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  • 1
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    Role of Escherichia coli curli operons in directing amyloid fiber formation (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-02-02
    Description: Amyloid is associated with debilitating human ailments including Alzheimer's and prion diseases. Biochemical, biophysical, and imaging analyses revealed that fibers produced by Escherichia coli called curli were amyloid. The CsgA curlin subunit, purified in the absence of the CsgB nucleator, adopted a soluble, unstructured form that upon prolonged incubation assembled into fibers that were indistinguishable from curli. In vivo, curli biogenesis was dependent on the nucleation-precipitation machinery requiring the CsgE and CsgF chaperone-like and nucleator proteins, respectively. Unlike eukaryotic amyloid formation, curli biogenesis is a productive pathway requiring a specific assembly machinery.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2838482/" 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/PMC2838482/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chapman, Matthew R -- Robinson, Lloyd S -- Pinkner, Jerome S -- Roth, Robyn -- Heuser, John -- Hammar, Marten -- Normark, Staffan -- Hultgren, Scott J -- 1 F32 AI10502-01A1/AI/NIAID NIH HHS/ -- AI29549/AI/NIAID NIH HHS/ -- AI48689/AI/NIAID NIH HHS/ -- DK51406/DK/NIDDK NIH HHS/ -- F32 AI010502/AI/NIAID NIH HHS/ -- F32 AI010502-03/AI/NIAID NIH HHS/ -- NIA P50 AG05681-17/AG/NIA NIH HHS/ -- New York, N.Y. -- Science. 2002 Feb 1;295(5556):851-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Microbiology and Microbial Pathogenesis, Box 8230, Washington University School of Medicine, 660 South Euclid Avenue, St. Louis, MO 63110, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11823641" target="_blank"〉PubMed〈/a〉
    Keywords: Adhesins, Bacterial/chemistry/genetics/metabolism/ultrastructure ; Amyloid/chemistry/*metabolism/ultrastructure ; Bacterial Proteins/chemistry/genetics/*metabolism/ultrastructure ; Biopolymers ; Circular Dichroism ; Congo Red/metabolism ; Escherichia coli/genetics/*metabolism ; Escherichia coli Proteins/chemistry/genetics/*metabolism/ultrastructure ; Mutation ; *Operon ; Protein Structure, Secondary ; Protein Subunits
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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    Coordinate regulation of beta-lactamase induction and peptidoglycan composition by the amp operon (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-01-11
    Description: The amp operon, which is located on the Escherichia coli chromosome, modulates the induction of plasmid-borne beta-lactamase genes by extracellular beta-lactam antibiotics. This suggests that the gene products AmpD and AmpE may function in the transduction of external signals. beta-Lactam antibiotics are analogs of cell wall components that can be released during cell wall morphogenesis of enterobacteria. The amp operon was studied to determine its importance in signal transduction during cell wall morphogenesis. The peptidoglycan compositions of amp mutants were determined by high-performance liquid chromatography and fast atom bombardment mass spectrometry. When a chromosomal or plasmid-borne copy of ampD was present, the amount of pentapeptide-containing muropeptides in the cell wall increased upon addition of the cell wall constituent diaminopimelic acid to the growth medium. These results suggest that beta-lactamase induction and modulation of the composition of the cell wall share elements of a regulatory circuit that involves AmpD. Escherichia coli requires AmpD to respond to extracellular signaling amino acids, such as diaminopimelic acid, and this signal transduction system may regulate peptidoglycan composition in response to cell wall turnover products.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tuomanen, E -- Lindquist, S -- Sande, S -- Galleni, M -- Light, K -- Gage, D -- Normark, S -- AI23459/AI/NIAID NIH HHS/ -- AI27913/AI/NIAID NIH HHS/ -- DRR00480/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1991 Jan 11;251(4990):201-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Microbiology, Rockefeller University, New York, NY 10021.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1987637" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacterial Proteins/*genetics/metabolism ; Carboxypeptidases/metabolism ; Cell Wall/metabolism ; Diaminopimelic Acid/pharmacology ; Enzyme Induction ; Escherichia coli/*genetics/metabolism ; *Gene Expression Regulation/drug effects ; Genotype ; Membrane Proteins/*genetics/metabolism ; Molecular Sequence Data ; Mutation ; *N-Acetylmuramoyl-L-alanine Amidase ; Oligopeptides/metabolism ; *Operon ; Peptidoglycan/metabolism ; Plasmids ; Signal Transduction ; Spectrometry, Mass, Fast Atom Bombardment ; beta-Lactamases/*biosynthesis/genetics
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
