Results 131 to 140 of about 55,224 (274)

Non‐canonical PKG1 regulation in cardiovascular health and disease

open access: yesBritish Journal of Pharmacology, EarlyView.
It is well established that the cyclic GMP‐dependent protein kinase I (PKG1) is canonically activated by cyclic guanosine monophosphate (cGMP), enabling its regulation of vascular tone, cardiac function and smooth muscle homeostasis. However, diverse non‐canonical stimuli of PKG1 have also been identified.
Jie Su, Joseph Robert Burgoyne
wiley   +1 more source

DNMT3a in the hippocampal CA1 is crucial in the acquisition of morphine self‐administration in rats [PDF]

open access: yes, 2019
Drug‐reinforced excessive operant responding is one fundamental feature of long-lasting addiction‐like behaviors and relapse in animals. However, the transcriptional regulatory mechanisms responsible for the persistent drug‐specific (not natural rewards)
Duan, Ying   +8 more
core   +1 more source

PLGA‐particle‐based vaccine induces SARS‐CoV‐2‐specific antibody and T‐cell responses

open access: yesBritish Journal of Pharmacology, EarlyView.
A novel coronavirus disease 2019 (COVID‐19) vaccine encapsulating recombinant severe acute respiratory syndrome coronavirus 2 (SARS‐CoV‐2) spike receptor binding domain (RBD) with the double stranded RNA (dsRNA) analogue Riboxxim induces robust systemic and respiratory T‐ and B‐cell responses in mice.
Dennis Horvath   +6 more
wiley   +1 more source

SLPI/FBW7/c‐Myc Axis Reduces Gemcitabine Sensitivity in PDAC by Enhancing Glycolysis and Impairing NK Cell Immunity

open access: yesCancer Science, EarlyView.
SLPI reduces the sensitivity of PDAC to gemcitabine by competing with FBW7 for binding to c‐Myc, thereby disrupting FBW7‐dependent ubiquitination and proteasomal degradation of c‐Myc, leading to increased c‐Myc stability and expression. SLPI knockdown could significantly increase gemcitabine sensitivity to gemcitabine‐induced direct cytotoxicity and NK
Haofei Chen   +7 more
wiley   +1 more source

Plant organelle C‐to‐U RNA editing factors can operate successfully in yeast (Saccharomyces cerevisiae) as an easily amenable eukaryotic system for their functional analysis

open access: yesThe FEBS Journal, EarlyView.
Plant‐type pentatricopeptide repeat proteins capable of C‐to‐U RNA editing perform faithfully when expressed in a new heterologous system, the yeast Saccharomyces cerevisiae. They were tested with constitutive and inducible expression and with a set of different solubility tags. PPR56, PPR65, and PPR78 from P.
Shyam Ramanathan   +4 more
wiley   +1 more source

High fludarabine exposure and relationship with treatment-related mortality after nonmyeloablative hematopoietic cell transplantation. [PDF]

open access: yes, 2011
Despite its common use in nonmyeloablative preparative regimens, the pharmacokinetics of fludarabine are poorly characterized in hematopoietic cell transplantation (HCT) recipients and exposure-response relationships remain undefined.
Brunstein, CG   +9 more
core   +1 more source

Harnessing S. cerevisiae to advance the engineering of pentatricopeptide repeat proteins

open access: yesThe FEBS Journal, EarlyView.
Heterologous expression systems have been instrumental in furthering our understanding of plant RNA editing proteins. In this commentary, we discuss how the establishment of yeast as a model for studying plant RNA editing by Ramanathan et al. could advance the engineering of pentatricopeptide repeat proteins, and how in return pentatricopeptide repeat ...
Farley M. Kwok van der Giezen, Ian Small
wiley   +1 more source

Deoxycytidine Kinase

open access: yesJournal of Biological Chemistry, 1969
JOHN P. DURHAM, DAVID H. IVES
openaire   +1 more source

Comparative evaluation of noncanonical amino acids as site‐specific NMR probes for the complex of E. coli SSB with single‐stranded DNA without isotope labelling

open access: yesThe FEBS Journal, EarlyView.
Genetic encoding of noncanonical amino acids (ncAA) enables their site‐specific installation in proteins. This work compares the nuclear magnetic resonance (NMR) performance of different ncAAs in a large protein−DNA complex (~ 100 kDa) without isotope labelling. The ncAAs deliver readily detectable NMR signals in the complex between E.
Sreelakshmi Mekkattu Tharayil   +7 more
wiley   +1 more source

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