Results 81 to 90 of about 7,190,308 (348)

Comparative NanoUPLC-MSE analysis between magainin I-susceptible and -resistant Escherichia coli strains

Scientific Reports, 2017
In recent years the antimicrobial peptides (AMPs) have been prospected and designed as new alternatives to conventional antibiotics. Indeed, AMPs have presented great potential toward pathogenic bacterial strains by means of complex mechanisms of action.
Marlon H. Cardoso, Keyla C. de Almeida, Elizabete de S. Cândido, André M. Murad, Simoni C. Dias, Octávio L. Franco   +5 more
doaj   +1 more source

Phylogenetic and complementation analysis of a single-stranded DNA binding protein family from lactococcal phages indicates a non-bacterial origin. [PDF]

PLoS ONE, 2011
BACKGROUND: The single-stranded-nucleic acid binding (SSB) protein superfamily includes proteins encoded by different organisms from Bacteria and their phages to Eukaryotes.
Agnieszka K Szczepankowska, Eric Prestel, Mahendra Mariadassou, Jacek K Bardowski, Elena Bidnenko   +4 more
doaj   +1 more source

Aβ42 promotes the aggregation of α‐synuclein splice isoforms via heterogeneous nucleation

FEBS Letters, EarlyView.
The aggregation of amyloid‐β (Aβ) and α‐synuclein (αSyn) is associated with Alzheimer's and Parkinson's diseases. This study reveals that Aβ aggregates serve as potent nucleation sites for the aggregation of αSyn and its splice isoforms, shedding light on the intricate interplay between these two pathogenic proteins.
Alexander Röntgen, Zenon Toprakcioglu, Michele Vendruscolo   +2 more
wiley   +1 more source

Bacterial Protein-Tyrosine Kinases [PDF]

Current Proteomics, 2010
Bacteria and Eukarya share essentially the same family of protein-serine/threonine kinases, also known as the Hanks-type kinases. However, when it comes to protein-tyrosine phosphorylation, bacteria seem to have gone their own way. Bacterial protein-tyrosine kinases (BY-kinases) are bacterial enzymes that are unique in exploiting the ATP/GTP-binding ...
Shi, Lei, Kobir, Ahasanul, Jers, Carsten, Mijakovic, Ivan   +3 more
openaire   +3 more sources

Archaeal protein containing domain of unknown function 2193 undergoes oligomeric reconfiguration upon iron–sulfur cluster binding

FEBS Letters, EarlyView.
This work presents the characterization of MvoDUF2193, a Methanococcus voltae (Mvo) protein from the domain of unknown function (DUF) 2193 family. We demonstrate that MvoDUF2193 binds a single [4Fe–4S] cluster per subunit and that cluster occupancy regulates the transition from an apo tetramer to a [4Fe–4S] monomeric form. This structural transition is
Emily M. Dieter, James Larson, Monika Tokmina‐Lukaszewska, Jin Xiong, Jared Green, Yisong Guo, William E. Broderick, Brian Bothner, Joan B. Broderick   +8 more
wiley   +1 more source

EffectiveDB—updates and novel features for a better annotation of bacterial secreted proteins and Type III, IV, VI secretion systems

Nucleic Acids Res., 2015
Protein secretion systems play a key role in the interaction of bacteria and hosts. EffectiveDB (http://effectivedb.org) contains pre-calculated predictions of bacterial secreted proteins and of intact secretion systems.
Valerie Eichinger, T. Nussbaumer, A. Platzer, Marc-André Jehl, Roland Arnold, T. Rattei   +5 more
semanticscholar   +1 more source

Redox‐dependent binding and conformational equilibria govern the fluorescence decay of NAD(P)H in living cells

FEBS Letters, EarlyView.
In this work, we reveal how different enzyme binding configurations influence the fluorescence decay of NAD(P)H in live cells using time‐resolved anisotropy imaging and fluorescence lifetime imaging microscopy (FLIM). Mathematical modelling shows that the redox states of the NAD and NADP pools govern these configurations, shaping their fluorescence ...
Thomas S. Blacker, Nimit Mistry, Nicoletta Plotegher, Elizabeth R. Westbrook, Michael D. E. Sewell, John Carroll, Gyorgy Szabadkai, Angus J. Bain, Michael R. Duchen   +8 more
wiley   +1 more source

Effective—a database of predicted secreted bacterial proteins

Nucleic Acids Res., 2010
Protein secretion is a key virulence mechanism of pathogenic and symbiotic bacteria, which makes the investigation of secreted proteins (‘effectors’) crucial for understanding the molecular bacterium–host interactions. Effective (http://effectors.org) is
Marc-André Jehl, Roland Arnold, Thomas Rattei   +2 more
semanticscholar   +1 more source

Functional role and folding properties of the glucan‐binding domain of oral bacterial glucansucrase

FEBS Letters, EarlyView.
The role of the glucan‐binding domain in Streptococcus sobrinus glucansucrase was examined, focusing on its impact on enzymatic activity, dextran binding, and structural stability of deletion mutants and a circularly permuted protein. Our research revealed that glucosyl transfer efficiency is linked to cooperative interdomain folding.
Hideyuki Komatsu, Takayuki Sadakane, Yudai Murata, Junichi Taira, Hiroshi Sakamoto, Takao Kodama   +5 more
wiley   +1 more source

Binding of silver nanoparticles to bacterial proteins depends on surface modifications and inhibits enzymatic activity.

Environmental Science and Technology, 2010
Here we describe results from a proteomic study of protein-nanoparticle interactions to further the understanding of the ecotoxicological impact of silver nanoparticles (AgNPs) in the environment.
N. Wigginton, A. de Titta, Flavio Piccapietra, J. Dobias, V. Nesatyy, M. Suter, R. Bernier-Latmani   +6 more
semanticscholar   +1 more source