Results 41 to 50 of about 41,338 (239)
Folding of a designed simple ankyrin repeat protein [PDF]
AbstractAnkyrin repeats (AR) are 33‐residue motifs containing a β‐turn, followed by two α‐helices connected by a loop. AR occur in tandem arrangements and stack side‐by‐side to form elongated domains involved in very different cellular tasks. Recently, consensus libraries of AR repeats were constructed.
V Sathya, Devi +5 more
openaire +2 more sources
Genome-Wide Association Study for Muscle Fat Content and Abdominal Fat Traits in Common Carp (Cyprinus carpio). [PDF]
Muscle fat content is an important phenotypic trait in fish, as it affects the nutritional, technical and sensory qualities of flesh. To identify loci and candidate genes associated with muscle fat content and abdominal fat traits, we performed a genome ...
Xianhu Zheng +5 more
doaj +1 more source
A novel mechanism of RNase L inhibition: Theiler\u27s virus L* protein prevents 2-5A from binding to RNase L [PDF]
The OAS/RNase L pathway is one of the best-characterized effector pathways of the IFN antiviral response. It inhibits the replication of many viruses and ultimately promotes apoptosis of infected cells, contributing to the control of virus spread ...
Drappier, Melissa +8 more
core +4 more sources
Functional diversity of ankyrin repeats in microbial proteins [PDF]
The ankyrin repeat (ANK) is the most common protein-protein interaction motif in nature, and is predominantly found in eukaryotic proteins. Genome sequencing of various pathogenic or symbiotic bacteria and eukaryotic viruses has identified numerous genes encoding ANK-containing proteins that are proposed to have been acquired from eukaryotes by ...
Souhaila, Al-Khodor +3 more
openaire +2 more sources
The expression of Muscle ankyrin repeat proteins in brown adipose tissue [PDF]
MARP family members CARP, Ankrd2 and DARP are expressed in the striated muscle, while DARP protein is also detected in brown adipose tissue (BAT). Taking into account recent findings concerning the common origin of muscle and brown fat, expression of ...
Rakićević Ljiljana +3 more
doaj +1 more source
Probing Muscle Ankyrin‐Repeat Protein (MARP) Structure and Function [PDF]
ABSTRACTMuscle ankyrin‐repeat proteins (MARPs) have been shown to serve diverse functions within cardiac and skeletal muscle cells. Apart from their interactions with sarcomeric proteins like titin or myopalladin that locate them along myofilaments, MARPs are able to shuttle to the nucleus where they act as modulators for a variety of transcription ...
Alexander Shiang Lun +2 more
openaire +5 more sources
Structural basis of diverse membrane target recognitions by ankyrins
Ankyrin adaptors together with their spectrin partners coordinate diverse ion channels and cell adhesion molecules within plasma membrane domains and thereby promote physiological activities including fast signaling in the heart and nervous system ...
Chao Wang +6 more
doaj +1 more source
Biological Regulation via Ankyrin Repeat Folding [PDF]
By mimicking the phosphorylation of p19(INK4d), a tumor suppressor containing five ankyrin repeats, the native state could be destabilized to such an extent that only a partially folded state is populated at physiological temperature. This partly folded state, which mimics an on-pathway folding intermediate lacking structure in ankyrin repeats 1 and 2,
openaire +2 more sources
Capturing coevolutionary signals in repeat proteins [PDF]
The analysis of correlations of amino acid occurrences in globular proteins has led to the development of statistical tools that can identify native contacts -- portions of the chains that come to close distance in folded structural ensembles.
Espada, Rocío +4 more
core +5 more sources
Protein Repeats from First Principles [PDF]
Some natural proteins display recurrent structural patterns. Despite being highly similar at the tertiary structure level, repeating patterns within a single repeat protein can be extremely variable at the sequence level. We use a mathematical definition
Becher, Veronica Andrea +4 more
core +1 more source

