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Protein Scienceжурнал

Статьи, опубликованные в журнале

• • 2021 A System of Auxin-inducible Degradation of Human Ku70 Protein to Study Its Role in HIV-1 Replication
  • Sorkin Anton, Shadrina Olga, Kapitonova Maria, Gottikh Marina
  • в журнале Protein Science, издательство Cold Spring Harbor Laboratory Press (United States), том 30, № S1, с. 54-54 DOI
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  • 2021 Differential Fatty Acylation Of Influenza A Virus Hemagglutinin Is Sensitive To Mutations In The Cholesterol Consensus Motive
  • Kordyukova Larisa V., Hu Bodan, Serebryakova Marina V., Veit Michael
  • в журнале Protein Science, издательство Cold Spring Harbor Laboratory Press (United States), том 30, № S1, с. 176-177 DOI
• • 2021 Luciferase-based SARS-CoV-2 Replicon System for Studying Viral Replication and Discontinuous Transcription
  • Galkin Simon, Anisenko Andrey, Shadrina Olga, Gottikh Marina
  • в журнале Protein Science, издательство Cold Spring Harbor Laboratory Press (United States), том 30, № S1, с. 59-60 DOI
• • 2021 Multi point mutagenesis of formate dehydrogenase
  • Galanicheva N., Parshin P., Shaposhnikov L., Atroshenko D., Savin S., Pometun A., Tishkov V.
  • в журнале Protein Science, издательство Cold Spring Harbor Laboratory Press (United States), том 30, № S1, с. 152-152
• • 2021 Phenylacetone monooxygenase: Coenzyme specificity
  • Parshin P.D., Martysuk U.A., Popinako A.V., Savin S.S., Tishkov V.I., Pometun A.A.
  • в журнале Protein Science, издательство Cold Spring Harbor Laboratory Press (United States), том 30, № S1, с. 162-163 DOI
• • 2021 Rational Screening for Inhibitors of the HIV Integrase-Ku70 (XRCC6) Interaction
  • Ilgova Ekaterina, Galkin Simon, Anisenko Andrey, Gottikh Marina
  • в журнале Protein Science, издательство Cold Spring Harbor Laboratory Press (United States), том 30, № S1, с. 58-59
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  • 2021 XL-MS for novel HIV-1 integrase partners detection
  • Anna Rozina, Anisenko Andrey, Galkin Simon, Gottikh Marina
  • в журнале Protein Science, издательство Cold Spring Harbor Laboratory Press (United States), том 30, № S1, с. 59-59
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  • 2019 Human MICAL1: Activation by the small GTPase Rab8 and small-angle X-ray scattering studies on the oligomerization state of MICAL1 and its complex with Rab8
  • Esposito Alessandro, Ventura Valeria, Petoukhov Maxim V., Rai Amrita, Svergun Dmitri I., Vanoni Maria A.
  • в журнале Protein Science, издательство Cold Spring Harbor Laboratory Press (United States), том 28, № 1, с. 150-166 DOI
• • 2019 Phenylacetone monooxygenase: Coenzyme specificity
  • Parshin P.D., Martysuk U.A., Popinako A.V., Savin S.S., Tishkov V.I., Pometun A.A.
  • в журнале Protein Science, издательство Cold Spring Harbor Laboratory Press (United States), том 30, № S1, с. 162-163
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  • 2015 Genetic engineering of new formate dehydrogenases for cofactor regeneration
  • Alekseeva A., Dolina I., Kargov I., Savin S., Tishkov V.
  • в журнале Protein Science, издательство Cold Spring Harbor Laboratory Press (United States), том 24, № S1, с. 174-175 DOI
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  • 2015 Structural characterization of the binding of HIV-1 integrase to its cellular co-factor Ku70
  • Knyazhanskaya Ekaterina, Anisenko Andrey, Gottikh Marina, Zatsepin Timofei
  • в журнале Protein Science, издательство Cold Spring Harbor Laboratory Press (United States), том 24, с. 165-165
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  • 2014 A maximum entropy approach to the study of residue-specific backbone angle distributions in a-synuclein, an intrinsically disordered protein
  • Mantsyzov A.B., Maltsev A.S., Shen Y., Ying J., Hummer G., Bax A.
  • в журнале Protein Science, издательство Cold Spring Harbor Laboratory Press (United States), том 23, с. 1275-1290 DOI
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  • 2014 Highly selective peptide substrates for the assay of cysteine peptidases from the C1 family
  • Elpidina E.N., Filippova I.Yu, Semashko T.A., Vorotnikova E.A., Sharikova V.F., Vinokurov K.S., Fallis L., Oppert B.
