EcoliWiki - User contributions [en]

PMID:20214609

2014-06-09T03:21:07Z

88.195.147.42: Fill PMID: Page!

{{RightTOC}}


{| id="J53952822b6adc" class=" tableEdit PMID_info_table"

|-
!align=left |Citation
||
'''Kutter, E, De Vos, D, Gvasalia, G, Alavidze, Z, Gogokhia, L, Kuhl, S and Abedon, ST''' (2010) Phage therapy in clinical practice: treatment of human infections. ''Curr Pharm Biotechnol'' '''11''':69-86
|-
!align=left |Abstract
||
Phage therapy is the application of bacteria-specific viruses with the goal of reducing or eliminating pathogenic or nuisance bacteria. While phage therapy has become a broadly relevant technology, including veterinary, agricultural, and food microbiology applications, it is for the treatment or prevention of human infections that phage therapy first caught the world's imagination--see, especially, Arrowsmith by Sinclair Lewis (1925)--and which today is the primary motivator of the field. Nonetheless, though the first human phage therapy took place in the 1920s, by the 1940s the field, was in steep decline despite early promise. The causes were at least three-fold: insufficient understanding among researchers of basic phage biology; over exuberance, which led, along with ignorance, to carelessness; and the advent of antibiotics, an easier to handle as well as highly powerful category of antibacterials. The decline in phage therapy was neither uniform nor complete, especially in the former Soviet Republic of Georgia, where phage therapy traditions and practice continue to this day. In this review we strive toward three goals: 1. To provide an overview of the potential of phage therapy as a means of treating or preventing human diseases; 2. To explore the phage therapy state of the art as currently practiced by physicians in various pockets of phage therapy activity around the world, including in terms of potential commercialization; and 3. To avert a recapitulation of phage therapy's early decline by outlining good practices in phage therapy practice, experimentation, and, ultimately, commercialization.
|-
!align=left |Links
||
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=20214609 PubMed]

|-
!align=left |Keywords
||
Bacterial Infections/therapy; Bacterial Infections/virology; Bacteriophages; Biological Therapy/trends; Humans; Viral Vaccines/therapeutic use

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.183526.J53952822b6adc&page=183526&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table] ||
|}


==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

== Useful Materials and Methods {{HelpIcon|Help:Literature}}==
{{LitMaterials}}

==Annotations {{HelpIcon|Help:Literature}}==
<annotationlinks/>

==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
{{LitLinks}}

==See also==

==References==
{{RefHelp}}
<references/>

PMID:20214609

2014-06-09T03:21:06Z

88.195.147.42: New PMID: Page!

PMID on Demand placeholder

PMID:1098662

2014-06-08T06:47:11Z

88.195.147.42: Fill PMID: Page!

{{RightTOC}}


{| id="Y539406eebfa86" class=" tableEdit PMID_info_table"

|-
!align=left |Citation
||
'''Liou, YF, Yoshikawa, M and Tanaka, N''' (1975) Alteration of ribosomal protein L5 in a thiopeptin-resistant mutant of Escherichia coli. ''Biochem. Biophys. Res. Commun.'' '''65''':1096-101
|-
!align=left |Abstract
||
No abstract in PubMed
|-
!align=left |Links
||
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=1098662 PubMed]

|-
!align=left |Keywords
||
Anti-Bacterial Agents/pharmacology; Binding Sites; Chromatography, Ion Exchange; Drug Resistance, Microbial; Electrophoresis, Polyacrylamide Gel; Escherichia coli/drug effects; Escherichia coli/metabolism; Escherichia coli Proteins/metabolism; Guanine Nucleotides/metabolism; Methylnitronitrosoguanidine/pharmacology; Mutation; Peptides/pharmacology; Ribosomal Proteins/metabolism; Ribosomes/drug effects; Ribosomes/metabolism

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.183521.Y539406eebfa86&page=183521&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table] ||
|}


==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

== Useful Materials and Methods {{HelpIcon|Help:Literature}}==
{{LitMaterials}}

==Annotations {{HelpIcon|Help:Literature}}==
<annotationlinks/>

==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
{{LitLinks}}

==See also==

==References==
{{RefHelp}}
<references/>

PMID:1098662

2014-06-08T06:47:10Z

88.195.147.42: New PMID: Page!

