about
Moniliophthora perniciosa necrosis- and ethylene-inducing protein 2 (MpNep2) as a metastable dimer in solution: structural and functional implicationsThe amino-terminal PrP domain is crucial to modulate prion misfolding and aggregation.Fourier transform infrared spectroscopy provides a fingerprint for the tetramer and for the aggregates of transthyretin.The p53 core domain is a molten globule at low pH: functional implications of a partially unfolded structure.Ligand binding and hydration in protein misfolding: insights from studies of prion and p53 tumor suppressor proteins.The hypothesis of the catalytic action of nucleic acid on the conversion of prion protein.Mutant p53 aggregates into prion-like amyloid oligomers and fibrils: implications for cancer.Volume and energy folding landscape of prion protein revealed by pressure.Protein folding and aggregation: two sides of the same coin in the condensation of proteins revealed by pressure studies.Intriguing nucleic-acid-binding features of mammalian prion protein.PrP interactions with nucleic acids and glycosaminoglycans in function and disease.Experimental approaches to the interaction of the prion protein with nucleic acids and glycosaminoglycans: Modulators of the pathogenic conversion.Allosteric function and dysfunction of the prion protein.The role of RNA in mammalian prion protein conversion.Unraveling Prion Protein Interactions with Aptamers and Other PrP-Binding Nucleic Acids.DNA converts cellular prion protein into the beta-sheet conformation and inhibits prion peptide aggregation.Structural insights into the interaction between prion protein and nucleic acid.Nonspecific prion protein-nucleic acid interactions lead to different aggregates and cytotoxic species.Modulation of prion protein oligomerization, aggregation, and beta-sheet conversion by 4,4'-dianilino-1,1'-binaphthyl-5,5'-sulfonate (bis-ANS).Prion protein complexed to N2a cellular RNAs through its N-terminal domain forms aggregates and is toxic to murine neuroblastoma cellsVirtual drug screening for prion diseases: A valuable step?Conformational dissection of Thermomyces lanuginosus lipase in solution.Synthesis and anti-prion activity evaluation of aminoquinoline analogues.Subunit-subunit interactions and overall topology of the dimeric mitochondrial ATP synthase of Polytomella sp.Pressure-induced formation of inactive triple-shelled rotavirus particles is associated with changes in the spike protein Vp4.Fibrillar aggregates of the tumor suppressor p53 core domain.Insights into the intramolecular coupling between the N- and C-domains of troponin C derived from high-pressure, fluorescence, nuclear magnetic resonance, and small-angle X-ray scattering studies.Cognate DNA stabilizes the tumor suppressor p53 and prevents misfolding and aggregation.Reciprocal remodeling upon binding of the prion protein to its signaling partner hop/STI1.Enhanced prion protein stability coupled to DNA recognition and milieu acidification.Hydration and packing effects on prion folding and beta-sheet conversion. High pressure spectroscopy and pressure perturbation calorimetry studies.A promising anti-prion trimethoxychalcone binds to the globular domain of PrP(C) and changes its cellular location.Distinct modulatory role