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Hongjiang Wu

Researcher at University of California, San Diego

Publications -  20
Citations -  1521

Hongjiang Wu is an academic researcher from University of California, San Diego. The author has contributed to research in topics: Chromogranin A & CREB. The author has an hindex of 16, co-authored 19 publications receiving 1462 citations. Previous affiliations of Hongjiang Wu include Veterans Health Administration & University of California, Berkeley.

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Book ChapterDOI

A novel, catecholamine release-inhibitory peptide from chromogranin A: autocrine control of nicotinic cholinergic-stimulated exocytosis.

TL;DR: It is highlighted that exposure of PC12 cells to a spectrum of nicotine doses, alone or with catestatin (10 μM), revealed that nicotine never overcameCatestatin's inhibition of norepinephrine release, even at the highest nicotine dosage, indicating that catstatin is likely to be a noncompetitive nicotinic cholinergic antagonist.
Journal ArticleDOI

Assignment of the chromogranin a (chga) locus to homologous regions on mouse chromosome 12 and rat chromosome 6

TL;DR: In mouse, rat, and human, chromogranin A is in a conserved region with nearby markers including the immunoglobulin heavy chain locus, while in the human genome, its locus has previously been positioned on the long arm of Chromosome 14 in the 14q32 region.
Journal ArticleDOI

Processing of chromaffin granule proteins : a profusion of proteases ?

TL;DR: The potential role of specific proteases in the processing of proenkephalin and the chromogranins is discussed, in particular, in the context of possible processing clues available from recent analysis of cDNA and genomic intron/exon structure.
Book ChapterDOI

Regulation of Chromogranin a Transcription and Catecholamine Secretion by the Neuropeptide Pacap

TL;DR: A model depicting putative signal transduction pathways underlying PACAP-induced CGA transcription and catecholamine secretion in PC12 cells is proposed and indicates that initial secretion is mediated by an L-type VOCC, while extended secretion may involve a SOCC activated through a Gq/11/PLC-β/PI signaling pathway.
Posted ContentDOI

Full-length αIIbβ3 CryoEM structure reveals intact integrin initiate-activation intrinsic architecture

TL;DR: In this article , the structure of integrin αIIbβ3 was resolved at 3Å resolution, revealing the overall topology of the heterodimer with the transmembrane (TM) helices and the head region ligand-binding domain tucked in a specific angle proximity to the TM region.