*  Escherichia coli proteins | Article about Escherichia coli proteins by The Free Dictionary
Looking for Escherichia coli proteins? Find out information about Escherichia coli proteins. common bacterium that normally inhabits the intestinal tracts of humans and animals, but can cause infection in other parts of the body, especially the... Explanation of Escherichia coli proteins
  https://encyclopedia2.thefreedictionary.com/Escherichia+coli+proteins
*  Probing the active site of YjeE: a vital Escherichia coli protein of unknown function | Biochemical Journal
In the study described here, we have taken steps to characterize the YjeE protein, an Escherichia coli protein of unknown function that is essential for bacterial viability. YjeE represents a protein family whose members are broadly conserved in bacteria, absent from eukaryotes and contain both Walker A and B motifs, characteristic of P-loop ATPases. We have revisited the dispensability of the yjeE gene in E. coli and describe efforts to probe the function of the YjeE protein with in vitro biochemistry. We have looked critically for ATPase activity in the recombinant E. coli protein and have made vigilant use of site-directed variants in the Walker A [K41A (Lys41→Ala) and T42A] and putative Walker B (D80Q) motifs. We noted that any hydrolysis of ATP by the wild-type E. coli protein might be attributed to background ATPase, since it was not appreciably different from that of the variants. To overcome potential contaminants, we turned to crystalline pure YjeE protein from Haemophilus ...
  http://www.biochemj.org/content/384/3/577
*  Gentaur Molecular :AbD \ MOUSE ANTI ESCHERICHIA COLI K88A, Product Type Monoclonal Antibody, Specificity ESCHERICHIA COLI...
Gentaur molecular products has all kinds of products like :search , AbD \ MOUSE ANTI ESCHERICHIA COLI K88A, Product Type Monoclonal Antibody, Specificity ESCHERICHIA COLI K88A, Target Species Bacterial, Host Mouse, Format Purified, Isotypes IgG2a, Applications E, IF, \ 4329-9758 for more molecular products just contact us
  http://www.antibody-antibodies.com/product_det.php?id=1415014&supplier=search&name=MOUSE%20ANTI%20ESCHERICHIA%20COLI%20K88A,%20Product%20Type%20%20Monoclonal%20Antibody,%20Specificity%20%20ESCHERICHIA%20COLI%20K88A,%20Target%20Species%20%20Bacterial,%20Host%20%20Mouse,%20Format%20%20Purified,%20Isotypes%20%20IgG2a,%20Applications%20%20E,%20IF,
*  Different cleavage sites are aligned differently in the active site of M1 RNA, the catalytic subunit of Escherichia coli RNase...
Base Sequence, Binding Sites, Catalysis, Cations; Divalent, Endoribonucleases/genetics/*metabolism, Escherichia coli/*enzymology, Escherichia coli Proteins, Hydrolysis, Molecular Sequence Data, Nucleic Acid Conformation, RNA; Catalytic/genetics/*metabolism, RNA; Messenger/chemistry/*metabolism, RNA; Transfer/chemistry/metabolism, Ribonuclease P ...
  http://uu.diva-portal.org/smash/record.jsf?pid=diva2:42681
*  Sec-independent protein translocation in Escherichia coli. A distinct and pivotal role for the TatB protein - Research Database...
In Escherichia coli, transmembrane translocation of proteins can proceed by a number of routes. A subset of periplasmic proteins are exported via the Tat pathway to which proteins are directed by N-terminal "transfer peptides" bearing the consensus (S/T)RRXFLK "twin-arginine" motif. The Tat system involves the integral membrane proteins TatA, TatB, TatC, and TatE. Of these, TatA, TatB, and TatE are homologues of the Hcf106 component of the DeltapH-dependent protein import system of plant thylakoids. Deletion of the tatB gene alone is sufficient to block the export of seven endogenous Tat substrates, including hydrogenase-2. Complementation analysis indicates that while TatA and TatE are functionally interchangeable, the TatB protein is functionally distinct. This conclusion is supported by the observation that Helicobacter pylori tatA will complement an E. coli tatA mutant, but not a tatB mutant. Analysis of Tat component stability in various tat deletion backgrounds shows that TatC is ...
  http://discovery.dundee.ac.uk/portal/en/research/secindependent-protein-translocation-in-escherichia-coli-a-distinct-and-pivotal-role-for-the-tatb-protein
*  JCVI: The Binary Protein-protein Interaction Landscape of Escherichia Coli.
