Cathepsin L in secretory vesicles functions as a prohormone-processing enzyme for production of the enkephalin peptide neurotransmitter. - Wikidata - awgldk - TriplyDB

Cathepsin L in secretory vesicles functions as a prohormone-processing enzyme for production of the enkephalin peptide neurotransmitter.

Cathepsin L in secretory vesicles functions as a prohormone-processing enzyme for production of the enkephalin peptide neurotransmitter.

http://www.wikidata.org/entity/Q35234967

about

Chromogranin A: a new proposal for trafficking, processing and induction of granule biogenesis Cysteine cathepsins: their role in tumor progression and recent trends in the development of imaging probes Processing of Capsid Protein by Cathepsin L Plays a Crucial Role in Replication of Japanese Encephalitis Virus in Neural and Macrophage Cells Toxoplasma gondii Cathepsin L Is the Primary Target of the Invasion-inhibitory Compound Morpholinurea-leucyl-homophenyl-vinyl Sulfone Phenyl The protein architecture of human secretory vesicles reveals differential regulation of signaling molecule secretion by protein kinases Cathepsin L colocalizes with chromogranin a in chromaffin vesicles to generate active peptides Cathepsin L participates in the production of neuropeptide Y in secretory vesicles, demonstrated by protease gene knockout and expression Novel odors affect gene expression for cytokines and proteinases in the rat amygdala and hippocampus Transcriptomic analysis of endangered Chinese salamander: identification of immune, sex and reproduction-related genes and genetic markers Promiscuous processing of human alphabeta-protryptases by cathepsins L, B, and C Cathepsin L is responsible for processing and activation of proheparanase through multiple cleavages of a linker segment.Proteolytic fragments of chromogranins A and B represent major soluble components of chromaffin granules, illustrated by two-dimensional proteomics with NH(2)-terminal Edman peptide sequencing and MALDI-TOF MS Stefin B interacts with histones and cathepsin L in the nucleus Catestatin: a multifunctional peptide from chromogranin A Leukocyte telomere length and plasma catestatin and myeloid-related protein 8/14 concentrations in children with obstructive sleep apnea.Reprint of: Chromogranin A: a new proposal for trafficking, processing and induction of granule biogenesis Pyroglutamate-amyloid-β and glutaminyl cyclase are colocalized with amyloid-β in secretory vesicles and undergo activity-dependent, regulated secretion.Peptidomics of the prolyl peptidases Neuropeptidomic components generated by proteomic functions in secretory vesicles for cell-cell communication Proteomics of dense core secretory vesicles reveal distinct protein categories for secretion of neuroeffectors for cell-cell communication.Mass spectrometry-based neuropeptidomics of secretory vesicles from human adrenal medullary pheochromocytoma reveals novel peptide products of prohormone processing Distinct roles for cysteine cathepsin genes in multistage tumorigenesis B-cell lymphopoiesis is regulated by cathepsin L.Unique biological function of cathepsin L in secretory vesicles for biosynthesis of neuropeptides.Direct vasoactive effects of the chromogranin A (CHGA) peptide catestatin in humans in vivo.Processing of human protryptase in mast cells involves cathepsins L, B, and C.Cysteine Cathepsins in the secretory vesicle produce active peptides: Cathepsin L generates peptide neurotransmitters and cathepsin B produces beta-amyloid of Alzheimer's disease Cathepsins: a new culprit behind abdominal aortic aneurysm.Cathepsin L and Arg/Lys aminopeptidase: a distinct prohormone processing pathway for the biosynthesis of peptide neurotransmitters and hormones.Human cathepsin V protease participates in production of enkephalin and NPY neuropeptide neurotransmitters.Cathepsin L targeting in cancer treatment.Neuropeptidomics Mass Spectrometry Reveals Signaling Networks Generated by Distinct Protease Pathways in Human Systems.Unique neuronal functions of cathepsin L and cathepsin B in secretory vesicles: biosynthesis of peptides in neurotransmission and neurodegenerative disease.Adipocytes promote prostate cancer stem cell self-renewal through amplification of the cholecystokinin autocrine loop Cysteine cathepsin non-inhibitory binding partners: modulating intracellular trafficking and function.Major role of cathepsin L for producing the peptide hormones ACTH, beta-endorphin, and alpha-MSH, illustrated by protease gene knockout and expression Proteases for processing proneuropeptides into peptide neurotransmitters and hormones.Cathepsin Protease Controls Copper and Cisplatin Accumulation via Cleavage of the Ctr1 Metal-binding Ectodomain.Activity-based probes as a tool for functional proteomic analysis of proteases.Linear and accurate quantitation of proenkephalin-derived peptides by isotopic labeling with internal standards and mass spectrometry.

P2860

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P2860

Cathepsin L in secretory vesicles functions as a prohormone-processing enzyme for production of the enkephalin peptide neurotransmitter.

http://www.wikidata.org/entity/Q35234967

description

2003 nî lūn-bûn

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2003 թուականի Յուլիսին հրատարակուած գիտական յօդուած

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2003 թվականի հուլիսին հրատարակված գիտական հոդված

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2003年の論文

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2003年論文

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2003年論文

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2003年論文

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2003年论文

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name

Cathepsin L in secretory vesic ...... alin peptide neurotransmitter.

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Cathepsin L in secretory vesic ...... alin peptide neurotransmitter.

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type

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Cathepsin L in secretory vesic ...... alin peptide neurotransmitter.

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Cathepsin L in secretory vesic ...... alin peptide neurotransmitter.

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Cathepsin L in secretory vesic ...... alin peptide neurotransmitter.

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Cathepsin L in secretory vesic ...... alin peptide neurotransmitter.

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Proceedings of the National Academy of Sciences of the United States of America

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Cathepsin L in secretory vesic ...... halin peptide neurotransmitter

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P2093

Anna Logvinova

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Birgit Schilling

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Bradford Gibson

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Christoph Peters

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Doron Greenbaum

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Ivonne Petermann

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Jessica Dehnert

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John M Neveu

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Katalin F Medzihradszky

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Paul Goldsmith

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P2860

Precursor convertases in the secretory pathway, cytosol and extracellular milieu

Processing of proenkephalin-A in bovine chromaffin cells. Identification of natural derived fragments by N-terminal sequencing and matrix-assisted laser desorption ionization-time of flight mass spectrometry.

Epoxide electrophiles as activity-dependent cysteine protease profiling and discovery tools.

Chemical approaches for functionally probing the proteome.

Small molecule affinity fingerprinting. A tool for enzyme family subclassification, target identification, and inhibitor design.

Proteolytic processing in the secretory pathway.

Molecular mechanisms and regulation of opioid receptor signaling.

Dilated cardiomyopathy in mice deficient for the lysosomal cysteine peptidase cathepsin L.

Towards specific functions of lysosomal cysteine peptidases: phenotypes of mice deficient for cathepsin B or cathepsin L.

Differential sorting of lysosomal enzymes out of the regulated secretory pathway in pancreatic beta-cells

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9590-9595

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16

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100

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Thomas Reinheckel

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2003-07-17T00:00:00Z

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10654209

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12869695

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neurotransmitter

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170962

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