B. Stec

发表

Global distribution of conformational states derived from redundant models in the PDB points to non-uniqueness of the protein structure

A. Godzik, Prasad Burra, Ying Zhang, 2009, Proceedings of the National Academy of Sciences.

Allosteric transition and binding of small molecule effectors causes curvature change in central β-sheets of selected enzymes

Piotr Cieplak, Miguel Argáez, Leticia Velázquez, 2011, Journal of molecular modeling.

Homology modeling of the dopamine D2 receptor and its testing by docking of agonists and tricyclic antagonists.

Mark Froimowitz, Boguslaw Stec, B. Stec, 1994, Journal of medicinal chemistry.

Structural Basis of Neutralization by a Human Anti-severe Acute Respiratory Syndrome Spike Protein Antibody, 80R*

William C. Hwang, Boguslaw Stec, Lukasz Jaroszewski, 2006, Journal of Biological Chemistry.

Structural and functional bases for broad-spectrum neutralization of avian and human influenza A viruses

Boguslaw Stec, W. C. Hwang, R. Liddington, 2009, Nature Structural &Molecular Biology.

MJ0109 is an enzyme that is both an inositol monophosphatase and the 'missing' archaeal fructose-1,6-bisphosphatase

B. Stec, Kenneth A. Johnson, M. Roberts, 2000, Nature Structural Biology.

A revised mechanism for the alkaline phosphatase reaction involving three metal ions.

B. Stec, E. Kantrowitz, K. Holtz, 2000, Journal of molecular biology.

Basis for substrate recognition and distinction by matrix metalloproteinases

Jeffrey W. Smith, A. Godzik, A. Strongin, 2014, Proceedings of the National Academy of Sciences.

Plant thionins – the structural perspective

B. Stec, Boguslaw Stec, 2006, Cellular and Molecular Life Sciences CMLS.

X-ray scattering studies of model lipid membrane interacting with purothionin provide support for a previously proposed mechanism of membrane lysis

B. Stec, J. Majewski, 2010, European Biophysics Journal.

Geometry of Protein Structures. I. Why Hyperbolic Surfaces are a Good Approximation for Beta-Sheets

Vladik Kreinovich, Boguslaw Stec, V. Kreinovich, 2004 .

Comments on the recent crystal structure of TsaBDE complex of bacterial t6A biosynthesis system and its significance for understanding TC-AMP processing

B. Stec, 2019, bioRxiv.

Structural Basis of Membrane Targeting by the Dock180 Family of Rho Family Guanine Exchange Factors (Rho-GEFs)*

R. Liddington, L. Jaroszewski, B. Stec, 2010, The Journal of Biological Chemistry.

AUTOMATED SOLID-PHASE SYNTHESIS, SEPARATION, AND STEREOCHEMISTRY OF PHOSPHOROTHIOATE ANALOGS OF OLIGODEOXYRIBONUCLEOTIDES

W. Stec, G. Zon, B. Stec, 1985 .

Direct structural evidence for a concerted allosteric transition in Escherichia coli aspartate transcarbamoylase

Boguslaw Stec, Evan R. Kantrowitz, C. Macol, 2001, Nature Structural Biology.

Shape Matters : Improving Docking Results by Prior Analysis of Geometric Attributes of Binding Sites

B. Stec, A. Rudnitskaya, Ken Huynh, 2016 .

Refinement of placental alkaline phosphatase complexed with nitrophenyl

B. Stec, J. Millán, A. Cheltsov, 2011 .

Refined structures of placental alkaline phosphatase show a consistent pattern of interactions at the peripheral site.

B. Stec, J. Millán, A. Cheltsov, 2010, Acta crystallographica. Section F, Structural biology and crystallization communications.

Crystallization and Characterization of Galdieria sulphuraria RUBISCO in Two Crystal Forms: Structural Phase Transition Observed in P21 Crystal Form

B. Stec, M. Baranowski, 2007, International Journal of Molecular Sciences.

Structural mechanism of RuBisCO activation by carbamylation of the active site lysine

B. Stec, 2012, Proceedings of the National Academy of Sciences.

Evidence for an active T‐state pig kidney fructose 1,6‐bisphosphatase: Interface residue Lys‐42 is important for allosteric inhibition and AMP cooperativity

B. Stec, E. Kantrowitz, E. Giroux, 1996, Protein science : a publication of the Protein Society.

Isolation and characterization of selective and potent human Fab inhibitors directed to the active-site region of the two-component NS2B-NS3 proteinase of West Nile virus.

