Shin‐Rong Hwang

发表

Resistance of cathepsin L compared to elastase to proteolysis when complexed with the serpin endopin 2C, and recovery of cathepsin L activity.

V. Turk, V. Stoka, Vivian V. H. Hook, 2006, Biochemical and biophysical research communications.

Neuropeptides: Chemical Activity Profiling and Proteomic Approaches

S. Bark, J. Wegrzyn, Shin‐Rong Hwang, 2008 .

Differential accessibilities of dibasic prohormone processing sites of proenkephalin to the aqueous environment revealed by H-D exchange mass spectrometry.

Virgil L. Woods, Sheng Li, Vivian V. H. Hook, 2009, Biochemistry.

Cathepsin L participates in dynorphin production in brain cortex, illustrated by protease gene knockout and expression

C. Peters, Shin‐Rong Hwang, A. Minokadeh, 2010, Molecular and Cellular Neuroscience.

Major Role of Cathepsin L for Producing the Peptide Hormones ACTH, β-Endorphin, and α-MSH, Illustrated by Protease Gene Knockout and Expression*

C. Peters, T. Reinheckel, F. Beuschlein, 2008, Journal of Biological Chemistry.

Endopin Serpin Protease Inhibitors Localize with Neuropeptides in Secretory Vesicles and Neuroendocrine Tissues

Shin‐Rong Hwang, R. Bundey, V. Hook, 2008, Neuroendocrinology.

Novel Chromaffin Granule Serpins, Endopin 1 and Endopin 2

S. Yasothornsrikul, Vivian V. H. Hook, Shin‐Rong Hwang, 2002, Annals of the New York Academy of Sciences.

Novel Secretory Vesicle Serpins, Endopin 1 and Endopin 2: Endogenous Protease Inhibitors with Distinct Target Protease Specificities

Vivian V. H. Hook, Shin‐Rong Hwang, V. Hook, 2002, Biological chemistry.

Molecular Cloning of Endopin 1, a Novel Serpin Localized to Neurosecretory Vesicles of Chromaffin Cells

S. Yasothornsrikul, Shin‐Rong Hwang, C. Sei, 1999, The Journal of Biological Chemistry.

Human pituitary contains dual cathepsin L and prohormone convertase processing pathway components involved in converting POMC into the peptide hormones ACTH, α-MSH, and β-endorphin

Shin‐Rong Hwang, Charles Mosier, Lydiane Funkelstein, 2009, Endocrine.

Cathepsin L participates in the production of neuropeptide Y in secretory vesicles, demonstrated by protease gene knockout and expression

C. Peters, T. Reinheckel, Shin‐Rong Hwang, 2008, Journal of neurochemistry.

The novel bovine serpin endopin 2C demonstrates selective inhibition of the cysteine protease cathepsin L compared to the serine protease elastase, in cross-class inhibition.

V. Turk, V. Stoka, Vivian V. H. Hook, 2005, Biochemistry.

Multiple domains of endopin 2A for serpin cross-class inhibition of papain.

Vivian V. H. Hook, Shin‐Rong Hwang, V. Hook, 2007, Archives of biochemistry and biophysics.

Proteases for processing proneuropeptides into peptide neurotransmitters and hormones.

Jill L. Wegrzyn, S. Bark, J. Wegrzyn, 2008, Annual review of pharmacology and toxicology.

Cathepsin L Expression Is Directed to Secretory Vesicles for Enkephalin Neuropeptide Biosynthesis and Secretion*

Shin‐Rong Hwang, Charles Mosier, V. Hook, 2007, Journal of Biological Chemistry.

α1‐Antichymotrypsin‐Like Proteins I and II Purified from Bovine Adrenal Medulla Are Enriched in Chromaffin Granules and Inhibit the Proenkephalin Processing Enzyme “Prohormone Thiol Protease”

S. Yasothornsrikul, Shin‐Rong Hwang, C. Sei, 1999, Journal of neurochemistry.

Zinc regulation of aminopeptidase B involved in neuropeptide production

Shin‐Rong Hwang, V. Hook, 2008, FEBS Letters.

Secretory vesicle aminopeptidase B related to neuropeptide processing: molecular identification and subcellular localization to enkephalin‐ and NPY‐containing chromaffin granules

T. Foulon, S. Bark, Shin‐Rong Hwang, 2007, Journal of neurochemistry.

Proteases and the emerging role of protease inhibitors in prohormone processing

Shin‐Rong Hwang, N. Tezapsidis, V. Hook, 1994, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

Molecular Studies Define the Primary Structure of α1-Antichymotrypsin (ACT) Protease Inhibitor in Alzheimer’s Disease Brains

M. Palkovits, A. Kohn, Shin‐Rong Hwang, 1999, The Journal of Biological Chemistry.

Arginine and Lysine Aminopeptidase Activities in Chromaffin Granules of Bovine Adrenal Medulla: Relevance to Prohormone Processing

S. Yasothornsrikul, Shin‐Rong Hwang, V. Hook, 1998, Journal of neurochemistry.

Comparison of huntingtin proteolytic fragments in human lymphoblast cell lines and human brain

M. Chesselet, L. Thompson, Shin‐Rong Hwang, 2002, Journal of neurochemistry.

Tissue-Specific Proteolysis of Huntingtin (htt) in Human Brain: Evidence of Enhanced Levels of N- and C-Terminal htt Fragments in Huntington's Disease Striatum

M. Chesselet, Shin‐Rong Hwang, L. Mende-Mueller, 2001, The Journal of Neuroscience.

The novel serpin endopin 2 demonstrates cross-class inhibition of papain and elastase: localization of endopin 2 to regulated secretory vesicles of neuroendocrine chromaffin cells.

Shin‐Rong Hwang, R. Bundey, V. Hook, 2002, Biochemistry.

Cloning and expression of the chloroplast-encoded rbcL and rbcS genes from the marine diatom Cylindrotheca sp. strain N1

Shin‐Rong Hwang, F. Robert Tabita, 1989, Plant Molecular Biology.

Demonstration of GTG as an alternative initiation codon for the serpin endopin 2B-2.

J. Wegrzyn, Shin‐Rong Hwang, V. Hook, 2005, Biochemical and biophysical research communications.

Proteases for processing proneuropeptides into peptide neurotransmitters and hormones.

S. Bark, J. Wegrzyn, Shin‐Rong Hwang, 2008, Annual review of pharmacology and toxicology.