Citation. Rajagopala SV, Sikorski P, Kumar A, Mosca R, Vlasblom J, Arnold R, Franca-Koh J, Pakala SB, Phanse S, Ceol A, Häuser R, Siszler G, Wuchty S, Emili A, Babu M, Aloy P, Pieper R, Uetz P. The Binary Protein-protein Interaction Landscape of Escherichia Coli.. Nature Biotechnology. 2014 Mar 01; 32: 285-90.. External Citation. Abstract. Efforts to map the Escherichia coli interactome have identified several hundred macromolecular complexes, but direct binary protein-protein interactions (PPIs) have not been surveyed on a large scale. Here we performed yeast two-hybrid screens of 3,305 baits against 3,606 preys (∼70% of the E. coli proteome) in duplicate to generate a map of 2,234 interactions, which approximately doubles the number of known binary PPIs in E. coli. Integration of binary PPI and genetic-interaction data revealed functional dependencies among components involved in cellular processes, including envelope integrity, flagellum assembly and protein quality ...
  http://www.jcvi.org/cms/publications/listing/abstract/article/the-binary-protein-protein-interaction-landscape-of-escherichia-coli-1/
*  AID 414701 - Resistance index, MIC for aminoglycosides-resistant Escherichia coli BL21 harboring pETSACG1 expressing APH(3')-3a...
BioAssay record AID 414701 submitted by ChEMBL: Resistance index, MIC for aminoglycosides-resistant Escherichia coli BL21 harboring pETSACG1 expressing APH(3')-3a enzyme to MIC for Escherichia coli BL21.
  https://pubchem.ncbi.nlm.nih.gov/bioassay/414701
*  Escherichia coli (Migula) Castellani and Chalmers ATCC ® 35401D-5&
Escherichia coli ATCC ® 35401D-5™ Designation: Genomic DNA from Escherichia coli strain H10407 TypeStrain=False Application: Food testing
  https://www.atcc.org/Global/Products/B/A/F/D/35401D-5.aspx
*  Escherichia coli (Migula) Castellani and Chalmers ATCC ® 8739D-5&t
Escherichia coli ATCC ® 8739D-5™ Designation: Genomic DNA from Escherichia coli strain Crooks TypeStrain=False Application: Food testing
  https://www.atcc.org/en/Products/Cells_and_Microorganisms/Bacteria/Bacterial_Genome_Sequencing_Strains/8739D-5.aspx?slp=1
*  Escherichia coli (Migula) Castellani and Chalmers ATCC ® BAA-2192D
Escherichia coli ATCC ® BAA-2192D-5™ Designation: Genomic DNA from Escherichia coli strain 99-3311 TypeStrain=False Application:
  https://atcc.org/products/all/BAA-2192D-5.aspx
*  Escherichia coli (Migula) Castellani and Chalmers ATCC ® BAA-2192D
Escherichia coli ATCC ® BAA-2192D-5™ Designation: Genomic DNA from Escherichia coli strain 99-3311 TypeStrain=False Application:
  https://www.atcc.org/Products/All/BAA-2192D-5.aspx?p=1&rel=%7B0%7D&slp=1
*  Escherichia coli (Migula) Castellani and Chalmers ATCC ® BAA-460D
Escherichia coli ATCC ® BAA-460D-5™ Designation: Genomic DNA from Escherichia coli strain RMID 0509952 TypeStrain=False Application:
  https://www.atcc.org/en/Products/Cells_and_Microorganisms/By_Focus_Area/Comparative_Genome_Sequencing/BAA-460D-5.aspx
*  Escherichia coli TolA tolerates multiple amino-acid substitutions as revealed by screening randomized variants for membrane...
