about
Molecular basis of RNA recognition and TAP binding by the SR proteins SRp20 and 9G8Graphene in therapeutics delivery: Problems, solutions and future opportunitiesParG, a protein required for active partition of bacterial plasmids, has a dimeric ribbon-helix-helix structureSpecificity and Autoregulation of Notch Binding by Tandem WW Domains in Suppressor of DeltexStructural Basis for the Recognition of Cellular mRNA Export Factor REF by Herpes Viral Proteins HSV-1 ICP27 and HVS ORF57Competitive and Cooperative Interactions Mediate RNA Transfer from Herpesvirus Saimiri ORF57 to the Mammalian Export Adaptor ALYREFMapping the binding site for the GTP-binding protein Rac-1 on its inhibitor RhoGDI-1Mutually exclusive interactions drive handover of mRNA from export adaptors to TAPIncreasing the sensitivity of cryoprobe protein NMR experiments by using the sole low-conductivity arginine glutamate salt.Fingerprinting food: current technologies for the detection of food adulteration and contamination.The structure of the folded domain from the signature multifunctional protein ICP27 from herpes simplex virus-1 reveals an intertwined dimer.The herpes viral transcription factor ICP4 forms a novel DNA recognition complex.The effects of arginine glutamate, a promising excipient for protein formulation, on cell viability: Comparisons with NaClCharacterizing monoclonal antibody formulations in arginine glutamate solutions using (1)H NMR spectroscopy.Dynamic studies of H-Ras•GTPγS interactions with nucleotide exchange factor Sos reveal a transient ternary complex formation in solution.Monitoring Ras Interactions with the Nucleotide Exchange Factor Son of Sevenless (Sos) Using Site-specific NMR Reporter Signals and Intrinsic Fluorescence.The effect of arginine glutamate on the stability of monoclonal antibodies in solution.A simple method for improving protein solubility and long-term stability.The structural basis of the TIM10 chaperone assembly.¹H, ¹³C and ¹⁵N resonance assignment for the human K-Ras at physiological pH.Simultaneous measurement of residual dipolar couplings for proteins in complex using the isotopically discriminated NMR approach.Investigating Liquid-Liquid Phase Separation of a Monoclonal Antibody Using Solution-State NMR Spectroscopy: Effect of Arg·Glu and Arg·HCl.Stabilization of proteins by enhancement of inter-residue hydrophobic contacts: lessons of T4 lysozyme and barnase.A new method to characterize hydrophobic organization of proteins: application to rational protein engineering of barnase.Assignment of 1H, 13C, and 15N resonances for the PilP pilot protein from Neisseria meningitidis.The unstructured N-terminal tail of ParG modulates assembly of a quaternary nucleoprotein complex in transcription repression.Overlapping motifs on the herpes viral proteins ICP27 and ORF57 mediate interactions with the mRNA export adaptors ALYREF and UIFDistinct Domains of Small Tims Involved in Subunit Interaction and Substrate RecognitionDetection of the adulteration of fresh coconut water via NMR spectroscopy and chemometricsF Dark-State Exchange Saturation Transfer NMR Reveals Reversible Formation of Protein-Specific Large Clusters in High-Concentration Protein MixturesThe solution structure of a domain from the Neisseria meningitidis lipoprotein PilP reveals a