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  • 1
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    Triggers, targets and treatments for thrombosis (2008)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2008-02-22
    Description: Thrombosis--localized clotting of the blood--can occur in the arterial or the venous circulation and has a major medical impact. Acute arterial thrombosis is the proximal cause of most cases of myocardial infarction (heart attack) and of about 80% of strokes, collectively the most common cause of death in the developed world. Venous thromboembolism is the third leading cause of cardiovascular-associated death. The pathogenic changes that occur in the blood vessel wall and in the blood itself resulting in thrombosis are not fully understood. Understanding these processes is crucial for developing safer and more effective antithrombotic drugs.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2848509/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2848509/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mackman, Nigel -- R01 HL095096/HL/NHLBI NIH HHS/ -- R01 HL095096-01/HL/NHLBI NIH HHS/ -- England -- Nature. 2008 Feb 21;451(7181):914-8. doi: 10.1038/nature06797.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Hematology/Oncology, Department of Medicine, University of North Carolina, Chapel Hill, North Carolina 27599, USA. nmackman@med.unc.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18288180" target="_blank"〉PubMed〈/a〉
    Keywords: Anticoagulants/pharmacology ; Atherosclerosis/complications/pathology ; Drug-Eluting Stents ; Humans ; Platelet Aggregation Inhibitors/pharmacology ; Thrombosis/complications/*metabolism/pathology/*therapy ; Venous Thrombosis/complications/pathology/therapy
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 2
    Electronic Resource
    Electronic Resource
    Escherichia coli haemolysin forms voltage-dependent ion channels in lipid membranes
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Biomembranes 905 (1987), S. 109-117 
    Details
    ISSN: 0005-2736
    Keywords: Bilayer membrane ; Hemolysin ; Ion channel ; Phospholipid bilayer ; Voltage-dependent ion channel
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine , Physics
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0005-2736(87)90014-9
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Conservation of tissue factor primary sequence among three mammalian species
    Amsterdam : Elsevier
    Gene 98 (1991), S. 265-269 
    Details
    ISSN: 0378-1119
    Keywords: Recombinant DNA ; blood coagulation ; conserved cysteines ; human ; murine ; rabbit cDNA libraries
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0378-1119(91)90184-D
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  • 4
    Electronic Resource
    Electronic Resource
    The C-terminal, 23 kDa peptide of E. coli haemolysin 2001 contains all the information necessary for its secretion by the haemolysin (Hly) export machinery
    Amsterdam : Elsevier
    FEBS Letters 204 (1986), S. 331-335 
    Details
    ISSN: 0014-5793
    Keywords: (E. coli) Hemolysin C-terminal secretion signal Expression vector Protein
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0014-5793(86)80838-9
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  • 5
    Electronic Resource
    Electronic Resource
    Characterisation of HlyC and mechanism of activation and secretion of haemolysin from E. coli 2001
    Amsterdam : Elsevier
    FEBS Letters 187 (1985), S. 339-344 
    Details
    ISSN: 0014-5793
    Keywords: Hemolysin secretion ; Post-translational modification ; hlyC sequence
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0014-5793(85)81272-2
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  • 6
    Electronic Resource
    Electronic Resource
    Genetics and biochemistry of the assembly of proteins into the outer membrane of E. coli
    Amsterdam : Elsevier
    Progress in Biophysics and Molecular Biology 49 (1987), S. 89-115 
    Details
    ISSN: 0079-6107
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Physics
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0079-6107(87)90010-1
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  • 7
    Electronic Resource
    Electronic Resource
    Identification of polypeptides required for the export of haemolysin 2001 from E. coli (1985)
    Springer
    Molecular genetics and genomics 201 (1985), S. 529-536 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary We have identified the polypeptides encoded by the haemolysin export genes from a haemolytic determinant 2001 carried by pLG570. This was previously cloned from an E. coli strain, serotype 04 isolated from a human urinary tract infection. Subclones from the recombinant plasmid pLG570 carrying hlyD analysed in vitro and in minicells showed that this gene is transcribed from an independent promoter and encodes a 53 Kd polypeptide. In contrast, detectable levels of the gene products encoded by hlyB were only observed when transcription presumably emanated from a vector promoter. This gene was found to encode at least two polypeptides apparently expressed from alternative translational start sites within a single reading frame. In minicells the major product was a 66 Kd polypeptide whilst after expression in nitro the major product was a 46 Kd polypeptide. Transposon mutagenesis leading to the synthesis of the expected truncated polypeptides was used to confirm the identity of the hlyD and the two hlyB products. Preliminary results suggest that the majority of the 53 Kd polypeptide is located in the inner membrane when cell envelopes from minicells and maxicells were fractionated using sarkosyl, although residual amounts of the 53 Kd polypeptide were also found in the outer membrane.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00331351
