Results 61 to 70 of about 2,160,956 (299)
Intrinsic disorder in putative protein sequences [PDF]
Proteome Science, 2011 Intrinsically disordered proteins (IDPs) and regions (IDRs) perform a variety of crucial biological functions despite lacking stable tertiary structure under physiological conditions in vitro. State-of-the-art sequence-based predictors of intrinsic disorder are achieving per-residue accuracies over 80%.
Uros Midic, Zoran Obradovic
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Biomolecules, 2018 Calcium is one of the most important second messengers and its intracellular signaling regulates many aspects of cell physiology. Calcium ions, like phosphate ions, are highly charged and thus are able to alter protein conformation upon binding; thereby ...
Ewa A. Grzybowska
doaj +1 more source
FEBS Letters, EarlyView.Proteostasis and the gut microbiota play a key role in shaping host physiology. Microbiota‐derived metabolites, vitamins, and RNA modulate host proteostasis. Findings from model systems, including C. elegans, indicate microbes can either stabilize or disrupt host proteostasis.
Abhishek Anil Dubey, Maria Ermolaeva
wiley +1 more source
Unreported Intrinsic Disorder in Proteins: Disorder Emergency Room
, 2015 This article continues an “Unreported Intrinsic Disorder in Proteins” series, the goal of which is to expose some interesting cases of missed (or overlooked, or ignored) disorder in proteins.
Uversky, Vladimir N.
core +1 more source
Intrinsically Disordered Proteins in Neurodegeneration [PDF]
Biophysical Journal, 2016 Intrinsically disordered proteins (IDPs) have gained wide recognition due to their versatile roles in cell physiology and pathology. A large repertoire of IDPs has been implicated in numerous diseases, making them potential targets for therapeutic intervention.
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Self‐recognition by an intrinsically disordered protein [PDF]
FEBS Letters, 2008 The intrinsically disordered translocation domain (T‐domain) of the protein antibiotic colicin N binds to periplasmic receptors of target Escherichia coli cells in order to penetrate their inner membranes. We report here that the specific 27 consecutive residues of the T‐domain of colicin N known to bind to the helper protein TolA in target cells also ...
Hecht O +7 more
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Dual-Family Peptidylprolyl Isomerases (Immunophilins) of Select Monocellular Organisms
Biomolecules, 2018 The dual-family peptidylprolyl cis-trans isomerases (immunophilins) represent a naturally occurring chimera of the classical FK506-binding protein (FKBP) and cyclophilin (CYN), connected by a flexible linker.
Sailen Barik
doaj +1 more source
Investigating transcription factor dynamics in health and disease using FRAP
FEBS Letters, EarlyView.FRAP analysis of GFP‐tagged transcription factors reveals how molecular mobility and target engagement change in response to drug treatment. By combining live‐cell imaging, quantitative model fitting, and statistical analysis, this approach uncovers transcription factor dynamics linked to disease mechanisms, providing a powerful framework for ...
Kannan Govindaraj +3 more
wiley +1 more source
Intrinsic disorder in E1B 55K.
, 2019 PONDR VLXT, PONDR XL1_XT, PONDR VL3-BA, PONDR VSL2, IUPred and DISOPRED predictors were used for disorder analysis. All predictors indicate a high level of intrinsic disorder in the N- and C-terminus.
Thomas Dobner (181801) +12 more
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HIV Vaccine Mystery and Viral Shell Disorder
Biomolecules, 2019 Hundreds of billions of dollars have been spent for over three decades in the search for an effective human immunodeficiency virus (HIV) vaccine with no success.
Gerard Kian-Meng Goh +3 more
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