Results 61 to 70 of about 199,615 (291)
Identification and Interrogation of Combinatorial Histone Modifications
Frontiers in Genetics, 2013 Histone proteins are dynamically modified to mediate a variety of cellular processes including gene transcription, DNA damage repair, and apoptosis. Regulation of these processes occurs through the recruitment of non-histone proteins to chromatin by ...
Kelly R Karch +3 more
doaj +1 more source
Analyzing peptides and proteins by mass spectrometry: principles and applications in proteomics [PDF]
, 2012 Podeu consultar el llibre complet a: http://hdl.handle.net/2445/32166The study of proteins has been a key element in biomedicine and biotechnology because of their important role in cell functions or enzymatic activity. Cells are the basic unit of living
Estanyol i Ullate, Josep Maria +3 more
core +1 more source
Characterisation of urinary WFDC12 in small nocturnal basal primates, mouse lemurs (Microcebus spp.) [PDF]
, 2017 Mouse lemurs are basal primates that rely on chemo- and acoustic signalling for social interactions in their dispersed social systems. We examined the urinary protein content of two mouse lemurs species, within and outside the breeding season, to assess ...
Beynon, RJ +8 more
core +1 more source
Real‐time assay of ribonucleotide reductase activity with a fluorescent RNA aptamer
FEBS Letters, EarlyView.Ribonucleotide reductases (RNR) synthesize DNA building blocks de novo, making them crucial in DNA replication and drug targeting. FLARE introduces the first single‐tube real‐time coupled RNR assay, which enables isothermal tracking of RNR activity at nanomolar enzyme levels and allows the reconstruction of allosteric regulatory patterns and rapid ...
Jacopo De Capitani +4 more
wiley +1 more source
Regulation of nitric oxide signaling by formation of a distal receptor-ligand complex. [PDF]
, 2017 The binding of nitric oxide (NO) to the heme cofactor of heme-nitric oxide/oxygen binding (H-NOX) proteins can lead to the dissociation of the heme-ligating histidine residue and yield a five-coordinate nitrosyl complex, an important step for NO ...
Britt, R David +5 more
core +1 more source
Disordered but rhythmic—the role of intrinsic protein disorder in eukaryotic circadian timing
FEBS Letters, EarlyView.Unstructured domains known as intrinsically disordered regions (IDRs) are present in nearly every part of the eukaryotic core circadian oscillator. IDRs enable many diverse inter‐ and intramolecular interactions that support clock function. IDR conformations are highly tunable by post‐translational modifications and environmental conditions, which ...
Emery T. Usher, Jacqueline F. Pelham
wiley +1 more source
SLAS TechnologyCovalent drug discovery has garnered renewed interest due to its potential to target proteins previously considered ''undruggable.'' Intact protein mass spectrometry (MS) is a critical technique for providing direct evidence of covalent drug ...
Ronghai Cheng +4 more
doaj +1 more source
In situ analysis of intact proteins by ion mobility mass spectrometry [PDF]
TrAC Trends in Analytical Chemistry, 2020 Abstract We describe ion mobility mass spectrometry techniques for the in situ analysis of intact proteins, i.e., the analysis of proteins directly from their biological environment. The benefits of in situ analysis include those associated more broadly with analysis of intact proteins, e.g., retention of connectivity between post-translational ...
Emma K. Sisley +2 more
openaire +1 more source
Protein pyrophosphorylation by inositol pyrophosphates — detection, function, and regulation
FEBS Letters, EarlyView.Protein pyrophosphorylation is an unusual signaling mechanism that was discovered two decades ago. It can be driven by inositol pyrophosphate messengers and influences various cellular processes. Herein, we summarize the research progress and challenges of this field, covering pathways found to be regulated by this posttranslational modification as ...
Sarah Lampe +3 more
wiley +1 more source
Photoaffinity labeling with cholesterol analogues precisely maps a cholesterol-binding site in voltage-dependent anion channel-1 [PDF]
, 2017 Voltage-dependent anion channel-1 (VDAC1) is a highly regulated β-barrel membrane protein that mediates transport of ions and metabolites between the mitochondria and cytosol of the cell.
Abramson, Jeff +10 more
core +3 more sources