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Bacterial Protein Kinases

2021
Bacteria are able to inhabit and survive vastly diverse environments. This enormous adaptive capacity depend on their ability to perceive cues from the micro-environment and process this information accordingly to mount appropriate metabolic responses and ultimately sustain homeostasis.
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Autophosphorylation of a Bacterial Protein at Tyrosine

Journal of Molecular Biology, 1996
Autophosphorylation at tyrosine is a common process in eukaryotic kinases, which is generally modulated by regulatory ligands and affects the properties of these enzymes. We report that this type of modification occurs also in bacteria, namely in an 81 kDa protein from Acinetobacter johnsonii.
Duclos, B.   +4 more
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Bacterial Moonlighting Proteins and Bacterial Virulence

2011
Implicit in the central dogma is the hypothesis that each protein gene product has but one function. However, over the past decade, it has become clear that many proteins have one or more unique functions, over-and-above the principal biological action of the specific protein.
Andrew J. Martin, Brian Henderson
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iLoc-Gpos: a multi-layer classifier for predicting the subcellular localization of singleplex and multiplex Gram-positive bacterial proteins.

Protein Peptide Letters, 2012
By introducing the "multi-layer scale", as well as hybridizing the information of gene ontology and the sequential evolution information, a novel predictor, called iLoc-Gpos, has been developed for predicting the subcellular localization of Gram positive
Zhi-cheng Wu, Xuan Xiao, K. Chou
semanticscholar   +1 more source

Protein–Protein Interaction: Bacterial Two-Hybrid

2017
The bacterial two-hybrid (BACTH, for "Bacterial Adenylate Cyclase-based Two-Hybrid") system is a simple and fast genetic approach to detect and characterize protein-protein interactions in vivo. This system is based on the interaction-mediated reconstitution of a cAMP signaling cascade in Escherichia coli.
Scot P. Ouellette   +5 more
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Analysis of bacterial biotin-proteins

Biochimica et Biophysica Acta (BBA) - Protein Structure, 1975
The biotin-protein populations in several bacterial strains were analyzed by solubilization of [3H]biotin-labeled cells with sodium dodecylsulfate followed by electrophoresis on polyacrylamide gels containing the detergent. A variety of patterns of biotin-labeled polypeptide chains was seen, ranging from a single biotin-protein in Escherichia coli ...
P R Vagelos, R. Ray Fall, A.W. Alberts
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A bacterial dynamin-like protein

Nature, 2006
Dynamins form a superfamily of large mechano-chemical GTPases that includes the classical dynamins and dynamin-like proteins (DLPs). They are found throughout the Eukarya, functioning in core cellular processes such as endocytosis and organelle division.
Harry H. Low, Jan Löwe
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Bacterial Protein Toxins and Inflammation

Scandinavian Journal of Infectious Diseases, 2003
Although human mucosal linings are continuously exposed to microbes, the microbes rarely induce disease. This is because mucosal surfaces are protected by a first line of defence termed the innate immunity system. Inflammatory processes are activated as a consequence of a complex interplay between microbes and host target cells.
Tomas Söderblom   +3 more
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Bacterial Protein Translocation

1988
Protein translocation is a process common to all cells. Both prokaryotes and eukaryotes are divided into distinct compartments, each containing a unique set of proteins important to specific cellular functions. Except for a few mitochondrial and chloroplast proteins, almost all proteins are synthesized in the cytoplasm; therefore many proteins must ...
Elliott Crooke, William Wickner
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Elongation in bacterial protein biosynthesis

Current Opinion in Biotechnology, 1996
The past year has brought some notable advances in our understanding of the structure and function of elongation factors (EFs) involved in protein biosynthesis. The structures of the ternary complex of aminoacylated tRNA with EF-Tu.GTP and of the complex EF-Tu.EF-Ts have been determined.
Morten Kjeldgaard, Jens Nyborg
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