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    Common themes amid diversity (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-05-02
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Normark, S -- Wolf-Watz, H -- New York, N.Y. -- Science. 1997 May 2;276(5313):659.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9157538" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Physiological ; Animals ; Bacteria/genetics ; *Bacterial Physiological Phenomena ; *Ecosystem ; Environmental Microbiology ; Genes, Bacterial ; Humans
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
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    Functional adaptation of BabA, the H. pylori ABO blood group antigen binding adhesin (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-07-27
    Description: Adherence by Helicobacter pylori increases the risk of gastric disease. Here, we report that more than 95% of strains that bind fucosylated blood group antigen bind A, B, and O antigens (generalists), whereas 60% of adherent South American Amerindian strains bind blood group O antigens best (specialists). This specialization coincides with the unique predominance of blood group O in these Amerindians. Strains differed about 1500-fold in binding affinities, and diversifying selection was evident in babA sequences. We propose that cycles of selection for increased and decreased bacterial adherence contribute to babA diversity and that these cycles have led to gradual replacement of generalist binding by specialist binding in blood group O-dominant human populations.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Aspholm-Hurtig, Marina -- Dailide, Giedrius -- Lahmann, Martina -- Kalia, Awdhesh -- Ilver, Dag -- Roche, Niamh -- Vikstrom, Susanne -- Sjostrom, Rolf -- Linden, Sara -- Backstrom, Anna -- Lundberg, Carina -- Arnqvist, Anna -- Mahdavi, Jafar -- Nilsson, Ulf J -- Velapatino, Billie -- Gilman, Robert H -- Gerhard, Markus -- Alarcon, Teresa -- Lopez-Brea, Manuel -- Nakazawa, Teruko -- Fox, James G -- Correa, Pelayo -- Dominguez-Bello, Maria Gloria -- Perez-Perez, Guillermo I -- Blaser, Martin J -- Normark, Staffan -- Carlstedt, Ingemar -- Oscarson, Stefan -- Teneberg, Susann -- Berg, Douglas E -- Boren, Thomas -- P30 DK52574/DK/NIDDK NIH HHS/ -- R01 AI38166/AI/NIAID NIH HHS/ -- R01 DK53727/DK/NIDDK NIH HHS/ -- R01 DK63041/DK/NIDDK NIH HHS/ -- R03 AI49161/AI/NIAID NIH HHS/ -- R0IGM62370/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2004 Jul 23;305(5683):519-22.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Odontology, section of Oral Microbiology, Umea University, SE-901 87 Umea, Sweden.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15273394" target="_blank"〉PubMed〈/a〉
    Keywords: ABO Blood-Group System/*metabolism ; Adaptation, Biological ; Adhesins, Bacterial/chemistry/*genetics/immunology/*metabolism ; Alleles ; *Bacterial Adhesion ; Base Sequence ; Binding Sites ; Evolution, Molecular ; Fucose/metabolism ; Gastric Mucosa/microbiology ; Helicobacter Infections/microbiology ; Helicobacter pylori/genetics/immunology/*physiology ; Humans ; Indians, South American ; Lewis Blood-Group System/metabolism ; Molecular Sequence Data ; Mutation ; Peru ; Phenotype ; Phylogeny ; Protein Binding ; Selection, Genetic ; Transformation, Bacterial
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
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    Microbiology. A pathogen attacks while keeping up defense (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-02-26
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Normark, Staffan -- Nilsson, Christina -- Normark, Birgitta Henriques -- New York, N.Y. -- Science. 2005 Feb 25;307(5713):1211-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Microbiology and Tumor Biology Center, Karolinska Institute, Stockholm, 171 77, Sweden. staffan.normark@stratresearch.se〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15731433" target="_blank"〉PubMed〈/a〉
    Keywords: Adhesins, Bacterial/chemistry/*metabolism ; Animals ; Bacterial Proteins/metabolism ; Bacteriophages/genetics ; Carbohydrate Conformation ; Cell Membrane/microbiology ; Dysentery, Bacillary/*microbiology ; Glucose/metabolism ; Glycosylation ; Lipopolysaccharides/chemistry/*metabolism ; Models, Biological ; Mutation ; O Antigens/chemistry/*metabolism ; Operon ; Rabbits ; Serotyping ; Shigella flexneri/classification/genetics/metabolism/*pathogenicity ; Virulence ; Virulence Factors/metabolism ; Yersinia enterocolitica/metabolism/*pathogenicity
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 6
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    Cellular microbiology emerging (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-01-19
