Results 121 to 130 of about 2,121,701 (315)

Protein-protein interactions facilitate DNA binding by the glucocorticoid receptor DNA-binding domain.

Journal of Biological Chemistry, 1990
We have studied the interaction of the DNA-binding domain of the glucocorticoid receptor with a glucocorticoid response element from the tyrosine aminotransferase gene. This response element consists of two binding sites (half-sites) for the glucocorticoid receptor DNA-binding domain. The sequences of these two half-sites are not identical, and we have
K, Dahlman-Wright, H, Siltala-Roos, J, Carlstedt-Duke, J A, Gustafsson   +3 more
openaire   +2 more sources

Three phosphatase families form a community: The phosphohydrolases that act upon inositol pyrophosphates

FEBS Letters, EarlyView.
Inositol pyrophosphates are energy‐rich signaling molecules that perform critical functions in cells. Three different families of phosphatases hydrolyze the β phosphate of the inositol pyrophosphate molecules: two have narrow specificities and one is promiscuous.
Ronda J. Rolfes
wiley   +1 more source

hSSB1 interacts directly with the MRN complex stimulating its recruitment to DNA double-strand breaks and its endo-nuclease activity

, 2013
hSSB1 is a recently discovered single-stranded DNA binding protein that is essential for efficient repair of DNA double-strand breaks (DSBs) by the homologous recombination pathway.
Bain, Amanda, Khanna, Kum Kum, Menon, Dinoop, White, Malcolm F., Richard, Derek J., Urquhart, Aaron J., Bolderson, Emma, Cubeddu, Liza   +7 more
core   +1 more source

Interaction of the 89K murine cytomegalovirus immediate-early protein with core histones [PDF]

, 1988
The conditions that permit the interaction of immediate-early proteins of murine cytornegalovirus (MCMV) with DNA were studied. Chromatography of extracts from infected cells on MCMV DNA cellulose and calf thymus DNA cellulose showed that pp89, the ...
Münch, Konrad, Koszinowski, Ulrich H., Messerle, Martin, Keil, Günther M.   +3 more
core   +1 more source

ABL kinase‐dependent phosphorylation of SH proteins promotes their direct interaction with CRK family SH2 domains

FEBS Letters, EarlyView.
CT10 regulator of kinase (CRK) and CRK‐Like (CRKL) are signaling adaptors driving cell adhesion, motility, differentiation, and proliferation. SH2‐domain containing (SH) proteins are enriched in YXXP motifs which when phosphorylated create preferred binding sites for CRK family SH2 domains.
Phoebe M. Cousens, Brendan W. Chandler, Anna M. Schmoker, Jaye L. Weinert, Charlotte A. Kearns, Warren T. Yacawych, Amila Šemić, Alicia M. Ebert, Bryan A. Ballif   +8 more
wiley   +1 more source

Detailed studies of the binding mechanism of the Sinorhizobium meliloti transcriptional activator ExpG to DNA

, 2005
Baumgarth B, Bartels FW, Anselmetti D, Becker A, Ros R. Detailed studies of the binding mechanism of the Sinorhizobium meliloti transcriptional activator ExpG to DNA. Microbiology.
Baumgarth, Birgit, Ros, Robert, Bartels, Frank Wilco, Anselmetti, Dario ; https://orcid.org/, Becker, Anke   +4 more
core   +1 more source

Optimising DNA binding to carbon nanotubes by non-covalent methods [PDF]

, 2011
The use of carbon nanotubes as a gene delivery system has been extensively studied in recent years owing to its potential advantages over viral vectors.
Coley, Helen M., Silva, S. Ravi P., Sanz, Vanessa, Flahaut, E, Ewa Borowiak, Petar Lukanov, Vanesa Sanz, Galibert, Anne-Marie, Johnjoe McFadden, Emmanuel Flahaut, Lukanov, Petar, Helen M. Coley, Coley, HM, Borowiak, E, Flahaut, Emmanuel, Lukanov, P, McFadden, J, S. Ravi P. Silva, McFadden, Johnjoe, Borowiak-Palen, Ewa, Sanz, V, Anna Marie Galibert, Silva, SRP, Galibert, AM   +23 more
core   +1 more source

Nuclear domain 10-associated proteins recognize and segregate intranuclear DNA/protein complexes to negate gene expression

Virology Journal, 2012
Background DNA viruses, such as herpes simplex virus type 1 (HSV-1), Simian virus 40 (SV40), and Cytomegaloviruses (CMV), start their replicative processes and transcription at specific nuclear domains known as ND10 (nuclear domain 10, also called PML ...
Rivera-Molina Yisel A, Rojas Bruno R, Tang Qiyi   +2 more
doaj   +1 more source

Reconstructing enzyme evolution by protein engineering

FEBS Letters, EarlyView.
Natural enzyme evolution can be retraced by protein engineering methods such as directed evolution, rational design, and ancestral sequence reconstruction. These approaches reveal how enzymes emerged from ligand‐binding scaffolds, developed varying substrate preferences, formed oligomeric complexes, adapted to environmental changes, and evolved novel ...
Lukas Drexler, Markus R. Busch, Reinhard Sterner   +2 more
wiley   +1 more source

Indirect DNA Readout by an H-NS Related Protein: Structure of the DNA Complex of the C-Terminal Domain of Ler

, 2011
Ler, a member of the H-NS protein family, is the master regulator of the LEE pathogenicity island in virulent Escherichia coli strains. Here, we determined the structure of a complex between the DNA-binding domain of Ler (CT-Ler) and a 15-mer DNA duplex.
Cordeiro Tiago N., Bernado, P., Jesús García, Juárez Antonio, Juarez, Antonio, Bernado, Pau, Pons, Miquel, Schmidt, Holger, Antonio Juárez, Pons Miquel, Miquel Pons, Tiago N. Cordeiro, Madrid Cristina, Holger Schmidt, Cristina Madrid, Pons, M., Cordeiro, Tiago N., Bernadó Peretó, Pau, Griesinger, Christian, Tiago N Cordeiro, García, Jesús, Madrid, C., Pons Vallès, Miquel, Garcia, J., Juárez Giménez, Antonio, Juarez, A., Bernadó Pau, Pau Bernadó, Christian Griesinger, García Jesús, Cordeiro, T., Griesinger, C. ; https://orcid.org/, Madrid, Cristina, Schmidt, H., Madrid Xufré, Cristina, Schmidt Holger, Griesinger Christian   +36 more
core   +1 more source