S. Martsev

发表

Partially structured state of the functional VH domain of the mouse anti‐ferritin antibody F11

Y. Tsybovsky, A. Chumanevich, A. Dubnovitsky, 2002, FEBS letters.

Fusion of barnase to antiferritin antibody F11 VH domain results in a partially folded functionally active protein

Y. Tsybovsky, O. Stremovskiy, S. Deyev, 2009, Biochemistry (Moscow).

Antiferritin single‐chain antibody: a functional protein with incomplete folding?

A. Chumanevich, A. Dubnovitsky, S. Deyev, 1998, FEBS letters.

Antiferritin single-chain Fv fragment is a functional protein with properties of a partially structured state: comparison with the completely folded V(L) domain.

Y. Tsybovsky, A. Chumanevich, A. Dubnovitsky, 2000, Biochemistry.

Amyloid fibril formation of the mouse V(L) domain at acidic pH.

A. Dubnovitsky, M. Hoshino, K. Hasegawa, 2002, Biochemistry.

Folding and Stability of Chimeric Immunofusion VL-Barstar

Y. Tsybovsky, O. Stremovskiy, S. Deyev, 2004, Biochemistry (Moscow).

Independent folding and conformational changes of the barnase module in the VL‐barnase immunofusion: calorimetric evidence

Y. Tsybovsky, S. Martsev, A. A. Kedrov, 2004, FEBS letters.

Local Conformational Changes in Ferritins with Variable Iron Content

S. Martsev, Z. Kravchuk, M. Yakutovich, 2002, Biochemistry (Moscow).

Truncated aspartate aminotransferase from alkalophilic Bacillus circulans with deletion of N-terminal 32 amino acids is a non-functional monomer in a partially structured state.

Y. Tsybovsky, A. Chumanevich, T. Korpela, 2001, Protein engineering.

Folding of an antibody variable domain in two functional conformations in vitro: calorimetric and spectroscopic study of the anti-ferritin antibody VL domain.

Y. Tsybovsky, S. Martsev, Z. Kravchuk, 2007, Protein engineering, design & selection : PEDS.

Distinct stability of recombinant L and H subunits of human ferritin: calorimetric and ANS binding studies.

P. Arosio, S. Martsev, A. Vlasov, 1998, Protein engineering.

Antiferritin VL homodimer binds human spleen ferritin with high specificity.

Jukka V. Lehtonen, T. Salminen, A. Chumanevich, 2002, Journal of structural biology.

Thermodynamic Stability and Functional Activity of Tumor-Associated Antibodies

L. D. Kozmin, O. P. Bliznukov, Y. Tsybovsky, 2004, Biochemistry (Moscow).

Two high-affinity monoclonal IgG2a antibodies with differing thermodynamic stability demonstrate distinct antigen-induced changes in protein A-binding affinity.

A. Chumanevich, S. Martsev, Z. Kravchuk, 1998, Journal of immunological methods.

Thermodynamic stability of immunoglobulins and allosteric interactions with ferritin and protein A: distinct properties of the two antibodies of IgG2a subclass.

A. Chumanevich, S. Martsev, Z. Kravchuk, 1998, Biochemistry. Biokhimiia.

Thermodynamic and functional characterization of a stable IgG conformer obtained by renaturation from a partially structured low pH‐induced state

S. Martsev, Z. Kravchuk, A. Vlasov, 1995, FEBS letters.

Modification of monoclonal and polyclonal IgG with palladium (II) coproporphyrin I: stimulatory and inhibitory functional effects induced by two different methods.

A. Savitsky, S. Martsev, Z. Kravchuk, 1995, Journal of immunological methods.

Fusion of the antiferritin antibody VL domain to barnase results in enhanced solubility and altered pH stability.

S. G. Odintsov, Y. Tsybovsky, O. Stremovskiy, 2004, Protein engineering, design & selection : PEDS.

Large increase in thermal stability of the CH2 domain of rabbit IgG after acid treatment as evidenced by differential scanning calorimetry.

S. Martsev, Z. Kravchuk, A. Vlasov, 1994, Immunology letters.