PMID on Demand placeholder

PMID:765257

2014-06-08T02:09:26Z

88.195.147.42: Fill PMID: Page!

{{RightTOC}}


{| id="I5393c5d5ee81e" class=" tableEdit PMID_info_table"

|-
!align=left |Citation
||
'''Vandekerckhove, J, Rombauts, W, Peeters, B and Wittmann-Liebold, B''' (1975) Determination of the complete amino acid sequence of protein S21 from Escherichia coli ribosomes. ''Hoppe-Seyler's Z. Physiol. Chem.'' '''356''':1955-76
|-
!align=left |Abstract
||
Protein S21 was digested with trypsin before and after maleylation, with chymotrypsin, thermolysin and a glutamyl-specific protease. The resulting peptides were isolated and their amino acid composition determined. The amino acid sequences of selected peptides were determined either by the manual subtractive Edman method or by the dansyl-Edman procedure. Additional information was obtained from the automatic Edman degradation of the whole protein in a modified Sequenator. All these results combined yielded the sequence shown in Fig. 1. Protein S21 consists of 70 amino acids (Asp1,Asn2,Thr3,Ser2,Glu8,Pro3,Gly1,Ala9,Val6,Cys1,Ile1,Leu4,Tyr2,Phe3,His1,Lys9 and Arg14). It contains neither Met nor Trp. The molecular weight amounts to 8359. Clustering of basic amino acids is observed in five regions. We also include a prediction for regions with alpha-helices and with beta-sheets.
|-
!align=left |Links
||
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=765257 PubMed]

|-
!align=left |Keywords
||
Amino Acid Sequence; Amino Acids/analysis; Bacterial Proteins/analysis; Escherichia coli; Ribosomal Proteins/analysis

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.183518.I5393c5d5ee81e&page=183518&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table] ||
|}


==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

== Useful Materials and Methods {{HelpIcon|Help:Literature}}==
{{LitMaterials}}

==Annotations {{HelpIcon|Help:Literature}}==
<annotationlinks/>

==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
{{LitLinks}}

==See also==

==References==
{{RefHelp}}
<references/>

PMID:765257

2014-06-08T02:09:25Z

88.195.147.42: New PMID: Page!

PMID on Demand placeholder

PMID:20023034

2014-06-07T12:31:38Z

88.195.147.42: Fill PMID: Page!

{{RightTOC}}


{| id="C53930629ef3d2" class=" tableEdit PMID_info_table"

|-
!align=left |Citation
||
'''Seffernick, JL, Dodge, AG, Sadowsky, MJ, Bumpus, JA and Wackett, LP''' (2010) Bacterial ammeline metabolism via guanine deaminase. ''J. Bacteriol.'' '''192''':1106-12
|-
!align=left |Abstract
||
Melamine toxicity in mammals has been attributed to the blockage of kidney tubules by insoluble complexes of melamine with cyanuric acid or uric acid. Bacteria metabolize melamine via three consecutive deamination reactions to generate cyanuric acid. The second deamination reaction, in which ammeline is the substrate, is common to many bacteria, but the genes and enzymes responsible have not been previously identified. Here, we combined bioinformatics and experimental data to identify guanine deaminase as the enzyme responsible for this biotransformation. The ammeline degradation phenotype was demonstrated in wild-type Escherichia coli and Pseudomonas strains, including E. coli K12 and Pseudomonas putida KT2440. Bioinformatics analysis of these and other genomes led to the hypothesis that the ammeline deaminating enzyme was guanine deaminase. An E. coli guanine deaminase deletion mutant was deficient in ammeline deaminase activity, supporting the role of guanine deaminase in this reaction. Two guanine deaminases from disparate sources (Bradyrhizobium japonicum USDA 110 and Homo sapiens) that had available X-ray structures were purified to homogeneity and shown to catalyze ammeline deamination at rates sufficient to support bacterial growth on ammeline as a sole nitrogen source. In silico models of guanine deaminase active sites showed that ammeline could bind to guanine deaminase in a similar orientation to guanine, with a favorable docking score. Other members of the amidohydrolase superfamily that are not guanine deaminases were assayed in vitro, and none had substantial ammeline deaminase activity. The present study indicated that widespread guanine deaminases have a promiscuous activity allowing them to catalyze a key reaction in the bacterial transformation of melamine to cyanuric acid and potentially contribute to the toxicity of melamine.
|-
!align=left |Links
||
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=20023034 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2812975 PMC2812975]
Online version:[http://dx.doi.org/10.1128/JB.01243-09 10.1128/JB.01243-09]
|-
!align=left |Keywords
||
Bacterial Proteins/metabolism; Bradyrhizobium/enzymology; Bradyrhizobium/genetics; Bradyrhizobium/metabolism; Catalytic Domain; Cluster Analysis; Computational Biology; Escherichia coli K12/enzymology; Escherichia coli K12/genetics; Escherichia coli K12/metabolism; Gene Deletion; Gene Order; Genes, Bacterial; Guanine Deaminase/isolation & purification; Guanine Deaminase/metabolism; Humans; Kinetics; Metabolic Networks and Pathways; Models, Molecular; Molecular Structure; Phylogeny; Protein Structure, Tertiary; Pseudomonas putida/enzymology; Pseudomonas putida/genetics; Pseudomonas putida/metabolism; Sequence Homology, Amino Acid; Substrate Specificity; Triazines/metabolism

