S. Borisova

发表

Structure Bases for Nucleotide Recognition by Guanyl-Specific Ribonucleases

A. Vagin, R. Sanishvili, A. Pavlovsky, 1988 .

A Single Point Mutation Reverses the Donor Specificity of Human Blood Group B-synthesizing Galactosyltransferase*

M. Palcic, A. Blancher, R. Polakowski, 2003, The Journal of Biological Chemistry.

Structural Basis for the Inactivity of Human Blood Group O2 Glycosyltransferase*

M. Palcic, A. Blancher, S. V. Evans, 2005, Journal of Biological Chemistry.

Preliminary joint neutron time-of-flight and X-ray crystallographic study of human ABO(H) blood group A glycosyltransferase.

P. Langan, M. Palcic, L. Coates, 2011, Acta crystallographica. Section F, Structural biology and crystallization communications.

Differential Recognition of the Type I and II H Antigen Acceptors by the Human ABO(H) Blood Group A and B Glycosyltransferases*

M. Palcic, S. V. Evans, S. Borisova, 2006, Journal of Biological Chemistry.

Antibody recognition of a unique tumor-specific glycopeptide antigen

Lai-Xi Wang, C. MacKenzie, P. Kufer, 2010, Proceedings of the National Academy of Sciences.

Bacillus thuringiensis CryIA(a) insecticidal toxin: crystal structure and channel formation.

J. Schwartz, M. Cygler, L. Masson, 1995, Journal of molecular biology.

Sequence-dependent effects of cryoprotectants on the active sites of the human ABO(H) blood group A and B glycosyltransferases.

J. Alfaro, S. V. Evans, S. Borisova, 2012, Acta crystallographica. Section D, Biological crystallography.

Antibodies raised against chlamydial lipopolysaccharide antigens reveal convergence in germline gene usage and differential epitope recognition.

C. MacKenzie, C. Brooks, H. Brade, 2010, Biochemistry.

ABO(H) Blood Group A and B Glycosyltransferases Recognize Substrate via Specific Conformational Changes*

M. Palcic, R. Polakowski, T. Lowary, 2008, Journal of Biological Chemistry.

Spectral properties of phosphopyridoxyl-Lys-7(-41)-ribonuclease A.

M. Karpeisky, S. V. Shlyapnikov, S. Borisova, 1975, Biochimica et biophysica acta.

The Structure of calnexin, an ER chaperone involved in quality control of protein folding.

D. Y. Thomas, Y. Li, J. Schrag, 2001, Molecular cell.

Conserved residues Arg188 and Asp302 are critical for active site organization and catalysis in human ABO(H) blood group A and B glycosyltransferases†

M. Palcic, R. Polakowski, Shuangjun Lin, 2018, Glycobiology.

High-resolution crystal structures and STD NMR mapping of human ABO(H) blood group glycosyltransferases in complex with trisaccharide reaction products suggest a molecular basis for product release

M. Palcic, T. Peters, S. V. Evans, 2017, Glycobiology.

The structural basis for specificity in human ABO(H) blood group biosynthesis

Monica M. Palcic, Svetlana N. Borisova, M. Palcic, 2002, Nature Structural Biology.

High Resolution Structures of the Human ABO(H) Blood Group Enzymes in Complex with Donor Analogs Reveal That the Enzymes Utilize Multiple Donor Conformations to Bind Substrates in a Stepwise Manner*

T. Lowary, S. V. Evans, O. Haji-Ghassemi, 2015, The Journal of Biological Chemistry.

The Influence of an Intramolecular Hydrogen Bond in Differential Recognition of Inhibitory Acceptor Analogs by Human ABO(H) Blood Group A and B Glycosyltransferases*

M. Palcic, S. V. Evans, E. Leinala, 2003, Journal of Biological Chemistry.

Glycosyltransfer in mutants of putative catalytic residue Glu303 of the human ABO(H) A and B blood group glycosyltransferases GTA and GTB proceeds through a labile active site

M. Palcic, R. Polakowski, S. V. Evans, 2016, Glycobiology.

Cysteine-to-serine mutants dramatically reorder the active site of human ABO(H) blood group B glycosyltransferase without affecting activity: structural insights into cooperative substrate binding.

M. Palcic, R. Polakowski, M. Persson, 2010, Journal of molecular biology.

Structural Effects of Naturally Occurring Human Blood Group B Galactosyltransferase Mutations Adjacent to the DXD Motif*

M. Palcic, M. Persson, S. V. Evans, 2007, Journal of Biological Chemistry.

Conserved residues Arg188 and Asp302 are critical for active site organization and catalysis in human ABO(H) blood group A and B glycosyltransferases.

M. Palcic, R. Polakowski, Shuangjun Lin, 2018 .

High resolution structures of the human ABO(H) blood group enzymes in complex with donor analogs reveal that the enzymes utilize multiple donor conformations to bind substrates in a stepwise manner.

T. Lowary, S. V. Evans, O. Haji-Ghassemi, 2016, The Journal of Biological Chemistry.

The structure of the complex of ribonuclease s with fluoride analogue of UpA at 2.5 Å resolution

V. Borisov, A. Pavlovsky, M. Karpeisky, 1978, FEBS letters.

Identification and crystallization of a protease-resistant core of calnexin that retains biological activity.

D. Tessier, D. Y. Thomas, J. Schrag, 1998, Journal of structural biology.

pH-induced conformational changes in human ABO(H) blood group glycosyltransferases confirm the importance of electrostatic interactions in the formation of the semi-closed state.

J. Alfaro, S. V. Evans, R. Blackler, 2014, Glycobiology.

Growth Hormones: Expression, Structure and Protein Engineering

M. P. Kirpichnikov, A. Parsadanian, S. Borisova, 1989 .

Antibody recognition of a conformational epitope in a peptide antigen: Fv-peptide complex of an antibody fragment specific for the mutant EGF receptor, EGFRvIII.

A. Klimowicz, S. V. Evans, S. Lavictoire, 2001, Journal of molecular biology.

Three-dimensional structure at 5 A resolution of cytosolic aspartate transaminase from chicken heart.

B. Vainshtein, V. Borisov, G. Kachalova, 1978, Journal of molecular biology.

Electron density map of chicken heart cytosol aspartate transaminase at 3.5 Å resolution

B. Vainshtein, V. Borisov, S. Borisova, 1980, Nature.

The effect of heavy atoms on the conformation of the active-site polypeptide loop in human ABO(H) blood-group glycosyltransferase B.

M. Palcic, M. Persson, S. V. Evans, 2007, Acta crystallographica. Section D, Biological crystallography.

Crystallization and preliminary X-ray diffraction studies of the lepidopteran-specific insecticidal crystal protein CrylA(a).

M. Cygler, P. Grochulski, H. van Faassen, 1994, Journal of molecular biology.