J. Bushweller

J. Bushweller, L. Kim, J. Arboleda-Velasquez, 2020, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

KIX domain determines a selective tumor-promoting role for EP300 and its vulnerability in small cell lung cancer

Kwon-Sik Park, Yunpeng Zhou, J. Bushweller, 2022, Science advances.

RUNX1 and RUNX2 transcription factors function in opposing roles to regulate breast cancer stem cells

S. K. Zaidi, G. Stein, J. Lian, 2020, Journal of cellular physiology.

Allosteric inhibition of the protein-protein interaction between the leukemia-associated proteins Runx1 and CBFbeta.

Bruce R Donald, Jolanta Grembecka, Yali Kong, 2007, Chemistry & biology.

The tetramer structure of the Nervy homology two domain, NHR2, is critical for AML1/ETO's activity.

Z. Dauter, J. Gaudet, J. Bushweller, 2006, Cancer cell.

CBFβ-SMMHC Inhibition Triggers Apoptosis by Disrupting MYC Chromatin Dynamics in Acute Myeloid Leukemia

J. Dekker, J. A. Pulikkan, L. Zhu, 2018, Cell.

Accelerated leukemogenesis by truncated CBF beta-SMMHC defective in high-affinity binding with RUNX1.

Takeshi Corpora, J. Bushweller, Yoshiaki Ito, 2010, Cancer cell.

Solution structure of core binding factor β and map of the CBFα binding site

J. Bushweller, N. Speck, Xuemei Huang, 1999, Nature Structural Biology.

Biochemical and Biophysical Properties of the Core-binding Factor α2 (AML1) DNA-binding Domain*

J. Bushweller, N. Speck, B. Crute, 1996, The Journal of Biological Chemistry.

NMR solution structure of the integral membrane enzyme DsbB: functional insights into DsbB-catalyzed disulfide bond formation.

J. Beckwith, T. Cierpicki, Yunpeng Zhou, 2008, Molecular cell.

The intrinsically disordered proteins MLLT3 (AF9) and MLLT1 (ENL) - multimodal transcriptional switches with roles in normal hematopoiesis, MLL fusion leukemia, and kidney cancer.

J. Bushweller, A. Kabra, 2021, Journal of molecular biology.

Leukemia fusion target AF9 is an intrinsically disordered transcriptional regulator that recruits multiple partners via coupled folding and binding.

Charles R. Schmidt, John H. Bushweller, T. Cierpicki, 2013, Structure.

Degree of recruitment of DOT1L to MLL-AF9 defines level of H3K79 Di- and tri-methylation on target genes and transformation potential.

N. Zeleznik-Le, Mazhar Adli, Ritambhara Singh, 2015, Cell reports.

Structure of outer membrane protein A transmembrane domain by NMR spectroscopy

Lukas K. Tamm, John H. Bushweller, J. Bushweller, 2001, Nature Structural Biology.

Binding specificity and mechanistic insight into glutaredoxin-catalyzed protein disulfide reduction.

J. Bushweller, M. Berardi, M J Berardi, 1999, Journal of molecular biology.

The interaction between RUNX2 and core binding factor beta (CBFβ) as a potential therapeutic target in canine osteosarcoma.

J. Bushweller, L. Wittenburg, F. Alegre, 2019, Veterinary and comparative oncology.

Small Molecule Inhibitor of CBFβ-RUNX Binding for RUNX Transcription Factor Driven Cancers

Mazhar Adli, J. A. Pulikkan, K. Janes, 2016, EBioMedicine.

The DCX-domain tandems of doublecortin and doublecortin-like kinase

C. Walsh, J. Otlewski, Z. Dauter, 2003, Nature Structural Biology.

Structure of the AML1-ETO eTAFH domain-HEB peptide complex and its contribution to AML1-ETO activity.

T. Cierpicki, J. Bushweller, N. Speck, 2009, Blood.

Protein Disulfide Exchange by the Intramembrane Enzymes DsbB, DsbD, and CcdA.

J. Bushweller, 2020, Journal of molecular biology.

The NMR solution structure of human glutaredoxin in the fully reduced form.

J. Bushweller, M. Berardi, C. Sun, 1998, Journal of molecular biology.

A mutation in the S-switch region of the Runt domain alters the dynamics of an allosteric network responsible for CBFbeta regulation.