A. Strongin, B. Stec, Ilian A Radichev, 2010, The Biochemical journal.

Crystal Structure of a Dual Activity IMPase/FBPase (AF2372) from Archaeoglobus fulgidus

B. Stec, Kenneth A. Johnson, B. Seaton, 2002, The Journal of Biological Chemistry.

Expression, purification and characterization of recombinant crambin.

V. Stojanoff, B. Stec, M. Teeter, 1996, Protein engineering.

Chinese hamster apurinic/apyrimidinic endonuclease (chAPE1) expressed in sf9 cells reveals that its endonuclease activity is regulated by phosphorylation

B. Stec, S. Purohit, P. Arenaz, 2010, The FEBS journal.

Structural Basis of Neutralization By a Human Anti-Sars Spike Protein Antibody, 80r

W. C. Hwang, R. Liddington, L. Jaroszewski, 2007 .

Structure of the inositol-1-phosphate cytidylyltransferase from Thermotoga maritima.

B. Stec, O. Kurnasov, M. Roberts, 2013, Acta crystallographica. Section D, Biological crystallography.

The road less travelled: taming phosphatases.

B. Stec, E. Kantrowitz, T. Widlanski, 1997, Chemistry & biology.

Refinement of purothionins reveals solute particles important for lattice formation and toxicity. Part 2: structure of beta-purothionin at 1.7 A resolution.

B. Stec, M. Teeter, U. Rao, 1995, Acta crystallographica. Section D, Biological crystallography.

Crystal structure of the tetrameric inositol 1‐phosphate phosphatase (TM1415) from the hyperthermophile, Thermotoga maritima

Weizhong Li, B. Stec, M. Roberts, 2007, The FEBS journal.

Not so clear on oxygen. Comment on Structural basis for cofactor-independent dioxygenation in vancomycin biosynthesis by Widboom et al. (2007), Nature (London), 447, 342-345.

B. Stec, K. Stieglitz, 2008, Acta crystallographica. Section D, Biological crystallography.

Alternate modes of binding in two crystal structures of alkaline phosphatase‐inhibitor complexes

B. Stec, E. Kantrowitz, T. Widlanski, 2000, Protein science : a publication of the Protein Society.

Crystal structure of soybean lipoxygenase L-1 at 1.4 A resolution.

Z Otwinowski, J. Bolin, Z. Otwinowski, 1996, Biochemistry.

The Structure of the R184A Mutant of the Inositol Monophosphatase Encoded by suhB and Implications for Its Functional Interactions in Escherichia coli*

D. Court, B. Stec, M. Roberts, 2007, Journal of Biological Chemistry.

Refined structure of yeast apo-enolase at 2.25 A resolution.

L. Lebioda, B. Stec, 1990, Journal of molecular biology.

Mechanism of enolase: the crystal structure of enolase-Mg2(+)-2-phosphoglycerate/phosphoenolpyruvate complex at 2.2-A resolution.

L. Lebioda, B. Stec, 1991, Biochemistry.

Insights into the mechanisms of catalysis and heterotropic regulation of Escherichia coli aspartate transcarbamoylase based upon a structure of the enzyme complexed with the bisubstrate analogue N‐phosphonacetyl‐L‐aspartate at 2.1 Å

W. Lipscomb, B. Stec, E. Kantrowitz, 1999, Proteins.

Mapping of isozymic differences in enolase.

L. Lebioda, B. Stec, 1991, International journal of biological macromolecules.

Crystal structure of enolase indicates that enolase and pyruvate kinase evolved from a common ancestor

Boguslaw Stec, L. Lebioda, B. Stec, 1988, Nature.