  • в журнале Protein Science, издательство Cold Spring Harbor Laboratory Press (United States), том 23, № S1, с. 199-199
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  • 2014 Isolation and characterization of proline specific dipeptidyl peptidase IV from the Tenebrio molitor larval midgut
  • Sharikova V.F., Goptar I.A., Smirnova Y.A., Oppert B., Filippova I.Yu, Elpidina E.N.
  • в журнале Protein Science, издательство Cold Spring Harbor Laboratory Press (United States), том 23, № S1, с. 176-177
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  • 2012 Structure and dynamics in solution of the stop codon decoding N-terminal domain of the human polypeptide chain release factor eRF1
  • Polshakov V.I., Eliseev B.D., Birdsall B., Frolova L.Y.
  • в журнале Protein Science, издательство Cold Spring Harbor Laboratory Press (United States), том 21, № 6, с. 896-903 DOI
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  • 2009 Crystal structures of the X-domains of a Group-1 and a Group-3 coronavirus reveal that ADP-ribose-binding may not be a conserved property
  • Piotrowski Yvonne, Hansen Guido, Linda Boomaars-van der Zanden A., Snijder Eric J., Gorbalenya Alexander E., Hilgenfeld Rolf
  • в журнале Protein Science, издательство Cold Spring Harbor Laboratory Press (United States), том 18, № 1, с. 6-16
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  • 2009 CxxS: Fold-independent redox motif revealed by genome-wide searches for thiol/disulfide oxidoreductase function
  • Fomenko Dmitri E., Gladyshev Vadim N.
  • в журнале Protein Science, издательство Cold Spring Harbor Laboratory Press (United States), том 11, № 10, с. 2285-2296 DOI
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  • 2009 How strong are side chain interactions in the folding intermediate?
  • Samatova E.N., Katina N.S., Balobanov V.A., Melnik B.S., Dolgikh D.A., Bychkova V.E., Finkelstein A.V.
  • в журнале Protein Science, издательство Cold Spring Harbor Laboratory Press (United States), том 18, № 10, с. 2152-2159 DOI
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  • 2009 The solution structure and dynamics of the DH-PH module of PDZRhoGEF in isolation and in complex with nucleotide-free RhoA
  • Cierpicki Tomasz, Bielnicki Jakub, Zheng Meiying, Gruszczyk Jakub, Kasterka Marta, Petoukhov Maxim, Zhang Aming, Fernandez Erik J., Svergun Dmitri I., Derewenda Urszula, Bushweller John H., Derewenda Zygmunt S.
  • в журнале Protein Science, издательство Cold Spring Harbor Laboratory Press (United States), том 18, № 10, с. 2067-2079 DOI
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  • 2008 To be folded or to be unfolded?
  • Garbuzynskiy Sergiy O., Lobanov Michail Yu, Galzitskaya Oxana V.
  • в журнале Protein Science, издательство Cold Spring Harbor Laboratory Press (United States), том 13, № 11, с. 2871-2877 DOI
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  • 2007 Selenoproteinless animals: Selenophosphate synthetase SPS1 functions in a pathway unrelated to selenocysteine biosynthesis
  • Lobanov A.V., Hatfield D.L., Gladyshev V.N.
  • в журнале Protein Science, издательство Cold Spring Harbor Laboratory Press (United States), том 17, № 1, с. 176-182 DOI
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  • 2006 Effective cotranslational folding of firefly luciferase without chaperones of the Hsp70 family
  • Svetlov M.S., Kommer A., Kolb V.A., Spirin A.S.
  • в журнале Protein Science, издательство Cold Spring Harbor Laboratory Press (United States), том 15, № 2, с. 242-247
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  • 2005 Misfolded forms of glyceraldehyde-3-phosphate dehydrogenase interact with GroEL and inhibit chaperonin-assisted folding of the wild-type enzyme
  • Polyakova O.V., Roitel O., Asryants R.A., Poliakov A.A., Branlant G., Muronetz V.I.
  • в журнале Protein Science, издательство Cold Spring Harbor Laboratory Press (United States), том 14, № 4, с. 921-928
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  • 2005 Reversible self-association of ovalbumin at air-water interfaces
  • Kudryashova E.V., Visser A.J.W.G, de Jongh H.H.J
  • в журнале Protein Science, издательство Cold Spring Harbor Laboratory Press (United States), том 14, № 2, с. 483-493 DOI
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  • 2005 Three-state protein folding: Experimental determination of free-energy profile
  • Baryshnikova Ekaterina N., Melnik Bogdan S., Finkelstein Alexei V., Semisotnov Gennady V., Bychkova Valentina E.
  • в журнале Protein Science, издательство Cold Spring Harbor Laboratory Press (United States), том 14, № 10, с. 2658-2667 DOI