Results 111 to 120 of about 936,446 (303)

Interaction of the maltose-binding protein with membrane vesicles of Escherichia coli [PDF]

open access: yesJournal of Bacteriology, 1982
The interaction of the radioactively labeled purified maltose-binding protein of Escherichia coli with membrane vesicles was studied. The maltose-binding protein bound specifically to the vesicles, in the presence of maltose, on few sites. Under conditions in which a potential was imposed across the membrane, the specific binding was (i) increased, (ii)
openaire   +3 more sources

Targets for the MalI repressor at the divergent Escherichia coliK-12malX-malI promoters [PDF]

open access: yes, 2010
Random mutagenesis has been used to identify the target DNA sites for the MalI repressor at the divergent Escherichia coli K-12 malX-malI promoters. The malX promoter is repressed by MalI binding to a DNA site located from position -24 to position -9 ...
Barnard   +22 more
core   +1 more source

Global protein function prediction in protein-protein interaction networks [PDF]

open access: yesNature Biotech. 21, 697-700 (2003), 2003
The determination of protein functions is one of the most challenging problems of the post-genomic era. The sequencing of entire genomes and the possibility to access gene's co-expression patterns has moved the attention from the study of single proteins or small complexes to that of the entire proteome. In this context, the search for reliable methods
arxiv  

Dependence of maltose transport and chemotaxis on the amount of maltose-binding protein.

open access: yesJournal of Biological Chemistry, 1985
Maltose-binding protein (MBP) is essential for maltose transport and chemotaxis in Escherichia coli. To perform these functions it must interact with two sets of cytoplasmic membrane proteins, the MalFGK transport complex and the chemotactic signal transducer Tar.
B A Rasmussen   +3 more
openaire   +3 more sources

Molecular cloning of the cDNA encoding pp36, a tyrosine-phosphorylated adaptor protein selectively expressed by T cells and natural killer cells. [PDF]

open access: yes, 1998
Activation of T and natural killer (NK) cells leads to the tyrosine phosphorylation of pp36 and to its association with several signaling molecules, including phospholipase Cgamma-1 and Grb2.
Berg, SF   +8 more
core   +1 more source

One-step affinity purification of fusion proteins with optimal monodispersity and biological activity: application to aggregation-prone HPV E6 proteins

open access: yesMicrobial Cell Factories, 2018
Background Bacterial expression and purification of recombinant proteins under homogeneous active form is often challenging. Fusion to highly soluble carrier proteins such as Maltose Binding Protein (MBP) often improves their folding and solubility, but ...
Anna Bonhoure   +7 more
doaj   +1 more source

Crystal structure of human IPS-1/MAVS/VISA/Cardif caspase activation recruitment domain [PDF]

open access: yes, 2010
Background: IPS-1/MAVS/VISA/Cardif is an adaptor protein that plays a crucial role in the induction of interferons in response to viral infection. In the initial stage of the intracellular antiviral response two RNA helicases, retinoic acid inducible ...
Potter, Jane A.   +2 more
core   +1 more source

Towards defining the role of glycans as hardware in information storage and transfer: Basic principles, experimental approaches and recent progress [PDF]

open access: yes, 2001
The term `code' in biological information transfer appears to be tightly and hitherto exclusively connected with the genetic code based on nucleotides and translated into functional activities via proteins.
Gabius, Hans-Joachim   +6 more
core   +1 more source

Design and production of various fusion proteins of the nicotinamide/nicotinate mononucleotide adenilil transferase (NMNAT) of Plasmodium falciparum

open access: yesRevista Colombiana de Química, 2017
Recombinant proteins have become useful tools in biochemistry research. During their production, however, inclusion bodies (IB) appear, on the one hand, due to the high expression rate from the recombinant plasmids, which have high efficiency promoters ...
Carlos Alfonso Nieto Clavijo   +2 more
doaj   +1 more source

Overexpression and purification of U24 from human herpesvirus type-6 in E. coli: unconventional use of oxidizing environments with a maltose binding protein-hexahistine dual tag to enhance membrane protein yield

open access: yesMicrobial Cell Factories, 2011
Background Obtaining membrane proteins in sufficient quantity for biophysical study and biotechnological applications has been a difficult task. Use of the maltose binding protein/hexahistidine dual tag system with E.coli as an expression host is ...
Straus Suzana K, Tait Andrew R
doaj   +1 more source

Home - About - Disclaimer - Privacy