Crystal Structure of Holoenzyme Refined at 1.9 Angstroms Resolution: Trigonal-Bipyramidal Geometry of the Cation Binding Site

L. Lebioda, B. Stec, 1989 .

Comparison of two T-state structures of regulatory-chain mutants of Escherichia coli aspartate transcarbamoylase suggests that His20 and Asp19 modulate the response to heterotropic effectors.

B. Stec, E. Kantrowitz, K. Stieglitz, 2007, Acta crystallographica. Section D, Biological crystallography.

Kinetic and X-ray structural studies of three mutant E. coli alkaline phosphatases: insights into the catalytic mechanism without the nucleophile Ser102.

B. Stec, E. Kantrowitz, C. Brennan, 1998, Journal of molecular biology.

Trapping and visualization of a covalent enzyme–phosphate intermediate

Boguslaw Stec, Evan R. Kantrowitz, Lan Ma, 1997, Nature Structural Biology.

Pharmacological inhibition of PHOSPHO1 suppresses vascular smooth muscle cell calcification

B. Stec, J. Millán, N. Cosford, 2013, Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research.

A Model of the Transition State in the Alkaline Phosphatase Reaction*

B. Stec, E. Kantrowitz, K. Holtz, 1999, The Journal of Biological Chemistry.

Genomic identification and in vitro reconstitution of a complete biosynthetic pathway for the osmolyte di-myo-inositol-phosphate

A. Osterman, B. Stec, D. Rodionov, 2007, Proceedings of the National Academy of Sciences.

Proposal for molecular mechanism of thionins deduced from physico-chemical studies of plant toxins.

B. Stec, M. Teeter, V. Brumfeld, 2004, The journal of peptide research : official journal of the American Peptide Society.

Crystal Structure of C5b-6 Suggests Structural Basis for Priming Assembly of the Membrane Attack Complex*

R. Liddington, B. Stec, A. Aleshin, 2012, The Journal of Biological Chemistry.

Structure of Complement C6 Suggests a Mechanism for Initiation and Unidirectional, Sequential Assembly of Membrane Attack Complex (MAC)*♦

R. Liddington, B. Stec, L. Bankston, 2012, The Journal of Biological Chemistry.

Crystal and solution structures of a prokaryotic M16B peptidase: an open and shut case.

Greg L. Hura, Jeffrey W. Smith, A. Strongin, 2009, Structure.

Phospholipid-binding Sites of Phosphatase and Tensin Homolog (PTEN)

B. Stec, A. Redfield, M. Roberts, 2014, The Journal of Biological Chemistry.

The Fas/FADD death domain complex structure unravels signaling by receptor clustering

Boguslaw Stec, Guy S. Salvesen, R. Schwarzenbacher, 2008, Nature.

Vaccinia virus N1L protein resembles a B cell lymphoma‐2 (Bcl‐2) family protein

R. Liddington, John Calvin Reed, B. Stec, 2006, Protein science : a publication of the Protein Society.

Crystallization of alcohol oxidase fromPichia pastoris. Secondary structure predictions indicate a domain with the eightfold β/α-barrel fold

L. Lebioda, B. Stec, E. Marchut, 1990 .

Structures of thermophilic and mesophilic adenylate kinases from the genus Methanococcus.

G. Phillips, E. Bae, B. Stec, 2003, Journal of molecular biology.

Comment on Stereochemical restraints revisited: how accurate are refinement targets and how much should protein structures be allowed to deviate from them? by Jaskolski, Gilski, Dauter & Wlodawer (2007).

Boguslaw Stec, B. Stec, 2007, Acta crystallographica. Section D, Biological crystallography.

Hinge sequences as signaling agents?

B. Stec, 2012, FEBS letters.

Crystal structure of a nonsymbiotic plant hemoglobin.

B. Stec, J. Olson, G. Sarath, 2000, Structure.

Cytotoxic amphiphiles and phosphoinositides bind to two discrete sites on the Akt1 PH domain.

B. Stec, A. Redfield, M. Roberts, 2014, Biochemistry.

The Cation-π Box Is a Specific Phosphatidylcholine Membrane Targeting Motif*

B. Stec, A. Gershenson, R. Goldstein, 2013, The Journal of Biological Chemistry.

Refinement of purothionins reveals solute particles important for lattice formation and toxicity. Part 1: alpha1-purothionin revisited.

