Results 21 to 30 of about 83,143 (263)
IUCrJ, 2020 Protein dimerization or oligomerization resulting from swapping part of the protein between neighboring polypeptide chains is known to play a key role in the regulation of protein function and in the formation of protein aggregates.
Kitaik Lee +12 more
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Frontiers in Microbiology, 2021 Cotton is a commercial crop of global importance. The major threat challenging the productivity in cotton has been the lepidopteron insect pest Helicoverpa armigera or cotton bollworm which voraciously feeds on various plant parts.
Kesiraju Karthik +4 more
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Retrotransposon Domain Swapping [PDF]
The Plant Cell, 2010 Whether you consider them major genomic parasites or potentially major drivers of genome expansion, long terminal repeat (LTR) retrotransposons are major, making up 15 to 90% of plant nuclear genomes (reviewed in Sabot and Schulman, 2006). These elements transpose by a replicate-and-paste mechanism, wherein an RNA copy of the retrotransposon is reverse
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Deposition Diseases and 3D Domain Swapping [PDF]
Structure, 2006 Protein aggregation is a feature of both normal cellular assemblies and pathological protein depositions. Although the limited order of aggregates has often impeded their structural characterization, 3D domain swapping has been implicated in the formation of several protein aggregates.
Bennett, Melanie J. +2 more
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Synthetic and Systems Biotechnology, 2020 Modular polyketide synthases (PKSs) are a multidomain megasynthase class of biosynthetic enzymes that have great promise for the development of new compounds, from new pharmaceuticals to high value commodity and specialty chemicals.
Erin E. Drufva +2 more
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Amyloid-like fibrils from a domain-swapping protein feature a parallel, in-register conformation without native-like interactions [PDF]
, 2011 The formation of amyloid-like fibrils is characteristic of various diseases, but the underlying mechanism and the factors that determine whether, when, and how proteins form amyloid, remain uncertain.
Hoop, CL +4 more
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Trimeric domain-swapped barnase
Proceedings of the National Academy of Sciences, 1999 The structure of a trimeric domain-swapped form of barnase (EC 3.1.27.3 ) was determined by x-ray crystallography at a resolution of 2.2 Å from crystals of space group R 32. Residues 1–36 of one molecule associate with residues 41–110 from another molecule related through threefold symmetry ...
Zegers, Nathalie +2 more
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Crystal structure of domain‐swapped STE20 OSR1 kinase domain [PDF]
Protein Science, 2009 AbstractOSR1 (oxidative stress‐responsive‐1) and SPAK (Ste20/Sps1‐related proline/alanine‐rich kinase) belong to the GCK‐VI subfamily of Ste20 group kinases. OSR1 and SPAK are key regulators of NKCCs (Na+/K+/2Cl− cotransporters) and activated by WNK family members (with‐no‐lysine kinase), mutations of which are known to cause Gordon syndrome, an ...
Seung-Jae, Lee +2 more
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Molecular Therapy: Methods & Clinical Development, 2022 Recent clinical successes have intensified interest in using adeno-associated virus (AAV) vectors for therapeutic gene delivery. The liver is a key clinical target, given its critical physiological functions and involvement in a wide range of genetic ...
Marti Cabanes-Creus +14 more
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Domain-swapping of mesophilic xylanase with hyper-thermophilic glucanase
BMC Biotechnology, 2012 Background Domain fusion is limited at enzyme one terminus. The issue was explored by swapping a mesophilic Aspergillus niger GH11 xylanase (Xyn) with a hyper-thermophilic Thermotoga maritima glucanase (Glu) to construct two chimeras, Xyn-Glu and Glu-Xyn,
Liu Liangwei +5 more
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