Results 21 to 30 of about 23,098 (204)
Nanospring behaviour of ankyrin repeats [PDF]
Nature, 2006 Ankyrin repeats are an amino-acid motif believed to function in protein recognition; they are present in tandem copies in diverse proteins in nearly all phyla. Ankyrin repeats contain antiparallel alpha-helices that can stack to form a superhelical spiral. Visual inspection of the extrapolated structure of 24 ankyrin-R repeats indicates the possibility
Gwangrog, Lee +5 more
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Mechanical Unfolding of an Ankyrin Repeat Protein [PDF]
Biophysical Journal, 2010 Ankryin repeat proteins comprise tandem arrays of a 33-residue, predominantly alpha-helical motif that stacks roughly linearly to produce elongated and superhelical structures. They function as scaffolds mediating a diverse range of protein-protein interactions, and some have been proposed to play a role in mechanical signal transduction processes in ...
Serquera D. +5 more
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Production of a common epitope specific anti-ankyrin monoclonal antibody
Journal of Associated Medical Sciences, 2022 Background: Ankyrin (Ank) is a protein family with crucial roles in retaining normal cellular physiology. In addition, ankyrin offers the potential as a non-antibody binder against various biomolecules.
On-anong Juntit +4 more
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Communications Biology, 2023 Ankyrin repeat and LEM-domain containing protein 1 (ANKLE1) cleaves the mitochondrial genome during erythropoiesis and ectopic expression of ANKLE1 promotes genome instability and apoptotic resistance, which contributes to breast cancer risk.
Piotr Przanowski +2 more
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Folding of a designed simple ankyrin repeat protein [PDF]
Protein Science, 2004 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.
Devi VS +5 more
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Functional diversity of ankyrin repeats in microbial proteins [PDF]
Trends in Microbiology, 2010 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
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Identifying tandem Ankyrin repeats in protein structures [PDF]
BMC Bioinformatics, 2014 Tandem repetition of structural motifs in proteins is frequently observed across all forms of life. Topology of repeating unit and its frequency of occurrence are associated to a wide range of structural and functional roles in diverse proteins, and defects in repeat proteins have been associated with a number of diseases.
Broto Chakrabarty, Nita Parekh
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Distinct conformations of the HIV-1 V3 loop crown are targetable for broad neutralization
Nature Communications, 2021 The V3-crown of the HIV-1 envelope protein largely elicits non-neutralizing antibodies. Here, the authors show that the V3-crown can be targeted by broadly neutralizing designed ankyrin repeat proteins recognizing two conformations one of which resembles
Nikolas Friedrich +24 more
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Multifunctional protein: cardiac ankyrin repeat protein [PDF]
Journal of Zhejiang University-SCIENCE B, 2016 Cardiac ankyrin repeat protein (CARP) not only serves as an important component of muscle sarcomere in the cytoplasm, but also acts as a transcription co-factor in the nucleus. Previous studies have demonstrated that CARP is up-regulated in some cardiovascular disorders and muscle diseases; however, its role in these diseases remains controversial now.
Na, Zhang, Xiao-Jie, Xie, Jian-An, Wang
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Resolving the fine structure in the energy landscapes of repeat proteins
QRB Discovery, 2022 Ankyrin (ANK) repeat proteins are coded by tandem occurrences of patterns with around 33 amino acids. They often mediate protein–protein interactions in a diversity of biological systems.
Murilo N. Sanches +6 more
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