J. Bushweller, N. Speck, Zhe Li, 2006, Journal of molecular biology.

Structure, dynamics and function of the outer membrane protein A (OmpA) and influenza hemagglutinin fusion domain in detergent micelles by solution NMR

J. Bushweller, F. Abildgaard, L. Tamm, 2003, FEBS letters.

The binding of the PDZ tandem of syntenin to target proteins.

Jolanta Grembecka, Zygmunt S Derewenda, T. Cierpicki, 2006, Biochemistry.

Probing the supramodular architecture of a multidomain protein: the structure of syntenin in solution.

T. Cierpicki, J. Bushweller, Z. Derewenda, 2005, Structure.

The NOESY jigsaw: automated protein secondary structure and main-chain assignment from sparse, unassigned NMR data

Chris Bailey-Kellogg, Bruce Randall Donald, Alik Widge, 2000, RECOMB '00.

BCOR Binding to MLL-AF9 Is Essential for Leukemia via Altered EYA1, SIX, and MYC Activity.

N. Zeleznik-Le, Shubin Zhang, J. Bushweller, 2020, Blood cancer discovery.

Sequence-specific 1H n.m.r. assignments and determination of the three-dimensional structure of reduced Escherichia coli glutaredoxin.

M. Billeter, K. Wüthrich, A. Holmgren, 1991, Journal of molecular biology.

The DC‐module of doublecortin: Dynamics, domain boundaries, and functional implications

T. Cierpicki, J. Bushweller, Z. Derewenda, 2006, Proteins.

MAPK/ERK2 phosphorylates ERG at serine 283 in leukemic cells and promotes stem cell signatures and cell proliferation

D. Beck, J. Wong, Yizhou Huang, 2016, Leukemia.

Solution Structure and Elevator Mechanism of the Membrane Electron Transporter CcdA

Yunpeng Zhou, J. Bushweller, 2018, Nature Structural & Molecular Biology.

Tom1 Modulates Binding of Tollip to Phosphatidylinositol 3-Phosphate via a Coupled Folding and Binding Mechanism.

Kristen I. Fread, J. Bushweller, J. Ellena, 2015, Structure.

Structural and dynamic studies of the transcription factor ERG reveal DNA binding is allosterically autoinhibited

John H. Bushweller, Edward E. Pryor, David S. Cafiso, 2013, Proceedings of the National Academy of Sciences.

The nuclear magnetic resonance solution structure of the mixed disulfide between Escherichia coli glutaredoxin(C14S) and glutathione.

M. Billeter, K. Wüthrich, A. Holmgren, 1994, Journal of molecular biology.

Biophysical characterization of interactions between the core binding factor alpha and beta subunits and DNA.

J. Kelley, J. Bushweller, N. Speck, 2000, FEBS letters.

Solution structure of core binding factor beta and map of the CBF alpha binding site.

J. Bushweller, N. Speck, J. Peng, 1999, Nature structural biology.

On the mechanism of autoinhibition of the RhoA-specific nucleotide exchange factor PDZRhoGEF

T. Cierpicki, J. Bushweller, Z. Derewenda, 2009, BMC Structural Biology.

Biochemical and biophysical properties of the core-binding factor alpha2 (AML1) DNA-binding domain.

J. Bushweller, N. Speck, B. Crute, 1996, Journal of Biological Chemistry.

Complete 1H, 13C, and 15N NMR resonance assignments and secondary structure of human glutaredoxin in the fully reduced form

Chaohong Sun, A. Holmgren, J. Bushweller, 1997, Protein science : a publication of the Protein Society.

Biosynthetic 15N and 13C isotope labelling of glutathione in the mixed disulfide with Escherichia coli glutaredoxin documented by sequence-specific NMR assignments.

K. Wüthrich, A. Holmgren, J. Bushweller, 1993, European journal of biochemistry.

Gene regulatory network analysis predicts cooperating transcription factor regulons required for FLT3-ITD+ AML growth

Salam A. Assi, C. Bonifer, P. Cockerill, 2023, bioRxiv.

Small molecule inhibition of the CBFβ/RUNX interaction decreases ovarian cancer growth and migration through alterations in genes related to epithelial-to-mesenchymal transition.

C. Landen, J. Bushweller, D. Wotton, 2018, Gynecologic oncology.

Comparison of backbone dynamics of reduced and oxidized Escherichia coli glutaredoxin-1 using 15N NMR relaxation measurements.

