Results 51 to 60 of about 1,161,651 (341)

The Puromycin Route to Assess Stereo- and Regiochemical Constraints on Peptide Bond Formation in Eukaryotic Ribosomes [PDF]

open access: yes, 2003
We synthesized a series of puromycin analogues to probe the chemical specificity of the ribosome in an intact eukaryotic translation system. These studies reveal that both d-enantiomers and β-amino acid analogues can be incorporated into protein, and ...
Asahara H.   +33 more
core   +1 more source

Automated access to well-defined ionic oligosaccharides [PDF]

open access: yes, 2020
Ionic polysaccharides are part of many biological events, but lack structural characterisation due to challenging purifications and complex synthesis. Four monosaccharides bearing modifications not found in nature are used for the automated synthesis of ...
Delbianco, M.   +5 more
core   +1 more source

Tunable translational control using site-specific unnatural amino acid incorporation in Escherichia coli [PDF]

open access: yesPeerJ, 2015
Translation of target gene transcripts in Escherichia coli harboring UAG amber stop codons can be switched on by the amber-codon-specific incorporation of an exogenously supplied unnatural amino acid, 3-iodo-L-tyrosine.
Yusuke Kato
doaj   +2 more sources

Structural instability impairs function of the UDP‐xylose synthase 1 Ile181Asn variant associated with short‐stature genetic syndrome in humans

open access: yesFEBS Letters, EarlyView.
The Ile181Asn variant of human UDP‐xylose synthase (hUXS1), associated with a short‐stature genetic syndrome, has previously been reported as inactive. Our findings demonstrate that Ile181Asn‐hUXS1 retains catalytic activity similar to the wild‐type but exhibits reduced stability, a looser oligomeric state, and an increased tendency to precipitate ...
Tuo Li   +2 more
wiley   +1 more source

Preparation of Translationally Competent tRNA by Direct Chemical Acylation [PDF]

open access: yes, 2010
Nonsense codon suppression for unnatural amino acid incorporation requires the preparation of a suppressor aminoacyl-tRNA. Chemical acylation strategies are general but inefficient and arduous. A recent report (J. Am. Chem. Soc.
Dougherty, Dennis A., Duffy, Noah H.
core   +2 more sources

Directed Evolution of a Designer Enzyme Featuring an Unnatural Catalytic Amino Acid

open access: yesAngewandte Chemie, 2019
The impressive rate accelerations that enzymes display in nature often result from boosting the inherent catalytic activities of side chains by their precise positioning inside a protein binding pocket.
Clemens Mayer   +4 more
semanticscholar   +1 more source

Evolution of phage with chemically ambiguous proteomes

open access: yesBMC Evolutionary Biology, 2003
Background The widespread introduction of amino acid substitutions into organismal proteomes has occurred during natural evolution, but has been difficult to achieve by directed evolution.
Bull James J   +2 more
doaj   +1 more source

PICALM::MLLT10 translocated leukemia

open access: yesFEBS Letters, EarlyView.
This comprehensive review of PICALM::MLLT10 translocated acute leukemia provides an in‐depth review of the structure and function of CALM, AF10, and the fusion oncoprotein (1). The multifaceted molecular mechanisms of oncogenesis, including nucleocytoplasmic shuttling (2), epigenetic modifications (3), and disruption of endocytosis (4), are then ...
John M. Cullen   +7 more
wiley   +1 more source

Formal Reduction Potential of 3,5-Difluorotyrosine in a Structured Protein: Insight into Multistep Radical Transfer [PDF]

open access: yes, 2013
The reversible Y–O•/Y–OH redox properties of the α[subscript 3]Y model protein allow access to the electrochemical and thermodynamic properties of 3,5-difluorotyrosine.
Armstrong F. A.   +59 more
core   +1 more source

Unnatural amino acid photo-crosslinking of the IKs channel complex demonstrates a KCNE1:KCNQ1 stoichiometry of up to 4:4

open access: yeseLife, 2016
Cardiac repolarization is determined in part by the slow delayed rectifier current (IKs), through the tetrameric voltage-gated ion channel, KCNQ1, and its β-subunit, KCNE1.
Christopher I. Murray   +5 more
semanticscholar   +1 more source

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