Results 11 to 20 of about 938,109 (291)

One-carbon metabolism in cancer [PDF]

open access: yes, 2017
Cells require one-carbon units for nucleotide synthesis, methylation and reductive metabolism, and these pathways support the high proliferative rate of cancer cells.
AJ MacFarlane   +55 more
core   +1 more source

Iterative focused screening with biological fingerprints identifies selective Asc-1 inhibitors distinct from traditional high throughput screening [PDF]

open access: yes, 2017
N-methyl-d-aspartate receptors (NMDARs) mediate glutamatergic signaling that is critical to cognitive processes in the central nervous system, and NMDAR hypofunction is thought to contribute to cognitive impairment observed in both schizophrenia and ...
Amoss, Adam   +18 more
core   +2 more sources

Controlled rotation mechanism of DNA strand exchange by the Hin serine recombinase. [PDF]

open access: yes, 2016
DNA strand exchange by serine recombinases has been proposed to occur by a large-scale rotation of halves of the recombinase tetramer. Here we provide the first direct physical evidence for the subunit rotation mechanism for the Hin serine invertase ...
Johnson, Reid C   +4 more
core   +1 more source

Serine Resolvases [PDF]

open access: yesMicrobiology Spectrum, 2015
ABSTRACT Serine resolvases are an interesting group of site-specific recombinases that, in their native contexts, resolve large fused replicons into smaller separated ones. Some resolvases are encoded by replicative transposons and resolve the transposition product, in which the donor and recipient molecules are fused, into separate replicons.
openaire   +2 more sources

The Bacillus subtilis signaling protein SpoIVB defines a new family of serine peptidases [PDF]

open access: yes, 2002
The protein SpoIVB plays a key role in signaling in the sigma (K) checkpoint of Bacillus subtilis. This regulatory mechanism coordinates late gene expression during development in this organism and we have recently shown SpoIVB to be a serine peptidase ...
Brannigan, J A, Cutting, S M, Hoa, N T
core   +2 more sources

Making serine integrases work for us [PDF]

open access: yes, 2017
DNA site-specific recombinases are enzymes (often associated with mobile DNA elements) that catalyse breaking and rejoining of DNA strands at specific points, thereby bringing about precise genetic rearrangements.
Stark, W. Marshall
core   +1 more source

Diversity in the serine recombinases [PDF]

open access: yesMolecular Microbiology, 2002
SummaryMost site‐specific recombinases fall into one of two families, based on evolutionary and mechanistic relatedness. These are the tyrosine recombinases orλintegrase family and the serine recombinases or resolvase/invertase family. The tyrosine recombinases are structurally diverse and functionally versatile and include integrases, resolvases ...
H M Thorpe, Margaret C. M. Smith
openaire   +3 more sources

Phosphofructokinase 1 Glycosylation Regulates Cell Growth and Metabolism [PDF]

open access: yes, 2012
Cancer cells must satisfy the metabolic demands of rapid cell growth within a continually changing microenvironment. We demonstrated that the dynamic posttranslational modification of proteins by O-linked β-N-acetylglucosamine (O-GlcNAcylation) is a key ...
Clark, Peter M.   +8 more
core   +2 more sources

Orchestrating serine resolvases [PDF]

open access: yesBiochemical Society Transactions, 2010
A remarkable feature of the serine resolvases is their regulation: the wild-type enzymes will catalyse intra- but not inter-molecular recombination, can sense the relative orientation of their sites and can exchange strands directionally, despite the fact that there is no net release of chemical bond energy.
Sherwin P. Montaño   +5 more
openaire   +3 more sources

PRK1 phosphorylates MARCKS at the PKC sites: serine 152, serine 156 and serine 163

open access: yesFEBS Letters, 1996
The 80kDa yristolated lanine‐ich ‐inase ubstrate (MARCKS) in a major in vivo substrate of protein kinase C (PKC). Here we report that MARCKS is a major substrate for the lipid‐activated PKC‐related kinase (PRK1) in cell extracts. Furthermore, PRK1 is shown to phosphorylate MARCKS on the same sites as PKC in vitro.
Dinah Rahman   +5 more
openaire   +2 more sources

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