Qingyu Tang

MeSH headings : Cell Adhesion Molecules / metabolism; Cell Adhesion Molecules / physiology; DNA / metabolism; DNA-Binding Proteins / metabolism; Humans; Microscopy, Atomic Force / methods; Models, Molecular; Multiprotein Complexes / metabolism; Protein Binding; Protein Isoforms / metabolism; Shelterin Complex / metabolism; Shelterin Complex / physiology; Telomere / metabolism; Telomere-Binding Proteins / metabolism; Telomere-Binding Proteins / physiology; Telomeric Repeat Binding Protein 1 / metabolism; Telomeric Repeat Binding Protein 1 / physiology; Telomeric Repeat Binding Protein 2 / metabolism; Telomeric Repeat Binding Protein 2 / physiology

TL;DR: Analysis of DNA molecular structures promoted by TRF1-TIN2 interaction supports a molecular model in which protein assemblies at telomeres are heterogeneous with distinct subcomplexes and full shelterin complexes playing distinct roles in telomere protection and elongation. (via Semantic Scholar)

MeSH headings : Arabidopsis / metabolism; Arabidopsis Proteins / metabolism; Flowers / growth & development; Ovule / metabolism; Plant Proteins / metabolism; Pollen / metabolism; Pollen Tube / growth & development; Pollination; Protein Kinases / metabolism; Protein Serine-Threonine Kinases / metabolism; Reproduction / physiology; Signal Transduction / physiology

TL;DR: The authors' structural analyses of PRK3 have provided a template for future functional studies of the PRK family of LRR-RLK receptors in the regulation of pollen tube development, and determined the crystal structure of the extracellular domain (ecd) ofPRK3 at 2.5 Å, which resembles the SERKfamily of plant co-receptors. (via Semantic Scholar)