Escherichia coli TolA is a cytoplasmic membrane protein required for outer membrane integrity and the translocation of F-specific filamentous (Ff) bacteriophage DNA. Both phage infection and membrane integrity depend on several TolA interactions, e.g. those of the TolA C-terminal domain (TolAIII). Membrane integrity involves interaction with two host proteins and phage translocation requires direct interaction with the N-terminal domain (N1) of Ff phage protein g3p. Although cocrystallization of TolAIII and N1g3p has identified several contact points, it is still uncertain which residues are selectively involved in the different TolA functions. Thus, four different limited substitution libraries of TolA were created, targeting contacts at positions 415-420. These libraries were introduced into the tolA strain K17DE3tolA/F+ and several variants, containing complementing, multiple amino-acid substitutions, were identified. However, most randomized variants did not complement the tolA strain ...
  http://www.madforcancer.lu.se/carl-borrebaeck/publication/46900603-ebe8-47aa-bcc8-12f036f6b84f
*  Different Regions of the Nonconserved Large Periplasmic Domain of Escherichia coli YidC Are Involved in the SecF...
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  https://www.infona.pl/resource/bwmeta1.element.acs-doi-10_1021_bi060826z
*  Peer Evaluation : Use of Energy Healing Medicine Against Escherichia coli for Antimicrobial Susceptibility, Biochemical...
Abstract : Escherichia coli (E. coli) infections are the major health concern, as it causes infections in human mainly in urinarytract, ear, and wound infections. The present study evaluates the impact of biofield energy treatment on E. coli regardingantimicrobial sensitivity assay, biochemical study and biotype number. Four multidrug resistant (MDR) clinical lab isolates (LSs)of E. coli (LS 12, LS 13, LS 42, and LS 51) were taken in two groups i.e. control and treated. After treatment, above mentionedparameter were evaluated on day 10 in control and treated samples using MicroScan Walk-Away® system. The antimicrobialsensitivity assay was reported with 46.67% alteration (14 out of 30 tested antimicrobials) in treated group of MDR E. coli isolates.The minimum inhibitory concentration (MIC) study showed the alteration in MIC values of about 34.37% (11 out of 32) testedantimicrobials, after biofield treatment in clinical isolates of E. coli. Piperacillin/tazobactam was reported with ...
  http://peerevaluation.org/read/libraryID:30360
*  Investigating cellular responses to mutations in the glutathione and thioredoxin pathways of Escherichia coli
Inhibition of disulfide bond formation in Escherichia coli implicates an intricate collaboration of proteins which comprise the glutathione and thioredoxin reducing pathways. Bioengineers have successfully engineered E. coli possessing mutated reducing pathways that promote, rather than inhibit, disulfide bond formation in the cytoplasm. The transcriptome of six such mutant E. coli strains have been characterized using Microarray technology. We find that all mutant strains, exhibit a unique response to oxidative stress, not observed in wild type. Statistical analyses revealed the expression of more than 200 genes that are affected by mutations within the reducing pathways. Significantly up-regulated biological processes include cysteine biosynthesis, histidine biosynthesis, NADH Dehydrogenase I biosynthesis, sugar catabolic processes, and activation of stress responses . The second part of this work describes the construction of an E. coli strain that promotes the complete conversion of ...
  https://repositories.lib.utexas.edu/handle/2152/ETD-UT-2009-12-706
*  Clustered third-base substitutions among wild strains of Escherichia coli. - Semantic Scholar
Nucleotide sequences of translated regions of the trp operon in 12 wild strains of Escherichia coli reveal striking uniformity among eight strains (suggesting recent common ancestry and supporting the importance of periodic selection in natural populations) and clustered substitutions in four strains (implicating events affecting runs of nucleotides).
  https://www.semanticscholar.org/paper/Clustered-third-base-substitutions-among-wild-stra-Milkman-Crawford/dcbbcb3c0de089f93aa7804833c2e79586805f6d
*  What is Escherichia coli (E. coli)?
