Post-translational modifications in proteins: resources, tools and prediction methods
S Ramazi, J Zahiri - Database, 2021 - academic.oup.com
Posttranslational modifications (PTMs) refer to amino acid side chain modification in some
proteins after their biosynthesis. There are more than 400 different types of PTMs affecting …
proteins after their biosynthesis. There are more than 400 different types of PTMs affecting …
Evaluation of post-translational modifications in histone proteins: A review on histone modification defects in developmental and neurological disorders
S Ramazi, A Allahverdi, J Zahiri - Journal of biosciences, 2020 - Springer
Post-translational modification (PTM) in histone proteins is a covalent modification which
mainly consists of methylation, phosphorylation, acetylation, ubiquitylation, SUMOylation …
mainly consists of methylation, phosphorylation, acetylation, ubiquitylation, SUMOylation …
iFeature: a Python package and web server for features extraction and selection from protein and peptide sequences
Structural and physiochemical descriptors extracted from sequence data have been widely
used to represent sequences and predict structural, functional, expression and interaction …
used to represent sequences and predict structural, functional, expression and interaction …
Most non-canonical proteins uniquely populate the proteome or immunopeptidome
Combining RNA sequencing, ribosome profiling, and mass spectrometry, we elucidate the
contribution of non-canonical translation to the proteome and major histocompatibility …
contribution of non-canonical translation to the proteome and major histocompatibility …
iLearn: an integrated platform and meta-learner for feature engineering, machine-learning analysis and modeling of DNA, RNA and protein sequence data
Z Chen, P Zhao, F Li, TT Marquez-Lago… - Briefings in …, 2020 - academic.oup.com
With the explosive growth of biological sequences generated in the post-genomic era, one
of the most challenging problems in bioinformatics and computational biology is to …
of the most challenging problems in bioinformatics and computational biology is to …
Intrinsically disordered proteins and intrinsically disordered protein regions
CJ Oldfield, AK Dunker - Annual review of biochemistry, 2014 - annualreviews.org
Intrinsically disordered proteins (IDPs) and IDP regions fail to form a stable structure, yet
they exhibit biological activities. Their mobile flexibility and structural instability are encoded …
they exhibit biological activities. Their mobile flexibility and structural instability are encoded …
Post-translational modifications of G Protein–Coupled receptors control cellular signaling dynamics in space and time
G protein–coupled receptors (GPCRs) are a large family comprising> 800 signaling
receptors that regulate numerous cellular and physiologic responses. GPCRs have been …
receptors that regulate numerous cellular and physiologic responses. GPCRs have been …
[HTML][HTML] PDL1 signals through conserved sequence motifs to overcome interferon-mediated cytotoxicity
M Gato-Cañas, M Zuazo, H Arasanz, M Ibañez-Vea… - Cell reports, 2017 - cell.com
PDL1 blockade produces remarkable clinical responses, thought to occur by T cell
reactivation through prevention of PDL1-PD1 T cell inhibitory interactions. Here, we find that …
reactivation through prevention of PDL1-PD1 T cell inhibitory interactions. Here, we find that …
Introducing protein intrinsic disorder
Proteins are the major component of the living cell. They play crucial roles in the
maintenance of life, and their dysfunctions are known to cause different pathologies. One of …
maintenance of life, and their dysfunctions are known to cause different pathologies. One of …
Intrinsic disorder and posttranslational modifications: the darker side of the biological dark matter
AL Darling, VN Uversky - Frontiers in genetics, 2018 - frontiersin.org
Intrinsically disordered proteins (IDPs) and intrinsically disordered protein regions (IDPRs)
are functional proteins and domains that devoid stable secondary and/or tertiary structure …
are functional proteins and domains that devoid stable secondary and/or tertiary structure …