J. Kelley, J. Bushweller, T. Laue, 1997, Biochemistry.

The solution structure and dynamics of the DH‐PH module of PDZRhoGEF in isolation and in complex with nucleotide‐free RhoA

D. Svergun, T. Cierpicki, J. Bushweller, 2009, Protein science : a publication of the Protein Society.

An erythroid to myeloid cell fate conversion is elicited by LSD1 inactivation.

J. D. Engel, M. Rosenfeld, J. Bushweller, 2021, Blood.

Application of fragment-based drug discovery to membrane proteins: identification of ligands of the integral membrane enzyme DsbB.

G. Siegal, S. Sligar, Yunpeng Zhou, 2010, Chemistry & biology.

The NOESY Jigsaw: Automated Protein Secondary Structure and The NOESY Jigsaw: Automated Protein Secondary Structure and Main-Chain Assignment from Sparse, Unassigned NMR Data Main-Chain Assignment from Sparse, Unassigned NMR Data

B. Donald, C. Bailey-Kellogg, A. Widge, 2023 .

Biochemical and Biophysical Properties of the Core-binding Factor a2 (AML1) DNA-binding Domain*

J. Bushweller, N. Speck, B. Crute, 1996 .

Overexpression, Purification, and Biophysical Characterization of the Heterodimerization Domain of the Core-binding Factor β Subunit*

J. Kelley, Chaohong Sun, J. Bushweller, 1998, The Journal of Biological Chemistry.

Increasing the accuracy of solution NMR structures of membrane proteins by application of residual dipolar couplings. High-resolution structure of outer membrane protein A.

T. Cierpicki, J. Bushweller, L. Tamm, 2006, Journal of the American Chemical Society.

Complete 'H, 13C, and 15N NMR and secondary structure of human in the fully reduced form resonance assignments glutaredoxin rn

Chaohong Sun, J. Bushweller, '. JOHNH.BUSHWELLER, 2002 .

Targeting RUNX1 Prevents Pulmonary Fibrosis and Reduces Expression of Severe Acute Respiratory Syndrome Coronavirus 2 Host Mediators

J. Bushweller, M. Glatzel, S. Krasemann, 2021 .

CBFbeta is critical for AML1-ETO and TEL-AML1 activity.

L. Roudaia, J. Bushweller, N. Speck, 2009, Blood.

CBF (cid:1) is critical for AML1-ETO and TEL-AML1 activity

L. Roudaia, J. Bushweller, N. Speck, 2009 .

CBF (cid:1) is critical for AML1-ETO and TEL-AML1 activity

L. Roudaia, J. Bushweller, N. Speck, 2009 .

CBF (cid:1) is critical for AML1-ETO and TEL-AML1 activity

L. Roudaia, J. Bushweller, N. Speck, 2009 .

CBF (cid:1) is critical for AML1-ETO and TEL-AML1 activity

L. Roudaia, J. Bushweller, N. Speck, 2009 .

CBF (cid:1) is critical for AML1-ETO and TEL-AML1 activity

L. Roudaia, J. Bushweller, N. Speck, 2009 .

CBF (cid:1) is critical for AML1-ETO and TEL-AML1 activity

L. Roudaia, J. Bushweller, N. Speck, 2009 .

CBF (cid:1) is critical for AML1-ETO and TEL-AML1 activity

L. Roudaia, J. Bushweller, N. Speck, 2009 .

CBF (cid:1) is critical for AML1-ETO and TEL-AML1 activity

L. Roudaia, J. Bushweller, N. Speck, 2009 .

CBF (cid:1) is critical for AML1-ETO and TEL-AML1 activity

L. Roudaia, J. Bushweller, N. Speck, 2009 .

CBF (cid:1) is critical for AML1-ETO and TEL-AML1 activity

L. Roudaia, J. Bushweller, N. Speck, 2009 .

Leukemia fusion target AF9 is an intrinsically disordered transcriptional regulator that recruits multiple partners via coupled folding and binding.

T. Cierpicki, J. Bushweller, Stephanie A. Johnson, 2013, Structure.

The NOESY jigsaw: automated protein secondary structure and main-chain assignment from sparse, unassigned NMR data

C. Bailey-Kellogg, A. Widge, J. Bushweller, 2000, RECOMB '00.

The solution structure and dynamics of the DH‐PH module of PDZRhoGEF in isolation and in complex with nucleotide‐free RhoA

D. Svergun, T. Cierpicki, J. Bushweller, 2009, Protein science : a publication of the Protein Society.