Escherichia coli (E. coli) is a bacterium that lives in the digestive tracts of healthy people and animals. Most types of E. coli are pretty harmless, but this bacterium should not be taken lightly, as it can cause severe damage to your body
  https://www.aquasana.com/education/meet-the-contaminant-e-coli
*  Escherichia coli DH10B ( ...)
Multiporator / Electroporator 2510 Transformation Protocol Protocol No. 4308 915.513 04/2002 Microorganism Escherichia coli DH10B,Escherichia,coli,DH10B,biological,advanced biology technology,biology laboratory technology,biology device technology,latest biology technology
  http://www.bio-medicine.org/biology-technology/Escherichia-coli-DH10B-546-1/
*  AID 1079176 - Inhibition of human truncated PAK2 expressed in Escherichia coli cell assessed as substrate phosphorylation using...
BioAssay record AID 1079176 submitted by ChEMBL: Inhibition of human truncated PAK2 expressed in Escherichia coli cell assessed as substrate phosphorylation using fluorescence-labelled peptides as substrate at 420 uM after 90 mins by microfluidic peptide phosphorylation assay.
  https://pubchem.ncbi.nlm.nih.gov/bioassay/1079176
*  Heterologous Expression of Mycobacterial Esx Complexes in Escherichia coli for Structural Studies Is Facilitated by the Use of...
Heterologous Expression of Mycobacterial Esx Complexes in Escherichia coli for Structural Studies Is Facilitated by the Use of Maltose Binding Protein Fusions. . Biblioteca virtual para leer y descargar libros, documentos, trabajos y tesis universitarias en PDF. Material universiario, documentación y tareas realizadas por universitarios en nuestra biblioteca. Para descargar gratis y para leer online.
  http://libros.duhnnae.com/2017/jun8/149832113432-Heterologous-Expression-of-Mycobacterial-Esx-Complexes-in-Escherichia-coli-for-Structural-Studies-Is-Facilitated-by-the-Use-of-Maltose-Binding-Protein.php
*  AID 1078597 - Inhibition of human full length p38 beta2 expressed in Escherichia coli cell assessed as substrate...
BioAssay record AID 1078597 submitted by ChEMBL: Inhibition of human full length p38 beta2 expressed in Escherichia coli cell assessed as substrate phosphorylation using fluorescence-labelled peptides as substrate at 70 uM after 90 mins by microfluidic peptide phosphorylation assay.
  https://pubchem.ncbi.nlm.nih.gov/bioassay/1078597
*  Iron in the structure of The Structure of Ubiquinol Oxidase From Escherichia Coli (pdb 1fft)
Mono- and Stereopictres of 5.0 Angstrom coordination sphere of Iron atom in PDB 1fft: The Structure of Ubiquinol Oxidase From Escherichia Coli
  http://iron.atomistry.com/pdb1fft.html
*  Frontiers | A mathematical model of metabolism and regulation provides a systems-level view of how Escherichia coli responds to...
The efficient redesign of bacteria for biotechnological purposes, such as biofuel production, waste disposal or specific biocatalytic functions, requires a quantitative systems-level understanding of energy supply, carbon and redox metabolism. The measurement of transcript levels, metabolite concentrations and metabolic fluxes per se gives an incomplete picture. An appreciation of the interdependencies between the different measurement values is essential for systems-level understanding. Mathematical modeling has the potential to provide a coherent and quantitative description of the interplay between gene expression, metabolite concentrations and metabolic fluxes. Escherichia coli undergoes major adaptations in central metabolism when the availability of oxygen changes. Thus, an integrated description of the oxygen response provides a benchmark of our understanding of carbon, energy and redox metabolism. We present the first comprehensive model of the central metabolism of E. coli that ...
  https://www.frontiersin.org/articles/10.3389/fmicb.2014.00124/full