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  • 8
    Electronic Resource
    Electronic Resource
    The carboxy-terminal region of haemolysin 2001 is required for secretion of the toxin fromEscherichia coli (1986)
    Springer
    Molecular genetics and genomics 205 (1986), S. 127-133 
    Details
    ISSN: 1617-4623
    Keywords: Haemolysin ; Secretion
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary As a first step in the detailed analysis of the mechanism of secretion of haemolysin, we sought to identify sequences or domains within haemolysin A (HlyA) that are essential for its secretion. For this purpose we examined the properties of a deletion and Tn5 insertions into the region of theHlyA gene encoding the C-terminal part of the protein, since both of these are relatively simple to generate. We showed that removal of 27 amino acids from the C-terminus of HlyA is sufficient to inhibit secretion drastically, although the residual polypeptide is still haemolytically active. Cellular fractionation studies showed that haemolytic activity does not accumulate in large amounts within the periplasmic space during normal secretion. More significantly, activity does not appear to accumulate within this compartment when the export functionshlyB andhlyD are removed. These results are consistent with a mechanism in which interaction of the C-terminus of HlyA with the secretion machinery, located in the inner membrane, is followed by direct transfer of haemolysin to the medium.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02428042
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  • 9
    Electronic Resource
    Electronic Resource
    Regulation of haemolysin synthesis in E. coli determined by HLY genes of human origin (1985)
    Springer
    Molecular genetics and genomics 199 (1985), S. 111-116 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary We have previously reported the secretion of a 107K polypeptide into the medium from a haemolytic E. coli K12 strain (Mackman and Holland 1984a). In addition, we demonstrated that haemolysin production was correlated with the presence of this polypeptide in the growth medium in a large number of E. coli isolates of human and animal origin (Mackman and Holland 1984b). In this paper we confirm that the 107K polypeptide is indeed haemolysin: both haemolytic activity and the 107K polypeptide show a similar pattern of accumulation during the growth cycle; identical levels are produced in three different growth media; they have the same half-life in minimal medium. The results also show that the expression of haemolysin is not influenced by the growth medium or subject to catabolite repression. However, expression is apparently switched off as cells enter the late exponential phase of growth. Finally, we present data indicating that the previously reported variation in haemolysin production in different media is entirely due to the instability of the haemoolysin itself. Degradation of the 107K polypeptide in the medium was accompanied by the accumulation of a major breakdown product of 60K.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00327519
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  • 10
    Electronic Resource
    Electronic Resource
    Genetical and functional organisation of the Escherichia coli haemolysin determinant 2001 (1985)
    Springer
    Molecular genetics and genomics 201 (1985), S. 282-288 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary We have identified gene products corresponding to hlyC, hlyA and hlyD encoded by the Escherichia coli haemolytic determinant 2001 of human origin cloned into the recombinant plasmid pLG570. The product of hlyC is required for the “activation” of the inactive 107K polypeptide encoded by the hlyA gene. the activated 107K protein constitutes the active haemolysin secreted into the medium. hlyB and hlyD are separate regions defined by complementation studies and encode functions essential for the export of haemolysin with hlyD encoding a 53K protein. Complementation studies using subclones and Tn5 insertions into pLG570 have revealed the presence of two major promoters upstream of hlyC and hlyD which transcribe the four hly genes in the same direction. Finally, we were able to reconstitute the complete haemolysin system from three different plasmids encoding hlyC, hlyA and hlyB+hlyD, respectively.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00425672
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