W. K. Schmidt

发表

Protein Isoprenylation in Yeast Targets COOH-Terminal Sequences Not Adhering to the CaaX Consensus

James L. Hougland, Brittany M. Berger, June-hyun Kim, 2018, Genetics.

MALDI-MS Analysis of Peptide Libraries Expands the Scope of Substrates for Farnesyltransferase

James L. Hougland, M. Distefano, E. Hildebrandt, 2021, International journal of molecular sciences.

Yeast as a Tractable Genetic System for Functional Studies of the Insulin-degrading Enzyme*

W. K. Schmidt, Seonil Kim, Andrea N Lapham, 2005, Journal of Biological Chemistry.

A common genetic system for functional studies of pitrilysin and related M16A proteases.

W. K. Schmidt, Benjamin J. Alper, Tatyana E. Nienow, 2006, The Biochemical journal.

Efficient farnesylation of an extended C-terminal C(x)3X sequence motif expands the scope of the prenylated proteome

James L. Hougland, M. Distefano, E. Hildebrandt, 2017, The Journal of Biological Chemistry.

Isoprenylated Protein Peptidase Rce1p

T. M. Dore, W. K. Schmidt, 2013 .

Endoplasmic reticulum membrane localization of Rce1p and Ste24p, yeast proteases involved in carboxyl-terminal CAAX protein processing and amino-terminal a-factor cleavage.

S. Michaelis, W. K. Schmidt, A. Tam, 1998, Proceedings of the National Academy of Sciences of the United States of America.

The Saccharomyces cerevisiae prenylcysteine carboxyl methyltransferase Ste14p is in the endoplasmic reticulum membrane.

S. Michaelis, W. K. Schmidt, J. Romano, 1998, Molecular biology of the cell.

Topology of the yeast Ras converting enzyme as inferred from cysteine accessibility studies.

E. Hildebrandt, W. K. Schmidt, Edward A. Lilla, 2013, Biochemistry.

Proteolytic processing of certain CaaX motifs can occur in the absence of the Rce1p and Ste24p CaaX proteases

W. K. Schmidt, Sarah R. Breevoort, Ranjith K Krishnankutty, 2009, Yeast.

Yeast Ste23p shares functional similarities with mammalian insulin‐degrading enzymes

W. K. Schmidt, Benjamin J. Alper, Jarrad W. Rowse, 2009, Yeast.

Ionic milieu controls the compartment-specific activation of pro-opiomelanocortin processing in AtT-20 cells.

W. K. Schmidt, H. Moore, H. Moore, 1995, Molecular biology of the cell.

Identification, functional expression and enzymic analysis of two distinct CaaX proteases from Caenorhabditis elegans.

I. Varela, C. López-Otín, J. Freije, 2003, The Biochemical journal.

Photoaffinity labeling of Ras converting enzyme using peptide substrates that incorporate benzoylphenylalanine (Bpa) residues: improved labeling and structural implications.

M. Distefano, K. Kyro, W. K. Schmidt, 2011, Bioorganic & medicinal chemistry.

Photoaffinity labeling of Ras converting enzyme 1 (Rce1p) using a benzophenone-containing peptide substrate.

M. Distefano, K. Kyro, W. K. Schmidt, 2010, Bioorganic & medicinal chemistry.

Expression of exogenous proteins in cells with regulated secretory pathways.

Y. T. Chen, L. Carnell, W. K. Schmidt, 1994, Methods in cell biology.

8-Hydroxyquinoline-based inhibitors of the Rce1 protease disrupt Ras membrane localization in human cells.

H. E. Smith, M. Distefano, L. Ashall, 2016, Bioorganic & medicinal chemistry.

Modulation of the inhibitor properties of dipeptidyl (acyloxy)methyl ketones toward the CaaX proteases.

T. M. Dore, W. K. Schmidt, S. B. Porter, 2010, Bioorganic & medicinal chemistry.

Inhibition of the CaaX proteases Rce1p and Ste24p by peptidyl (acyloxy)methyl ketones.

T. M. Dore, W. K. Schmidt, David Z. Mokry, 2007, Biochimica et biophysica acta.

Ste6p mutants defective in exit from the endoplasmic reticulum (ER) reveal aspects of an ER quality control pathway in Saccharomyces cerevisiae.

