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Valery Kh. Akparov

Observed names: V Akparov, V Kh Akparov, V. K. Akparov, V. Kh. Akparov, V.K. Akparov, V.Kh Akparov, VALERY K. AKPAROV, Valerii Kh. Akparov, Valerij Akparov, Valery Akparov
ORCID: 0000-0002-5821-5632
Observed ORCID: 0000-0002-5821-5632
OpenAlex ID: A5015021049
Identification of a novel endogenous memory facilitating cyclic dipeptide cyclo‐prolylglycine in rat brain
1996 · T.A Gudasheva, S.S Boyko, et al. · FEBS Letters · 87
Phenylboronic acid as a ligand for biospecific chromatography of serine proteinases
1978 · Valerii Kh. Akparov, Valentin M. Stepanov · Journal of Chromatography A · 57
Crystal growth of phosphopantetheine adenylyltransferase, carboxypeptidase t, and thymidine phosphorylase on the international space station by the capillary counter-diffusion method
2011 · I. P. Kuranova, E. A. Smirnova, et al. · Crystallography Reports · 41
The major metabolite of dipeptide piracetam analogue GVS-111 in rat brain and its similarity to endogenous neuropeptide cyclo-l-prolylglycine
1997 · T. A. Gudasheva, S. S. Boyko, et al. · European Journal of Drug Metabolism and Pharmacokinetics · 29
Structural insights into the broad substrate specificity of carboxypeptidase T from Thermoactinomyces vulgaris
2015 · Valery Kh. Akparov, Vladimir I. Timofeev, et al. · FEBS Journal · 19
Structural principles of the wide substrate specificity of Thermoactinomyces vulgaris carboxypeptidase T. reconstruction of the carboxypeptidase B primary specificity pocket
2007 · V. Kh. Akparov, A. M. Grishin, et al. · Biochemistry (Moscow) · 16
Amino acid sequence pattern in the regulatory peptides
1991 · GEORGY Y BAKALKIN, ALEXANDRA B. RAKHMANINOVA, et al. · International journal of peptide & protein research · 16
Structural principles of the broad substrate specificity of Thermoactinomyces vulgaris carboxypeptidase T--role of amino acid residues at positions 260 and 262
2008 · A.M. Grishin, V.K. Akparov, et al. · Protein Engineering Design and Selection · 13
Structure of the carboxypeptidase B complex with N-sulfamoyl-L-phenylalanine – a transition state analog of non-specific substrate
2017 · Valery Akparov, Vladimir Timofeev, et al. · Journal of Biomolecular Structure and Dynamics · 12
Leu254 residue and calcium ions as new structural determinants of carboxypeptidase T substrate specificity
2008 · A. M. Grishin, V. Kh. Akparov, et al. · Biochemistry (Moscow) · 12
The nature of the ligand’s side chain interacting with the S1'-subsite of metallocarboxypeptidase T (from Thermoactinomyces vulgaris) determines the geometry of the tetrahedral transition complex
2019 · Valery Kh. Akparov, Vladimir I. Timofeev, et al. · PLoS ONE · 10
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Structure of the complex of carboxypeptidase B and N-sulfamoyl- L -arginine
2015 · Valery Akparov, Nikolay Sokolenko, et al. · Acta Crystallographica Section F Structural Biology Communications · 10
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Three-dimensional structure of recombinant carboxypeptidase T from Thermoactinomyces vulgaris without calcium ions
2011 · V. Kh. Akparov, V. I. Timofeev, et al. · Crystallography Reports · 10
Ipsilateral Responses Induced by Factors Present in left and right Hemispheres
1989 · Georgy Ya. Bakalkin, Arkady S. Pivovarov, et al. · International Journal of Neuroscience · 10
Dipeptide mimetic of BDNF ameliorates motor dysfunction and striatal apoptosis in 6-OHDA-induced Parkinson’s rat model: Considering Akt and MAPKs signaling
2023 · Bita Firouzan, Farideh Iravanpour, et al. · Behavioural Brain Research · 9
Three-dimensional structure of carboxypeptidase T from Thermoactinomyces vulgaris in complex with N-BOC-L-leucine
2013 · V. I. Timofeev, S. A. Kuznetsov, et al. · Biochemistry (Moscow) · 9
Crystal structures of carboxypeptidase T complexes with transition-state analogs
2017 · Valery Kh. Akparov, Vladimir I. Timofeev, et al. · Journal of Biomolecular Structure and Dynamics · 8
Preparation, crystallization, and preliminary X-ray diffraction study of mutant carboxypeptidase T containing the primary specificity pocket of carboxypeptidase B
2010 · V. Kh. Akparov, A. M. Grishin, et al. · Crystallography Reports · 8
Crystal structure of mutant carboxypeptidase T from Thermoactinomyces vulgaris with an implanted S1′ subsite from pancreatic carboxypeptidase B
2018 · Valery Kh. Akparov, Vladimir I. Timofeev, et al. · Acta Crystallographica Section F Structural Biology Communications · 6
[Subtilisin 72: a serine protease from Bac. subtilis strain 72 - an enzyme similar to subtilisin Carlsberg].
1979 · V Kh Akparov, L P Belianova, et al. · PubMed · 5
Structure of the microbial carboxypeptidase T complexed with the transition state analog N-sulfamoyl-l-lysine
2020 · Valery Kh. Akparov, Galina E. Konstantinova, et al. · Biophysical Chemistry · 4
Mobile Loop in the Active Site of Metallocarboxypeptidases as an Underestimated Determinant of Substrate Specificity
2018 · V. Kh. Akparov, V. I. Timofeev, et al. · Biochemistry (Moscow) · 4
Three-dimensional structure of porcine pancreatic carboxypeptidase B with an acetate ion and two zinc atoms in the active site
2017 · V. Kh. Akparov, V. I. Timofeev, et al. · Crystallography Reports · 4
Preparation, Crystallization, and Preliminary X-Ray Diffraction Study of Mutant Carboxypeptidase T Bearing the Primary Specificity Pocket and the Active-Site Loop of Carboxypeptidase B
2020 · V. Kh. Akparov, G. E. Konstantinova, et al. · Crystallography Reports · 3
[Characterization of S1' subsite specificity of Thermoactinomyces vulgaris carboxypeptidase T by site-directed mutagenesis].
2002 · L A Trachuk, A M Bushueva, et al. · PubMed · 3
Works count: 56
Citation count: 416
H-index: 10
I10-index: 14
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