S. Harper

发表

Systematic analysis of peptide recoveries from in-gel digestions for protein identifications in proteome studies.

D. Speicher, K. Speicher, O. Kolbas, 2000, Journal of biomolecular techniques : JBT.

Crystal structure and functional interpretation of the erythrocyte spectrin tetramerization domain complex.

A. Mondragón, D. Speicher, R. Marmorstein, 2010, Blood.

Probing structures of large protein complexes using zero-length cross-linking.

D. Speicher, S. Sriswasdi, S. Harper, 2015, Methods.

Cdc13 OB2 dimerization required for productive Stn1 binding and efficient telomere maintenance.

E. Skordalakes, F. Johnson, D. Speicher, 2013, Structure.

Enhanced identification of zero-length chemical cross-links using label-free quantitation and high-resolution fragment ion spectra.

D. Speicher, S. Sriswasdi, Hsin-Yao Tang, 2014, Journal of proteome research.

Structural basis for dimerization in DNA recognition by Gal4.

D. Speicher, R. Marmorstein, M. X. Fitzgerald, 2008, Structure.

Probing erectile function: S-(2-boronoethyl)-L-cysteine binds to arginase as a transition state analogue and enhances smooth muscle relaxation in human penile corpus cavernosum.

D. Speicher, D. Christianson, N. Kim, 2001, Biochemistry.

Purification of proteins fused to glutathione S-transferase.

D. Speicher, S. Harper, 2011, Methods in molecular biology.

Oxidation of Peroxiredoxin 6 in the Presence of GSH Increases its Phospholipase A2 Activity at Cytoplasmic pH

D. Speicher, H. Forman, C. Dodia, 2018, Antioxidants.

Characterizing Recombinant Proteins Using HPLC Gel Filtration and Mass Spectrometry

D. Speicher, G. Begg, S. Harper, 1999, Current protocols in protein science.

PPT1 inhibition enhances the antitumor activity of anti–PD-1 antibody in melanoma

E. Wherry, P. Gimotty, D. Speicher, 2020, JCI insight.

A new chromophoric assay for arginase activity.

D. Speicher, D. Christianson, S. Harper, 1999, Analytical biochemistry.

Detection of Proteins on Blot Membranes

D. Speicher, S. Harper, A. Goldman, 1995, Current protocols in protein science.

Comparing Complex Protein Samples Using Two‐Dimensional Polyacrylamide Gels

S. Harper, David W Speicher, 2019, Current protocols in protein science.

Detection of Proteins on Blot Membranes

D. Speicher, S. Harper, 1995, Current protocols in protein science.

UNIT 10.8 Detection of Proteins on Blot Membranes

D. Speicher, S. Harper, 2001 .

The Physiological Molecular Shape of Spectrin: A Compact Supercoil Resembling a Chinese Finger Trap

Esther Bullitt, Jeffrey W. Brown, Sira Sriswasdi, 2015, PLoS Comput. Biol..

CLIC1 and CLIC4 complement CA125 as a diagnostic biomarker panel for all subtypes of epithelial ovarian cancer

Benjamin G. Bitler, D. Speicher, R. Drapkin, 2018, Scientific Reports.

CLIC1 and CLIC4 complement CA125 as a diagnostic biomarker panel for all subtypes of epithelial ovarian cancer

Benjamin G. Bitler, D. Speicher, R. Drapkin, 2018, Scientific Reports.

Expression and purification of GST fusion proteins.

D. Speicher, S. Harper, 1997, Current protocols in protein science.

Effect of glutathione on the phospholipase A2 activity of peroxiredoxin 6

D. Speicher, C. Dodia, A. Fisher, 2013 .

Structural and functional effects of hereditary hemolytic anemia-associated point mutations in the alpha spectrin tetramer site.

D. Speicher, P. Gallagher, S. Harper, 2008, Blood.

Pathogenic proline mutation in the linker between spectrin repeats: disease caused by spectrin unfolding.

D. Speicher, V. Ortiz, D. Discher, 2007, Blood.

Biochemical Analysis of the Kruppel-associated Box (KRAB) Transcriptional Repression Domain

Sandra L. Harper, David W. Speicher, D. Speicher, 2000, The Journal of Biological Chemistry.

A Comprehensive Model of the Spectrin Divalent Tetramer Binding Region Deduced Using Homology Modeling and Chemical Cross-linking of a Mini-spectrin*

David W Speicher, D. Speicher, Hsin-Yao Tang, 2010, Journal of Biological Chemistry.

CLIC1 and CLIC4 complement CA125 as a diagnostic biomarker panel for all subtypes of epithelial ovarian cancer

D. Speicher, R. Drapkin, Rugang Zhang, 2018, Scientific Reports.

Cdc13 N-Terminal Dimerization, DNA Binding, and Telomere Length Regulation

E. Skordalakes, F. Johnson, D. Speicher, 2010, Molecular and Cellular Biology.

Initiation of Spectrin Dimerization Involves Complementary Electrostatic Interactions between Paired Triple-helical Bundles*

D. Speicher, M. Morris, G. Begg, 2000, The Journal of Biological Chemistry.

Proteome analysis of the triton-insoluble erythrocyte membrane skeleton.

Esther N. Pesciotta, D. Speicher, A. Chakrabarti, 2015, Journal of proteomics.

The exon 46-encoded sequence is essential for stability of human erythroid alpha-spectrin and heterodimer formation.