B. Stec, M. Teeter, U. Rao, 1995, Acta crystallographica. Section D, Biological crystallography.

Complete Model of Vinculin Suggests the Mechanism of Activation by Helical Super-Bundle Unfurling

B. Stec, Dominik L. Stec, 2022, The Protein Journal.

Conformational communication mediates the reset step in t6A biosynthesis

B. Stec, A. Luthra, M. Swairjo, 2019, Nucleic acids research.

Structure and mechanism of a bacterial t6A biosynthesis system

B. Stec, A. Luthra, M. Swairjo, 2018, Nucleic acids research.

Structure and mechanism of a bacterial t 6 A biosynthesis system

B. Stec, A. Luthra, M. Swairjo, 2018 .

Reaching for mechanistic consensus across life kingdoms: structure and insights into catalysis of the myo-inositol-1-phosphate synthase (mIPS) from Archaeoglobus fulgidus.

B. Stec, M. Roberts, Hongying Yang, 2005, Biochemistry.

Between order and disorder in protein structures: analysis of "dual personality" fragments in proteins.

Adam Godzik, Boguslaw Stec, A. Godzik, 2007, Structure.

Crystal structure of α‐hordothionin at 1.9 Å resolution

B. Stec, S. Suh, M. Teeter, 2005 .

Crystal structure of C-phycocyanin from Cyanidium caldarium provides a new perspective on phycobilisome assembly.

B. Stec, M. Teeter, R. Troxler, 1999, Biophysical journal.

Sampling of the native conformational ensemble of myoglobin via structures in different crystalline environments

Boguslaw Stec, George N Phillips, Wei Zhang, 2007, Proteins.

Mechanism and catalytic strategy of the prokaryotic-specific GTP cyclohydrolase-IB.

B. Stec, A. Luthra, M. Swairjo, 2017, The Biochemical journal.

A single mutation in the regulatory chain of Escherichia coli aspartate transcarbamoylase results in an extreme T-state structure.

B. Stec, E. Kantrowitz, M. K. Williams, 1998, Journal of molecular biology.

Structure of the S. aureus PI-specific phospholipase C reveals modulation of active site access by a titratable π-cation latched loop.

B. Stec, R. Goldstein, M. Roberts, 2012, Biochemistry.

Crystal structure of a trapped catalytic intermediate suggests that forced atomic proximity drives the catalysis of mIPS.

B. Stec, M. Roberts, K. Neelon, 2011, Biophysical journal.

B. Stec, B. Seaton, M. Roberts, 2003, Protein science : a publication of the Protein Society.

Inhibition of enolase: the crystal structures of enolase-Ca2(+)- 2-phosphoglycerate and enolase-Zn2(+)-phosphoglycolate complexes at 2.2-A resolution.

J. Brewer, L. Lebioda, B. Stec, 1992, Biochemistry.

The structure of yeast enolase at 2.25-A resolution. An 8-fold beta + alpha-barrel with a novel beta beta alpha alpha (beta alpha)6 topology.

J. Brewer, L. Lebioda, B. Stec, 1989, The Journal of biological chemistry.

On the nature of a glassy state of matter in a hydrated protein: Relation to protein function

B. Stec, U. Mohanty, M. Teeter, 2001, Proceedings of the National Academy of Sciences of the United States of America.

New crystal structures of HSC-70 ATP binding domain confirm the role of individual binding pockets and suggest a new method of inhibition.

B. Stec, M. Pellecchia, P. Teriete, 2015, Biochimie.

Role of Asn-382 and Thr-383 in Activation and Inactivation of Human Prostaglandin H Synthase Cyclooxygenase Catalysis*

B. Stec, R. Kulmacz, C. Rogge, 2004, Journal of Biological Chemistry.

Competition between Anion Binding and Dimerization Modulates Staphylococcus aureus Phosphatidylinositol-specific Phospholipase C Enzymatic Activity*

B. Stec, A. Gershenson, R. Goldstein, 2012, The Journal of Biological Chemistry.

Review Plant thionins - the structural perspective

B. Stec, N. Torrey, 2006 .

Monitoring the transition from the T to the R state in E.coli aspartate transcarbamoylase by X-ray crystallography: crystal structures of the E50A mutant enzyme in four distinct allosteric states.

