent from lymphoid, kidney, liver, heart, and red cells. Gm-3.2 is a differentiation antigen of myeloid cells, as granulocyte/macrophage colony-forming cells are Gm-3.2− while mature neutrophils are Gm-3.2+. Strain distribution pattern analysis shows linkage of the Gm-3 locus to the Ly-4, B2m, H-3 complex on chromosome 2.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00372242
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  • 7
    Electronic Resource
    Electronic Resource
    Hormonal control of FAT cells adenylate cyclase (1976)
    Springer
    Molecular and cellular biochemistry 13 (1976), S. 141-146 
    Details
    ISSN: 1573-4919
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Summary Fat cells were preincubated for 2 h in the presence and absence of growth hormone (GH) and Dexamethasone (Dex) before the addition of increasing concentrations of either epinephrine, theophylline or glucagon and final incubation of the cells for an additional 5 minutes. GH and Dex increased by 85%, 28% and 72%, respectively, the cAMP levels reached in the sole presence of 10−5 m epinephrine, 10−2 m theophylline or 5 × 10−5 m glucagon. An adenylate cyclase particulate preparation shows that epinephrine decreases Km from 2mm to 0.6mm and increases Vmax and the strength of interaction value (n) from 0.91 to 1.75.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01731776
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  • 8
    Electronic Resource
    Electronic Resource
    Calorimetric and spectroscopic examination of the solution phase structures of prekallikrein binding domain peptides of high molecular weight kininogen (1991)
    Springer
    The protein journal 10 (1991), S. 301-311 
    Details
    ISSN: 1573-4943
    Keywords: Circular dichroism ; differential scanning calorimetry ; fluorescence emission spectroscopy ; high molecular weight kininogen ; peptide conformation ; prekallikrein ; 2D-NMR
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Unique sequence-binding sites are exposed on the surface of high molecular weight kininogen which complex prekallikrein or factor XI with high affinity and specificity. A sequence comprising 31 residues of the mature kininogen molecule (Asp565-Lys595) retains full binding activity for prekallikrein (K D =20 nM) and assumes a complex folded structure in solution which is stabilized by long-range interactions between N- and C-terminal residues. The sequence Trp569-Lys595 (27 residues) shows only 28% of this binding affinity and lacks the key structural features required for protein recognition (Scarsale, J. N., and Harris, R. B.,J. Prot. Chem. 9, 647–659, 1990). We were thus able to predict that N- or C-terminal truncations of the binding-site sequence would disrupt the conformational integrity required for binding. Two new peptides of 20- and 22- residues have now been synthesized and their solution phase structures examined. These peptides are N- and C-terminal truncations, respectively, of the 27-residue sequence and correspond to the sequences Asp576-Lys595 and Trp569-Asp590 of high molecular weight kininogen. The results of fluorescence emission and circular dichroism (CD) spectroscopies in the range 25–90°C and from differential scanning calorimetry (DSC) all substantiate the idea that the C-terminal truncation peptide binds prekallikrein 35-fold poorer than the 31-residue peptide because it is relatively unoredered and possesses a less stable structure. Surprisingly, the N-terminal truncation peptide (20-mer) shows structural stability even at elevated temperatures and, like the 31-residue peptide, undergoes cold-induced denaturation observable in the DSC. 2D-NMR analysis of the 20-residue peptide revealed two distinct structures; one conformer possesses a more compact, folded structure than the other. However, the predicted structures assumed by either conformer are very different from those of either the 31- or 27-residue peptides. Hence, the binding affinity of the 20-residue peptide is 60-fold poorer than that for the 31-residue peptide because it assumes a nonproductive binding conformation(s).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01025629
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  • 9
    Electronic Resource
    Electronic Resource
    Preparations of Ψ-peptide bond and peptide-aldehyde inhibitors of atrial granule serine proteinase, a candidate processing enzyme of pro-atrial natriuretic factor (1995)
    Springer
    The protein journal 14 (1995), S. 431-440 
    Details
    ISSN: 1573-4943
    Keywords: ANF ; atrial natriuretic factors ; atrial granule serine proteinase ; peptide inhibitors ; peptide aldehydes ; processing enzymes ; pseudo-bond inhibitors ; serine proteinase ; Swern oxidation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Pseudo-peptide bond inhibitors (ψ-bond inhibitors) and peptide-aldehyde inhibitors of atrial granule serine proteinase, the candidate processing enzyme of pro-atrial natrieuretic factor, are prepared in high yield and purity by novel synthetic routes. The ψ-bond compounds retain essential residues for enzyme binding, but place the enzyme inhibition site in the midst of the peptide sequence. Thus, Bz-APR-ψ-LR and Bz-APR-ψ-SLRR can be considered “readthrough inhibitors” of atrial granule serine proteinase. The most potent ψ-peptide, Bz-APR-ψ-SLRR (IC50=250 ΜM), is about fivefold less potent than the best peptide-aldehyde inhibitor (EACA-APR-CHO), and both the ψ-bond and peptide-aldehyde compounds are competitive, reversible inhibitors of the enzyme. The ψ-bond peptides containing two C-terminal Arg residues are three-to tenfold more potent than the analogous compounds containing only one C-terminal Arg residue, confirming the importance of both Arg residues in the enzyme processing recognition site. As expected, because of their moderate potencies, the ψ-peptides are not useful affinity ligands for purification of atrial granule serine proteinase, but both peptide aldehydes are effective affinity ligands [Damodaran and Harris (1995),J. Protein Chem., this issue].
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01888137
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  • 10
    Electronic Resource
    Electronic Resource
    N-terminal sequence analysis of atrial granule serine proteinase purified by affinity chromatography (1995)
    Springer
    The protein journal 14 (1995), S. 441-449 
    Details
    ISSN: 1573-4943
    Keywords: Affinity chromatography ; ANF ; atrial natriuretic factors ; atrial granule serine proteinase ; N-terminal sequence determination ; peptide inhibitors ; peptide aldehydes ; processing enzymes ; protein purification ; serine proteinase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Atrial granule serine proteinase is considered the leading candidate endoproteolytic processing enzyme of pro-atrial natriuretic factor. Its cleavage specificity is directed toward a monobasic amino acid processing site, and as such, the atrial enzyme is distinguished from the family of prohormone convertases which act at dibasic amino acid processing sites. To delineate the molecular mechanisms which distinguish monobasic from dibasic amino acid-directed processing enzymes, pure atrial enzyme is needed for sequence determination leading to molecular cloning, and for preparation of antisera. An affinity chromatography purification scheme seemed a logical modification of our established procedures to yield suitable amounts of enzyme for further studies. Surprisingly, pseudo-peptide bond inhibitors of the atrial enzyme [Damodaran and Harris (1995),J. Protein Chem., this issue] formed ineffective affinity ligands, even though these compounds contain essential residues on either side of what would be the scissile bond in a peptide substrate. On the other hand, tripeptide aldehydes (based on the substrate recognition sequence of the atrial enzyme) linked to Sepharose formed effective affinity matrices, permitting purification of the enzyme in a single step from a subcellular fraction enriched for atrial granules and lysosomes. Hence, the enzyme was purified 2000-fold in 90% overall yield, and subjected to N-terminal sequence analysis through 26 residues. The sequence determined, XXPEAAGLPG[R, L]GNPVP[F, G]R[Q, I]XY[G, E]XR(N, A]V, indicates that the atrial enzyme is unique, showing little sequence homology to other proteins in the database.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01888138
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