D. Speicher, J. Delaunay, S. Harper, 1997, Blood.

Pathway shifts and thermal softening in temperature-coupled forced unfolding of spectrin domains.

D. Speicher, D. Discher, R. Law, 2003, Biophysical journal.

Influence of Lateral Association on Forced Unfolding of Antiparallel Spectrin Heterodimers*

Dennis E Discher, David W Speicher, D. Speicher, 2004, Journal of Biological Chemistry.

Role of terminal nonhomologous domains in initiation of human red cell spectrin dimerization.

D. Speicher, G. Begg, S. Harper, 2001, Biochemistry.

The common hereditary elliptocytosis-associated α-spectrin L260P mutation perturbs erythrocyte membranes by stabilizing spectrin in the closed dimer conformation.

D. Speicher, S. Sriswasdi, Hsin-Yao Tang, 2013, Blood.

RED CELLS , IRON , AND ERYTHROPOIESIS The common hereditary elliptocytosis-associated a-spectrin L 260 P mutation perturbs erythrocyte membranes by stabilizing spectrin in the closed dimer conformation

D. Speicher, S. Sriswasdi, Hsin-Yao Tang, 2013 .

Spectrin Tetramer Formation Is Not Required for Viable Development in Drosophila*

D. Speicher, Floyd J Mattie, G. Thomas, 2014, The Journal of Biological Chemistry.

Two‐Dimensional Gel Electrophoresis

D. Speicher, S. Harper, S Harper, 1999, Current protocols in cell biology.

Two‐Dimensional Gel Electrophoresis

D. Speicher, S. Harper, J. Mozdzanowski, 1998, Current protocols in protein science.

The catalytic mechanism of the ESA1 histone acetyltransferase involves a self-acetylated intermediate

D. Speicher, R. Marmorstein, S. Harper, 2002, Nature Structural Biology.

Cooperativity in forced unfolding of tandem spectrin repeats.

Dennis E Discher, David W Speicher, D. Speicher, 2003, Biophysical journal.

The structurally disordered KRAB repression domain is incorporated into a protease resistant core upon binding to KAP-1-RBCC domain.

D. Speicher, K. Borden, R. Marmorstein, 2007, Journal of molecular biology.

Probing large conformational rearrangements in wild-type and mutant spectrin using structural mass spectrometry

D. Speicher, S. Sriswasdi, Hsin-Yao Tang, 2014, Proceedings of the National Academy of Sciences.

Chemistry on a Single Protein, Vascular Cell Adhesion Molecule-1, during Forced Unfolding*

Hui Lu, Dennis E Discher, David W Speicher, 2004, Journal of Biological Chemistry.

disease caused by spectrin unfolding Pathogenic proline mutation in the linker between spectrin repeats

D. Speicher, V. Ortiz, D. Discher, 2009 .

A Fused α-β “Mini-spectrin” Mimics the Intact Erythrocyte Spectrin Head-to-head Tetramer*

D. Speicher, P. Gallagher, S. Harper, 2010, The Journal of Biological Chemistry.

Full-Length Anion Exchanger 1 Structure and Interactions with Ankyrin-1 Determined by Zero Length Crosslinking of Erythrocyte Membranes.

D. Speicher, S. Sriswasdi, S. Harper, 2017, Structure.

Peroxiredoxin 6 homodimerization and heterodimerization with glutathione S-transferase pi are required for its peroxidase but not phospholipase A2 activity.

D. Speicher, C. Dodia, A. Fisher, 2016, Free radical biology & medicine.

Physical properties of a single-motif erythrocyte spectrin peptide: a highly stable independently folding unit.

D. Speicher, L. Otvos, T. DeSilva, 1997, Biochemistry.

Initiation and propagation of spectrin heterodimer assembly involves distinct energetic processes.

D. Speicher, S. Harper, Donghai Li, 2007, Biochemistry.

Lysosomal lipid peroxidation regulates tumor immunity.

D. Speicher, A. Aplin, J. Winkler, 2023, Journal of Clinical Investigation.

Solution structure of the reduced form of human peroxiredoxin-6 elucidated using zero-length chemical cross-linking and homology modelling.

D. Speicher, A. Fisher, S. Sriswasdi, 2015, The Biochemical journal.

Probing large conformational rearrangements in wild-type and mutant spectrin using structural mass spectrometry

D. Speicher, S. Sriswasdi, Hsin-Yao Tang, 2014, Proceedings of the National Academy of Sciences.

The common hereditary elliptocytosis-associated α-spectrin L260P mutation perturbs erythrocyte membranes by stabilizing spectrin in the closed dimer conformation.

D. Speicher, S. Sriswasdi, Hsin-Yao Tang, 2013, Blood.

Peroxiredoxin 6 homodimerization and heterodimerization with glutathione S-transferase pi are required for its peroxidase but not phospholipase A2 activity.

D. Speicher, C. Dodia, A. Fisher, 2016, Free radical biology & medicine.

A Comprehensive Model of the Spectrin Divalent Tetramer Binding Region Deduced Using Homology Modeling and Chemical Cross-linking of a Mini-spectrin*

D. Speicher, Hsin-Yao Tang, P. Gallagher, 2010, The Journal of Biological Chemistry.

Targeting UGCG overcomes resistance to lysosomal autophagy inhibition.

P. Gimotty, M. Herlyn, H. Stark, 2022, Cancer discovery.