new beta-sandwich foldThe divalent cation-binding sites of gramicidin A transmembrane ion-channelAmino acid residue: is it structural or functional?Isotopically discriminated NMR spectroscopy: a tool for investigating complex protein interactions in vitroQuantification of casein phosphorylation with conformational interpretation using Raman spectroscopyAssignment of 1H, 13C, and 15N resonances for the REF2-I mRNA export factor19F NMR as a Tool for Monitoring Individual Differentially Labeled Proteins in Complex MixturesMolecular Mechanism of SR Protein Kinase 1 Inhibition by the Herpes Virus Protein ICP27New Disulphide Bond in Cystatin-Based Protein Scaffold Prevents Domain-Swap-Mediated Oligomerization and Stabilizes the Functionally Active FormArginine to Lysine Mutations Increase the Aggregation Stability of a Single-Chain Variable Fragment through Unfolded-State Interactions
P50
Q24306711-74146177-D26F-4AF9-9014-66A0C60E8FB3Q26750485-0D2A923B-DB42-418E-AC50-2C0E1216FE61Q27642550-33DBA1C9-AAB2-43B1-9A0F-FBE707F11EA2Q27646888-D4807572-5B91-4BF3-B626-C45E86DD27A5Q27666677-A426A2CB-CD52-45C1-9D2E-70F667C9AACDQ27681835-9268DEA6-DE85-485C-AE54-D17323843F63Q28144724-008DC25A-C374-4F09-B6E1-F4F28F9B49E0Q28512678-96A0B8DA-CDEF-4618-B315-C31147C16BADQ31143284-E4A0F2EF-4836-4FAC-A8F3-08BB5773B46BQ34315897-DA008BC4-F809-4C1D-96F1-4A08DAF5745EQ36293751-8838AD5F-9BD9-492A-9DEB-0C781342912BQ38785758-93642C78-6A71-4ACC-9E9E-AAEBD05ECD2FQ38794404-0B9B2397-8E54-40C0-866E-3E5460AF92DCQ39428136-364FC470-BF13-46D4-A31A-73C2CFABE121Q39604170-E14E4F9A-892C-4BB7-A55D-7E0C28F78B86Q40325189-838E68D6-956A-4DA8-A1A1-FA8CA577A7CFQ42875108-DA9A9C54-2482-4553-833B-C361273CF139Q44986296-5455E245-88E7-4BA8-A7E1-5BE6DF4C468AQ47197538-C71379E2-44D6-492F-9A54-C788499011A3Q47272364-077F79A5-1E34-40B4-B449-B82AD4C32522Q47682573-5A1AF4D7-BD8C-4D3E-8E69-3E026ADFC155Q48277457-64BE6B26-7BDF-484C-9BCF-E4FEBC341E70Q52069292-03C05B90-7AE3-4697-B7A4-77CD7B9700E9Q52246959-DE5507D0-282C-4138-B530-0E6FC5C91F5CQ53791107-96CA564C-C23C-43BF-A190-9DB8E3B105CFQ54484534-F5D9FCED-8062-476B-AE22-D36E615B9DCEQ57292453-533CDAAC-622A-4D20-ACC8-E3C1E02D9FDAQ57832381-E66D605B-B3D1-4EF7-9EDC-B77C7657D0BBQ62648800-C8F830BD-7A1F-4838-A7E7-6B5CA0884D34Q64103736-7EFDC5A0-1DE6-476F-BB58-38BD0C4DED89Q64449291-23F56BBE-A38C-46CC-AC20-4C69FE89CA5FQ67696113-D4EEB052-96F2-47AC-9B03-DDA9CED1F3A4Q71583909-2BB7CEC4-FA8F-4046-B62F-1160BAD94CEDQ80216429-DFA75066-8BF7-443E-9870-9C06D6648098Q81348737-C514D0FC-28F2-40BC-850E-AFD320B4DC1CQ83888508-7BDC55EB-86F2-4C57-A779-5E296447F94EQ88973275-52DDEF17-FB3E-46F9-8437-0D79BEC1488EQ90883562-2EBCA593-3BE4-4A3B-9CCF-49C1BEC4DD56Q91263410-78011C12-346A-4F07-AAE5-360B96BC0913Q91956175-437ACCCB-B97C-482B-BCE0-DA1A07EFC880
P50
description
hulumtues
@sq
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Alexander P Golovanov
@ast
Alexander P Golovanov
@en
Alexander P Golovanov
@es
Alexander P Golovanov
@nl
Alexander P Golovanov
@sl
type
label
Alexander P Golovanov
@ast
Alexander P Golovanov
@en
Alexander P Golovanov
@es
Alexander P Golovanov
@nl
Alexander P Golovanov
@sl
altLabel
Alexander P. Golovanov
@en
Sasha Golovanov
@en
prefLabel
Alexander P Golovanov
@ast
Alexander P Golovanov
@en
Alexander P Golovanov
@es
Alexander P Golovanov
@nl
Alexander P Golovanov
@sl
P106
P21
P31
P496
0000-0002-8592-3984