D. Loayza, S. Michaelis, W. K. Schmidt, 1998, Molecular biology of the cell.

Mutational Analysis of the Ras Converting Enzyme Reveals a Requirement for Glutamate and Histidine Residues*

W. K. Schmidt, S. B. Porter, Victoria A Rogers, 2006, Journal of Biological Chemistry.

AtFACE-2, a functional Prenylated Protein Protease from Arabidopsis thaliana Related to Mammalian Ras-converting Enzymes*

I. Varela, C. López-Otín, A. Díaz‐Perales, 2003, Journal of Biological Chemistry.

Small-Molecule Inhibitors of the Rce1p CaaX Protease

W. K. Schmidt, Surya P. Manandhar, Emily R. Hildebrandt, 2007, Journal of biomolecular screening.

Synthesis and targeting of insulin-like growth factor-I to the hormone storage granules in an endocrine cell line.

W. K. Schmidt, H. Moore, 1994, The Journal of biological chemistry.

Ste24p Mediates Proteolysis of Both Isoprenylated and Non-prenylated Oligopeptides*

M. Wiener, W. K. Schmidt, Buenafe T. Arachea, 2016, The Journal of Biological Chemistry.

A capillary electrophoresis method for evaluation of Aβ proteolysis in vitro

W. K. Schmidt, Benjamin J. Alper, 2009, Journal of Neuroscience Methods.

Rce1: mechanism and inhibition

T. M. Dore, W. K. Schmidt, S. Hampton, 2018, Critical reviews in biochemistry and molecular biology.

Functional classification and validation of yeast prenylation motifs using machine learning and genetic reporters

N. Kannan, Zhongliang Zhou, Wayland Yeung, 2021, bioRxiv.

A shunt pathway limits the CaaX processing of Hsp40 Ydj1p and regulates Ydj1p-dependent phenotypes

L. Wells, Peng Zhao, June-hyun Kim, 2016, eLife.

Chemical inhibition of CaaX protease activity disrupts yeast Ras localization

G. Santangelo, W. Jacobsen, W. K. Schmidt, 2010, Yeast.

Specific Disruption of Ras2 CAAX Proteolysis Alters Its Localization and Function

T. M. Dore, W. K. Schmidt, S. Gore, 2023, Microbiology spectrum.

Anion Activation Site of Insulin-degrading Enzyme*

L. Hersh, D. Rodgers, N. Noinaj, 2011, The Journal of Biological Chemistry.

Evaluating amyloid Beta (aβ) 1-40 degradation by capillary electrophoresis.

W. K. Schmidt, Benjamin J. Alper, 2013, Methods in molecular biology.

121 – Ste24 protease

W. K. Schmidt, 2004 .

The Ras Converting Enzyme (Rce1p)

T. M. Dore, W. K. Schmidt, 2011 .

Cell-Permeable, Small-Molecule Activators of the Insulin-Degrading Enzyme

W. K. Schmidt, Benjamin J. Alper, S. Manandhar, 2012, Journal of biomolecular screening.

Heterologous Expression Studies of Saccharomyces cerevisiae Reveal Two Distinct Trypanosomatid CaaX Protease Activities and Identify Their Potential Targets

G. Santangelo, W. K. Schmidt, David Z. Mokry, 2009, Eukaryotic Cell.

Chapter 10 - The Ras Converting Enzyme (Rce1p): Orthologs, Enzymology, and Inhibitors

T. M. Dore, W. K. Schmidt, 2011 .

A comprehensive in vivo screen of yeast farnesyltransferase activity reveals broad reactivity across a majority of CXXX sequences

N. Kannan, Wayland Yeung, Junehyung Kim, 2023, bioRxiv.

A capillary electrophoresis method for evaluation of Aβ proteolysis in vitro

W. K. Schmidt, Benjamin J. Alper, 2009, Journal of Neuroscience Methods.

Targeted genetic and small molecule disruption of N-Ras CaaX cleavage alters its localization and oncogenic potential.

James L. Hougland, W. K. Schmidt, Emily R. Hildebrandt, 2024, Bioorganic chemistry.