Publications by authors named "Chenxue Ma"

Introduction: This study aimed to evaluate treatment outcomes of regenerative endodontic treatment (RET) in nonvital immature permanent teeth due to developmental malformation and trauma, and to analyze the influence of etiology on the prognosis.

Methods: Fifty-five cases were included and divided into a malformation group (n = 33) and a trauma group (n = 22). Treatment outcomes were classified as healed, healing, and failure.

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Article Synopsis
  • PSD-95 is an important protein in neurons that helps organize signaling structures, and its function is influenced by phosphorylation, although studying this has been challenging.
  • Researchers introduced specific phosphorylation sites on PSD-95 and created 11 different variants to analyze how these changes affected its interactions and the formation of protein complexes.
  • They discovered that phosphorylation at Ser78 reduced phase separation with GluN2B and stargazin, while phosphorylation at Ser116 promoted phase separation with stargazin, offering new insights into how PSD-95 is regulated and how it interacts within the postsynaptic density.
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Hantzsch esters (HEs) served as two-carbon partners in a copper(I)-catalyzed enantioselective [3 + 2] annulation with racemic 2-(hetero)aryl--sulfonyl aziridines via kinetic resolution to provide pyrrolo[2,3-]tetrahydropyridines containing multiple contiguous stereogenic centers including all-carbon quaternary centers in excellent yields and enantiopurities and moderate-to-excellent diastereoselectivities. Mainly dependent upon the structures of the aziridines, a competitive hydrogenolysis process with HEs as the hydrogen source was also observed in some cases.

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Ionotropic glutamate delta receptors do not bind glutamate and do not generate ionic current, resulting in difficulty in studying the function and trafficking of these receptors. Here, we utilize chimeric constructs, in which the ligand-binding domain of GluD1 is replaced by that of GluK1, to examine its synaptic trafficking and plasticity. GluD1 trafficked to the synapse, but was incapable of expressing long-term potentiation (LTP).

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Kidney ankyrin repeat-containing proteins (KANK1/2/3/4) belong to a family of scaffold proteins, playing critical roles in cytoskeleton organization, cell polarity, and migration. Mutations in KANK proteins are implicated in cancers and genetic diseases, such as nephrotic syndrome. KANK proteins can bind various target proteins through different protein regions, including a highly conserved ankyrin repeat domain (ANKRD).

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