W. Swietnicki

发表

The Prion Protein Has RNA Binding and Chaperoning Properties Characteristic of Nucleocapsid Protein NCp7 of HIV-1*

C. Gabus, W. Surewicz, J. Darlix, 2001, The Journal of Biological Chemistry.

The prion protein has DNA strand transfer properties similar to retroviral nucleocapsid protein.

C. Péchoux, C. Gabus, W. Surewicz, 2001, Journal of molecular biology.

Crystal structure of the human prion protein reveals a mechanism for oligomerization

Witold K. Surewicz, W. Surewicz, W. Swietnicki, 2002, Nature Structural Biology.

Analysis of proteinase specificity by studies of peptide substrates. The use of UV and fluorescence spectroscopy to quantitate rates of enzymatic cleavage.

B. Dunn, R. Davenport, W. Swietnicki, 1994, Methods in molecular biology.

Thermodynamic stabilization of the folded domain of prion protein inhibits prion infection in vivo.

J. L. Mills, W. Surewicz, W. Swietnicki, 2013, Cell reports.

KBTBD13 interacts with Cullin 3 to form a functional ubiquitin ligase.

W. Swietnicki, V. Matrosova, S. Techtmann, 2012, Biochemical and biophysical research communications.

In silico analysis of bacteriophage tail tubular proteins suggests a putative sugar binding site and a catalytic mechanism.

E. Brzozowska, W. Swietnicki, 2019, Journal of molecular graphics & modelling.

Design of small molecule inhibitors of type III secretion system ATPase EscN from enteropathogenic Escherichia coli.

W. Swietnicki, K. Nowińska, G. Chodaczek, 2017, Acta biochimica Polonica.

Zinc Binding and Dimerization of Streptococcus pyogenes Pyrogenic Exotoxin C Are Not Essential for T-cell Stimulation*

W. Swietnicki, R. Ulrich, Anne M Barnie, 2003, The Journal of Biological Chemistry.

Folding of Aggregated Proteins to Functionally Active Form

W. Swietnicki, 2006 .

Fv structure of monoclonal antibody II-481 against herpes simplex virus Fc gamma-binding glycoprotein gE contains immunodominant complementarity determining region epitopes that react with human immunoglobulin M rheumatoid factors

R. Williams, B. Dunn, W. Swietnicki, 1994, The Journal of experimental medicine.

Identification of a potent inhibitor of type II secretion system from Pseudomonas aeruginosa.

W. Swietnicki, K. Marycz, A. Czarny, 2019, Biochemical and biophysical research communications.

Identification of Small-Molecule Inhibitors of Yersinia pestis Type III Secretion System YscN ATPase

Michael S. Lee, Daniel O. Carmany, M. A. Olson, 2011, PloS one.

A Yersinia pestis YscN ATPase mutant functions as a live attenuated vaccine against bubonic plague in mice.

W. Swietnicki, J. Bozue, C. Cote, 2012, FEMS microbiology letters.

Dihydrolipoamide Acetyltransferase AceF Influences the Type III Secretion System and Resistance to Oxidative Stresses through RsmY/Z in Pseudomonas aeruginosa

W. Swietnicki, Weihui Wu, Yongxin Jin, 2022, Microorganisms.

Review of Potential Pseudomonas Weaponry, Relevant to the Pseudomonas–Aspergillus Interplay, for the Mycology Community

W. Swietnicki, D. Stevens, Paulami Chatterjee, 2020, Journal of fungi.

Hepatitis A virus 3C proteinase substrate specificity.

D. Jewell, B. Dunn, W. Swietnicki, 1992, Biochemistry.

Yersinia pestis YopD 150-287 fragment is partially unfolded in the native state.

W. Swietnicki, R. Raab, 2008, Protein expression and purification.

Identification of an epitope in the C terminus of normal prion protein whose expression is modulated by binding events in the N terminus.

W. Surewicz, W. Swietnicki, M. Morillas, 2000, Journal of molecular biology.

Secretory System Components as Potential Prophylactic Targets for Bacterial Pathogens

W. Swietnicki, 2021, Biomolecules.

Vitamin D analogs combined with 5-fluorouracil in human HT-29 colon cancer treatment

W. Swietnicki, A. Kutner, J. Wietrzyk, 2014, Oncology reports.

Aggregation and fibrillization of the recombinant human prion protein huPrP90-231.

W. Surewicz, W. Swietnicki, M. Morillas, 2000, Biochemistry.

Solution Structure of the E200K Variant of Human Prion Protein

W. Surewicz, W. Swietnicki, Yongbo Zhang, 2000, The Journal of Biological Chemistry.

Familial Mutations and the Thermodynamic Stability of the Recombinant Human Prion Protein*

W. Surewicz, W. Swietnicki, R. Petersen, 1998, The Journal of Biological Chemistry.

pH-dependent Stability and Conformation of the Recombinant Human Prion Protein PrP(90–231)*

W. Surewicz, W. Swietnicki, R. Petersen, 1997, The Journal of Biological Chemistry.

Folding aggregated proteins into functionally active forms.

W. Swietnicki, 2006, Current opinion in biotechnology.

Prediction of Selected Biosynthetic Pathways for the Lipopolysaccharide Components in Porphyromonas gingivalis

R. Caspi, W. Swietnicki, 2021, Pathogens.

Metallacarborane Derivatives Effective against Pseudomonas aeruginosa and Yersinia enterocolitica

M. Drab, W. Swietnicki, A. Boguszewska-Czubara, 2021, International journal of molecular sciences.

Yersinia pestis Yop secretion protein F: purification, characterization, and protective efficacy against bubonic plague.

W. Swietnicki, B. Powell, Jeremy L. Goodin, 2005, Protein expression and purification.

PrPC has nucleic acid chaperoning properties similar to the nucleocapsid protein of HIV-1.

C. Gabus, J. Darlix, E. Derrington, 2002, Comptes rendus biologies.

Novel Protein-Protein Interactions of the Yersinia pestis Type III Secretion System Elucidated with a Matrix Analysis by Surface Plasmon Resonance and Mass Spectrometry*

David S. Waugh, Robert G. Ulrich, W. Swietnicki, 2004, Journal of Biological Chemistry.

Membrane Environment Alters the Conformational Structure of the Recombinant Human Prion Protein*

W. Surewicz, W. Swietnicki, M. Morillas, 1999, The Journal of Biological Chemistry.

W. Swietnicki, Ralph C. Williams, Hugo Johansson, 1994, The Journal of experimental medicine.

Model systems to study a superantigen-induced disease: Toxic shock syndrome

W. Swietnicki, M. Hale, 2006 .

Design of small molecule inhibitors of type III secretion system ATPase EscN from enteropathogenic Escherichia coli.

W. Swietnicki, K. Nowińska, G. Chodaczek, 2017, Acta biochimica Polonica.