Peer-Reviewed Research Papers (2020-present):

• Comprehensive analysis of CXXX sequence space reveals that S. cerevisiae GGTase-I mainly relies on a2X substrate determinants.
  Sarkar A, Hildebrandt ER, Patel K, Mai E, Shah S, Kim JH, Schmidt WK.
  bioRxiv (2024), https://doi.org/10.1101/2024.03.04.583369
  Under evaluation at a peer-reviewed journal.

• Library screening, in vivo confirmation, and structural and bioinformatic analysis of pentapeptide sequences as substrates for protein farnesyltransferase.
  Schey GL, Hildebrandt ER, Wang Y, Safwan D, Passetti HA, Potts GW, Sprague-Getsy AM, Leoni EA, Kuebler TS, Sham YY, Hougland JL, Beese LS, Schmidt WK, Distefano MD.
  Under evaluation at a peer-reviewed journal.

• A humanized yeast system for evaluating the protein prenylation of a wide range of human and viral CaaX sequences.
  Hildebrandt ER, Sarkar A, Ravishankar R, Kim JH, Schmidt WK.
  bioRxiv (2023), https://doi.org/10.1101/2023.09.19.558494
  Disease Models & Mechanisms (2024), in press.

• Targeted genetic and small molecule disruption of N-Ras CAAX cleavage alters its localization and oncogenic potential.
  Hildebrandt ER, Hussain S, Ravishankar R, Sieburg MA, Asad N, Gore S, Ito T, Hougland JL, Dore TM, Schmidt WK.
  Social Science Research Network (SSRN) - Elsevier (2023), http://dx.doi.org/10.2139/ssrn.4682179
  Bioorganic Chemistry (2024), 147:107316. https://doi.org/10.1016/j.bioorg.2024.107316.

• A comprehensive in vivo screen of yeast farnesyltransferase activity reveals broad reactivity across a majority of CXXX sequences.
  Kim J, Hildebrandt ER, Sarkar A, Wayland Y, Waldon LA, Kannan N, Schmidt WK.
  bioRxiv (2023), https://www.biorxiv.org/content/10.1101/2023.02.06.527295v2.
  Genes, Genomes, Genetics (G3) (2023), 13(7):jkad094.

• Specific disruption of Ras CAAX cleavage alters its localization and function.
  Ravishankar R, Greenway G, Asad N, Gore S, Hildebrandt ER, Dore TM, Ito T, Schmidt WK.
  Microbiology Spectrum (2023), 11(1):e0269222.

• Functional classification and validation of yeast prenylation motifs using machine learning and genetic reporters.
  Berger BM, Wayland Y, Goyal A, Zhou Z, Hildebrandt ER, Kannan N, Schmidt WK.
  PLOS One (2022), 17(6):e0270128.

• MALDI analysis of peptide libraries expands the scope of substrates for farnesyltransferase.
  Schey GL, Hildebrandt ER, Novak SX, Schmidt WK, Hougland JL, Distefano MD.
  International Journal of Molecular Sciences (2021), 22:12042.

• Protein farnesyltransferase catalyzes unanticipated farnesylation and geranylgeranylation of shortened target sequences.
  Ashok S, Hildebrandt ER (co-first author), Samuelson-Ruiz MC, Hardgrove DS, Coreno, DW, Schmidt WK, Hougland JL.
  Biochemistry (2020), 59:1149-62.
  
  

Invited Book Chapters and Reviews (Lifetime)

• RCE1: Mechanism and Inhibition.
  Hampton SE, Dore TM, and Schmidt WK.
  In Critical Reviews in Biochemistry and Molecular Biology (2018); 53:157-174.

• Evaluating amyloid Beta (Aβ) 1-40 degradation by capillary electrophoresis.
  Alper BJ and Schmidt WK.
  In Methods Mol Biol (2013); 984:263-73.

• The yeast M16A proteases: Axl1p and Ste23p.
  Kukday S and Schmidt WK.
  In Handbook of Proteolytic Enzymes (2013).

• Isoprenylated protein peptidase Rce1.
  Dore TM and Schmidt WK.
  In Handbook of Proteolytic Enzymes (2013).

• The Ras Converting Enzyme (Rce1p): Orthologs, Enzymology, and Inhibitors.
  Dore TM and Schmidt WK.
  In The Enzymes (2011), 30B: 231-258.

• The Ste24 protease.
  Schmidt WK and Michaelis S.
  In Handbook of Proteolytic Enzymes (2004), p. 460-465.

• The Axl1p gene product (Saccharomyces cerevisiae).
  Schmidt WK and Michaelis S.
  In Handbook of Proteolytic Enzymes (2004), p. 879-882.

• Expression of exogenous proteins in cells with regulated secretory pathways.
  Chavez RA, Chen YT, Schmidt WK, Carnell L, and Moore HP.
  In Methods Cell Biol. (1994), 43 Pt A:263-88.
  
  

Ph.D. Dissertation (1995)

• Schmidt WK. Sorting and prohormone processing within the regulated secretory pathway of the pituitary-derived AtT-20 cell line. University of California.