of RNA in the aggregation of the tumor suppressor protein p53 core domain.Erratum to “Co-localization of mutant p53 and amyloid-like protein aggregates in breast tumors” [Int. J. Biochem. Cell Biol. 43 (1) (2011) 60–64]Heparin Binding by Murine Recombinant Prion Protein Leads to Transient Aggregation and Formation of RNA-Resistant SpeciesResponse to Radulescu and Brenig: Infectious nucleic acids in prion disease: halfway thereRecognition mechanism of d- and l-tryptophan enantiomers using 2-hydroxypropyl-α- or β-cyclodextrins as chiral selectorsDesign, synthesis, structural characterization and in vitro evaluation of new 1,4-disubstituted-1,2,3-triazole derivatives against glioblastoma cellsThe effect of temperature on protein refolding at high pressure: Enhanced green fluorescent protein as a modelA Comprehensive Study on the Activity and Deactivation of Immobilized Lecitase Ultra in Esterifications of Food Waste Streams to Monoacylglycerols
P50
Q28483984-CCF5C29D-55E7-4D07-8384-2A5E6CCFEFAFQ33433749-8BD167AF-E410-49BD-9DBE-15FD3F153266Q33435248-33EAAFC7-BAC3-4F43-9567-C28B79052D07Q33594094-510F38FC-E840-413C-93D8-9D07C662A865Q33671560-1CEA1EE1-BD65-4B2F-8FC5-D53157D61086Q36074709-D5EEE866-3A11-4AEA-95CC-A7025C95CF6FQ36201740-60F72515-CF52-4F3B-9EA1-B400135DC8B8Q36219386-3A68593B-22EA-43B1-8EB4-2662E8F543BEQ36397566-65EAE11C-DF65-4DDB-A2A7-2A0CE09FF7D3Q37075209-55CC5DF7-40BA-4AE2-B2EE-A562C26E7F1AQ37663171-D6846252-59B0-4AEC-A196-33964F8CA585Q37818890-4474C4C6-77EA-4B61-9DC0-0820DEB7553AQ37943799-8E659047-BA8E-440E-A479-DF42B11AADB3Q37957794-0F129264-07A8-4BFA-ACD7-8A7ED3C8BD70Q38288126-6DA051E2-D4C9-474E-940A-BD9A1A334BC1Q38295713-FA25823F-4FE8-49E5-BC42-D5E950E2306FQ38311203-168314BD-A9A8-436F-BE53-06C1DC2BBB1CQ38324510-8D174926-E909-4491-8EBD-1A0EE00E43D2Q38347673-1F1F8B3F-ADCC-48CF-A783-CA942FFC5055Q39680285-49F24033-2CFB-4DFF-BF28-261D5B51CDD6Q42382334-6E1880B4-2353-4383-A8B0-34C9EA843934Q42635584-5638F23B-1F63-41F2-92F9-C67FD2FB2D36Q42924771-49E77C46-86EB-4CF2-AC74-16E123D65307Q43147828-0FF93462-5763-491A-8287-08CC7466EBD6Q43567994-4E58E511-8FB8-4B5E-A60F-C839F4EE6F65Q44528743-D6507032-DD36-44EC-9881-BF8F4FA3B5A1Q44811083-DFF10990-5F61-4F45-8D23-8EE557D40D66Q45978438-CEA00B19-AD18-4CC8-A7E4-61E19C709074Q45985246-66E90BE0-0878-4B95-B68F-F2229DCB9F17Q46088287-7F550E1A-B2A5-49BE-8B9D-39E4F44455E6Q47406192-73922526-9648-45FF-9524-042032EBFAFEQ47406923-7213A53D-D060-4C81-9F7C-F078C534B077Q48262142-37758BEB-6D51-4DF8-9F0A-0AE959F4619FQ57084697-899AF9EA-767B-4211-8DA7-D2D25B9463BBQ57084698-7D6C678E-24ED-46EB-8571-6585CDECDFD9Q57084711-49AC0798-8C4B-4702-97D6-615229C1A227Q57268149-32A69A1D-EAAD-40CD-8FB1-C905AEDA6768Q58089974-D39E8396-4267-47AD-A61B-19362D5607B6Q58089998-35C1A442-22C6-409D-8F29-07148CD0B78AQ58090006-84EAA09E-E566-44D1-937E-6DE4DCB67C7A
P50
description
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Yraima Cordeiro
@ast
Yraima Cordeiro
@en
Yraima Cordeiro
@es
Yraima Cordeiro
@nl
Yraima Cordeiro
@sl
type
label
Yraima Cordeiro
@ast
Yraima Cordeiro
@en
Yraima Cordeiro
@es
Yraima Cordeiro
@nl
Yraima Cordeiro
@sl
prefLabel
Yraima Cordeiro
@ast
Yraima Cordeiro
@en
Yraima Cordeiro
@es
Yraima Cordeiro
@nl
Yraima Cordeiro
@sl
P1053
J-7619-2012
P106
P31
P3829
P496
0000-0003-4278-212X
P569
2000-01-01T00:00:00Z