Results 31 to 40 of about 117,832 (333)

Posttranslational modification of a vanadium nitrogenase [PDF]

open access: yesMicrobiologyOpen, 2015
In microbes that fix nitrogen, nitrogenase catalyzes the conversion of N2 to ammonia in an ATP-demanding reaction. To help conserve energy some bacteria inhibit nitrogenase activity upon exposure to ammonium. The purple nonsulfur phototrophic bacterium Rhodopseudomonas palustris strain CGA009 can synthesize three functional nitrogenase isoenzymes: a ...
Erin K. Heiniger, Caroline S. Harwood
openaire   +3 more sources

Posttranslational Modifications and the Immunogenicity of Biotherapeutics [PDF]

open access: yesJournal of Immunology Research, 2016
Whilst the amino acid sequence of a protein is determined by its gene sequence, the final structure and function are determined by posttranslational modifications (PTMs), including quality control (QC) in the endoplasmic reticulum (ER) and during passage through the Golgi apparatus.
openaire   +4 more sources

Posttranslational Modifications of RAS Proteins [PDF]

open access: yesCold Spring Harbor Perspectives in Medicine, 2018
The three human RAS genes encode four proteins that play central roles in oncogenesis by acting as binary molecular switches that regulate signaling pathways for growth and differentiation. Each is subject to a set of posttranslational modifications (PTMs) that modify their activity or are required for membrane targeting.
Ian M. Ahearn, Mo Zhou, Mark R. Philips
openaire   +3 more sources

EF-P Posttranslational Modification Has Variable Impact on Polyproline Translation in Bacillus subtilis

open access: yesmBio, 2018
Elongation factor P (EF-P) is a ubiquitous translation factor that facilitates translation of polyproline motifs. In order to perform this function, EF-P generally requires posttranslational modification (PTM) on a conserved residue.
Anne Witzky   +6 more
doaj   +1 more source

A Novel Peptide-Based SILAC Method to Identify the Posttranslational Modifications Provides Evidence for Unconventional Ubiquitination in the ER-Associated Degradation Pathway. [PDF]

open access: yes, 2013
The endoplasmic reticulum-associated degradation (ERAD) pathway is responsible for disposing misfolded proteins from the endoplasmic reticulum by inducing their ubiquitination and degradation.
Anania, Veronica   +4 more
core   +3 more sources

Posttranslational modifications of proopiomelanocortin in vertebrates and their biological significance

open access: yesFrontiers in Endocrinology, 2013
Proopiomelanocortin (POMC) is the precursor of several peptide hormones generated in the pituitary gland. After biosynthesis, POMC undergoes several posttranslational modifications, including proteolytic cleavage, acetylation, amidation, phosphorylation,
Akiyoshi eTakahashi, Kanta eMizusawa
doaj   +1 more source

Phosphofructokinase 1 Glycosylation Regulates Cell Growth and Metabolism [PDF]

open access: yes, 2012
Cancer cells must satisfy the metabolic demands of rapid cell growth within a continually changing microenvironment. We demonstrated that the dynamic posttranslational modification of proteins by O-linked β-N-acetylglucosamine (O-GlcNAcylation) is a key ...
Clark, Peter M.   +8 more
core   +2 more sources

Posttranslational Modifications in Innate Immunity [PDF]

open access: yesJournal of Innate Immunity, 2012
Taking into account that a large number of nascent gene translation products are subject to limited proteolytic processing, proteolysis is one of the most common PTMs and due to its irreversible nature needs to be very precisely controlled on multiple levels.
openaire   +4 more sources

Posttranslational Modification and Quality Control [PDF]

open access: yesCirculation Research, 2013
Protein quality control functions to minimize the level and toxicity of misfolded proteins in the cell. Protein quality control is performed by intricate collaboration among chaperones and target protein degradation. The latter is performed primarily by the ubiquitin-proteasome system and perhaps autophagy.
Xuejun Wang, J. Scott Pattison, Huabo Su
openaire   +2 more sources

PHOSIDA 2011: the posttranslational modification database [PDF]

open access: goldNucleic Acids Research, 2010
The primary purpose of PHOSIDA (http://www.phosida.com) is to manage posttranslational modification sites of various species ranging from bacteria to human. Since its last report, PHOSIDA has grown significantly in size and evolved in scope. It comprises more than 80,000 phosphorylated, N-glycosylated or acetylated sites from nine different species ...
Florian Gnad   +2 more
openalex   +4 more sources

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