B. Stec, D. Baker, E. Kantrowitz, 2004, Journal of molecular biology.

Autocatalytic Activation of the Furin Zymogen Requires Removal of the Emerging Enzyme's N-Terminus from the Active Site

A. Strongin, B. Stec, R. Day, 2009, PloS one.

Crystal structures of the active site mutant (Arg‐243 → Ala) in the T and R allosteric states of pig kidney fructose‐1,6‐bisphosphatase expressed in escherichia coli

B. Stec, E. Kantrowitz, E. Giroux, 1996, Protein science : a publication of the Protein Society.

Structure of human plasminogen kringle 4 at 1.68 a and 277 K. A possible structural role of disordered residues.

B. Stec, M. Whitlow, M. Teeter, 1997, Acta crystallographica. Section D, Biological crystallography.

Mobile loop mutations in an archaeal inositol monophosphatase: Modulating three‐metal ion assisted catalysis and lithium inhibition

Boguslaw Stec, Mary F Roberts, B. Stec, 2010, Protein science : a publication of the Protein Society.

Structure of the wild-type TEM-1 beta-lactamase at 1.55 A and the mutant enzyme Ser70Ala at 2.1 A suggest the mode of noncovalent catalysis for the mutant enzyme.

Boguslaw Stec, Evan R Kantrowitz, B. Stec, 2005, Acta crystallographica. Section D, Biological crystallography.

Itaconic acid, a missing link in macrophage activation, is produced by IRG1

T. Chiles, B. Stec, Jiongjia Cheng, 2013 .

Chinese hamster AP endonuclease operates by a two‐metal ion assisted catalytic mechanism

B. Stec, P. Arenaz, Mandula Borjigin, 2012, FEBS Letters.

1-2018 Structure and Mechanism of a Bacterial t 6 A Biosynthesis System

B. Stec, A. Luthra, M. Swairjo, 2018 .

Model studies of the function of blockers on the small conductance potassium ion channel.

B. Stec, B. Oleksyn, K. Lewiński, 2003, The journal of peptide research : official journal of the American Peptide Society.

The 80s loop of the catalytic chain of Escherichia coli aspartate transcarbamoylase is critical for catalysis and homotropic cooperativity

C. Macol, B. Stec, H. Tsuruta, 1999, Protein science : a publication of the Protein Society.

Design of High-Affinity Metal-Controlled Protein Dimers.

B. Stec, T. Huxford, J. Love, 2019, Biochemistry.

Structure of the inositol-1-phosphate cytidylyltransferase from Thermotoga maritima.

B. Stec, O. Kurnasov, M. Roberts, 2013, Acta Crystallographica Section D: Biological Crystallography.

Probing the Mechanism of the Archaeoglobus fulgidus Inositol-1-phosphate Synthase*

B. Stec, M. Roberts, Yan Wang, 2005, Journal of Biological Chemistry.

Dynamic Interdomain Interactions Contribute to the Inhibition of Matrix Metalloproteinases by Tissue Inhibitors of Metalloproteinases*

A. Strongin, B. Stec, Ilian A Radichev, 2011, The Journal of Biological Chemistry.

Structure of Complement C6 Suggests a Mechanism for Initiation and Unidirectional, Sequential Assembly of Membrane Attack Complex (MAC)*♦

R. Liddington, B. Stec, L. Bankston, 2012, The Journal of Biological Chemistry.

Pharmacological inhibition of PHOSPHO1 suppresses vascular smooth muscle cell calcification

B. Stec, J. Millán, N. Cosford, 2013, Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research.

Living and Nonliving Matter

B. Stec, 2004, Science.

Dynamic interdomain interactions contribute to the inhibition of matrix metalloproteinases (MMPs) by tissue inhibitors of metalloproteinases (TIMPs)

B. Stec, Ilian A Radichev, A. Remacle, 2011 .