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.183514.C53930629ef3d2&page=183514&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table] ||
|}


==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

== Useful Materials and Methods {{HelpIcon|Help:Literature}}==
{{LitMaterials}}

==Annotations {{HelpIcon|Help:Literature}}==
<annotationlinks/>

==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
{{LitLinks}}

==See also==

==References==
{{RefHelp}}
<references/>

PMID:20023034

2014-06-07T12:31:37Z

88.195.147.42: New PMID: Page!

PMID on Demand placeholder

Category:GO:0006270 ! DNA-dependent DNA replication initiation

2014-06-07T09:02:56Z

88.195.147.42: New GO term category page

{{GO term stub|GO:0006270_!_DNA-dependent_DNA_replication_initiation}}

==References==
{{RefHelp}}
<references/>

PMID:16935877

2014-06-03T05:36:54Z

88.195.147.42: Fill PMID: Page!

{{RightTOC}}


{| id="G538d5ef5888bf" class=" tableEdit PMID_info_table"

|-
!align=left |Citation
||
'''Killoran, MP and Keck, JL''' (2006) Sit down, relax and unwind: structural insights into RecQ helicase mechanisms. ''Nucleic Acids Res.'' '''34''':4098-105
|-
!align=left |Abstract
||
Helicases are specialized molecular motors that separate duplex nucleic acids into single strands. The RecQ family of helicases functions at the interface of DNA replication, recombination and repair in bacterial and eukaryotic cells. They are key, multifunctional enzymes that have been linked to three human diseases: Bloom's, Werner's and Rothmund-Thomson's syndromes. This review summarizes recent studies that relate the structures of RecQ proteins to their biochemical activities.
|-
!align=left |Links
||
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=16935877 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1616949 PMC1616949]
Online version:[http://dx.doi.org/10.1093/nar/gkl538 10.1093/nar/gkl538]
|-
!align=left |Keywords
||
Adenosine Triphosphatases/chemistry; Adenosine Triphosphatases/genetics; Adenosine Triphosphatases/metabolism; Adenosine Triphosphate/metabolism; Bloom Syndrome/genetics; DNA Helicases/chemistry; DNA Helicases/genetics; DNA Helicases/metabolism; DNA Replication/physiology; Humans; Hydrolysis; Protein Structure, Tertiary/physiology; RecQ Helicases; Rothmund-Thomson Syndrome/genetics; Werner Syndrome/genetics

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.183501.G538d5ef5888bf&page=183501&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table] ||
|}


==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

== Useful Materials and Methods {{HelpIcon|Help:Literature}}==
{{LitMaterials}}

==Annotations {{HelpIcon|Help:Literature}}==
<annotationlinks/>

==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
{{LitLinks}}

==See also==

==References==
{{RefHelp}}
<references/>

PMID:16935877

2014-06-03T05:36:53Z

88.195.147.42: New PMID: Page!

PMID on Demand placeholder