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cossart, P -- Boquet, P -- Normark, S -- Rappuoli, R -- New York, N.Y. -- Science. 1996 Jan 19;271(5247):315-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Unite des Interactions Bacteries-Cellules, Institut Pasteur, Paris, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8553065" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/*metabolism ; Animals ; Bacteria/*pathogenicity ; Bacterial Physiological Phenomena ; Bacterial Toxins/toxicity ; Cell Membrane/*physiology/ultrastructure ; Cytoskeleton/*physiology ; Endocytosis ; Humans ; Signal Transduction ; Trypanosoma cruzi/*pathogenicity/physiology ; Vacuoles/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 7
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    Induction of gene expression in Escherichia coli after pilus-mediated adherence (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-08-30
    Description: The induction of cascades of virulence factors after contact between bacteria and host cells was investigated. P-pili mediate the binding of uropathogenic Escherichia coli to its host cell receptor. After P-pili binding there was transcriptional activation of a sensor-regulator protein that is essential for the bacterial iron-starvation response. An insertion mutation of the sensor-regulator gene eliminated the ability of uropathogenic E. coli to produce siderophores and their iron-regulated membrane receptors, thereby abolishing their ability to grow in urine. These results suggest that P-pilus-mediated attachment may be an important part of the sensor-regulatory process involved in uropathogenic E. coli urinary tract infection.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhang, J P -- Normark, S -- 5RO1GM44655-05/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Aug 30;273(5279):1234-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Microbiology, Washington University School of Medicine, 666 South Euclid Avenue, St. Louis, MO 63110-1093, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8703059" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Bacterial Adhesion ; Bacterial Outer Membrane Proteins/metabolism ; Bacterial Proteins/*genetics/physiology ; Base Sequence ; Culture Media ; Escherichia coli/genetics/growth & development/*pathogenicity ; *Escherichia coli Proteins ; Fimbriae, Bacterial/*physiology ; *Gene Expression Regulation, Bacterial ; Humans ; Iron/metabolism ; Iron-Binding Proteins ; Membrane Proteins/*genetics/physiology ; Molecular Sequence Data ; Periplasmic Binding Proteins ; *Phosphotransferases ; Rabbits ; Receptors, Immunologic/metabolism ; Siderophores/metabolism ; Urine/microbiology ; Virulence/*genetics
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 8
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    Attachment of Helicobacter pylori to human gastric epithelium mediated by blood group antigens (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-12-17
    Description: Helicobacter pylori is associated with development of gastritis, gastric ulcers, and adenocarcinomas in humans. The Lewis(b) (Le(b)) blood group antigen mediates H. pylori attachment to human gastric mucosa. Soluble glycoproteins presenting the Leb antigen or antibodies to the Leb antigen inhibited bacterial binding. Gastric tissue lacking Leb expression did not bind H. pylori. Bacteria did not bind to Leb antigen substituted with a terminal GalNAc alpha 1-3 residue (blood group A determinant), suggesting that the availability of H. pylori receptors might be reduced in individuals of blood group A and B phenotypes, as compared with blood group O individuals.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Boren, T -- Falk, P -- Roth, K A -- Larson, G -- Normark, S -- TW04669-02/TW/FIC NIH HHS/ -- New York, N.Y. -- Science. 1993 Dec 17;262(5141):1892-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Microbiology, Washington University School of Medicine, St. Louis, MO 63110.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8018146" target="_blank"〉PubMed〈/a〉
    Keywords: Antibodies, Monoclonal ; Carbohydrate Sequence ; Epithelium/microbiology ; Fucose/metabolism ; Gastric Mucosa/*microbiology ; Glycoconjugates/chemistry/metabolism ; Glycosphingolipids/metabolism ; Glycosylation ; H-2 Antigens/immunology ; Helicobacter pylori/*metabolism ; Humans ; Immunoblotting ; Lewis Blood-Group System/chemistry/immunology/*metabolism ; Molecular Sequence Data ; Oligosaccharides/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 9
    Electronic Resource
    Electronic Resource
    Overlapping Genes (1983)
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Genetics 17 (1983), S. 499-525 
    Details
    ISSN: 0066-4197
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1146/annurev.ge.17.120183.002435
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  • 10
    Electronic Resource
    Electronic Resource
    Chaperone-Assisted Assembly and Molecular Architecture of Adhesive Pili (1991)
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Microbiology 45 (1991), S. 383-415 
    Details
    ISSN: 0066-4227
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1146/annurev.mi.45.100191.002123
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