about
The Staphylococcus aureus pathogenicity island 1 protein gp6 functions as an internal scaffold during capsid size determination.West Nile virus core protein; tetramer structure and ribbon formation.DNA packaging intermediates of bacteriophage phi X174.Phosphate induces formation of matrix vesicles during odontoblast-initiated mineralization in vitroIncorporation of scaffolding protein gpO in bacteriophages P2 and P4.Cryo-EM analysis of the organization of BclA and BxpB in the Bacillus anthracis exosporium.Structure and size determination of bacteriophage P2 and P4 procapsids: function of size responsiveness mutationsStructural studies on the authentic mumps virus nucleocapsid showing uncoiling by the phosphoproteinDirect observation of membrane insertion by enveloped virus matrix proteins by phosphate displacementStructural heterogeneity and protein composition of exosome-like vesicles (prostasomes) in human semen.Specific N-terminal cleavage of ribosomal protein L27 in Staphylococcus aureus and related bacteriaMobilization of pathogenicity islands by Staphylococcus aureus strain Newman bacteriophagesAssembly of bacteriophage 80α capsids in a Staphylococcus aureus expression system.The Type 2 dUTPase of Bacteriophage ϕNM1 Initiates Mobilization of Staphylococcus aureus Bovine Pathogenicity Island 1.Grape exosome-like nanoparticles induce intestinal stem cells and protect mice from DSS-induced colitis.Convergent evolution of pathogenicity islands in helper cos phage interference.ϕX174 Procapsid Assembly: Effects of an Inhibitory External Scaffolding Protein and Resistant Coat Proteins In VitroDerepression of SaPIbov1 Is Independent of φNM1 Type 2 dUTPase Activity and Is Inhibited by dUTP and dUMP.A conformational switch involved in maturation of Staphylococcus aureus bacteriophage 80α capsids.Capsid size determination by Staphylococcus aureus pathogenicity island SaPI1 involves specific incorporation of SaPI1 proteins into procapsids.The capsid size-determining protein Sid forms an external scaffold on phage P4 procapsids.Structural transitions during maturation of bacteriophage lambda capsids.Capsid localization of the bacteriophage P4 Psu protein.Competing scaffolding proteins determine capsid size during mobilization of Staphylococcus aureus pathogenicity islands.The roles of SaPI1 proteins gp7 (CpmA) and gp6 (CpmB) in capsid size determination and helper phage interference.Functional domains of the bacteriophage P2 scaffolding protein: identification of residues involved in assembly and protease activity.Bacteriophage P2 and P4 morphogenesis: assembly precedes proteolytic processing of the capsid proteins.Purification, crystallization and X-ray analysis of Hibiscus chlorotic ringspot virus.Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of the structural domain of the nucleocapsid N protein from porcine reproductive and respiratory syndrome virus (PRRSV).Expression, purification, crystallization and preliminary crystallographic analysis of the calponin-homology domain of Rng2.Bacteriophage P2 and P4 assembly: alternative scaffolding proteins regulate capsid size.Three-dimensional reconstruction of hibiscus chlorotic ringspot virus.Cleavage and Structural Transitions during Maturation of Staphylococcus aureus Bacteriophage 80α and SaPI1 Capsids.The gpQ portal protein of bacteriophage P2 forms dodecameric connectors in crystals.Characterization of the capsid associating activity of bacteriophage P4's Psu protein.Exosomal transfer of mitochondria from airway myeloid-derived regulatory cells to T cells.Structure, crystal packing and molecular dynamics of the calponin-homology domain ofSchizosaccharomyces pombeRng2Cleavage leads to expansion of bacteriophage P4 procapsids in vitroIn Vitro Assembly of Bacteriophage P4 Procapsids from Purified Capsid and Scaffolding ProteinsStructure of the host cell recognition and penetration machinery of a Staphylococcus aureus bacteriophage
P50
Q27671573-C82727A6-DD56-4F77-8DC5-F79439ACCA22Q30342184-ED53A65F-DE03-40C0-A4EB-57819A9ECF1DQ30537248-714601A3-B82E-4E20-8AC4-EBE2B81AE86DQ30760327-8DDDC385-19DF-4158-8008-72670A671494Q33302360-9731C179-C372-4E33-84F7-7C14B92A1AFDQ33852981-A56F0B9C-E9B0-4660-AFE6-2603FCA81694Q34268576-129137D3-F186-4724-9AB7-EA172ABEFA46Q34409094-B5C5BAED-9F23-4940-A54B-BB4344BFDAE8Q34612640-9C886B5B-ECF5-4D46-B28D-E1BA117B3441Q34838195-0523510C-1350-4AC9-97C1-DCD70CBC462EQ35565456-342130E2-07DC-456B-80DC-C6DF35EB44D2Q36235367-C5570FC4-0100-4D32-B1B6-440A18E8E529Q36457215-06BC92FD-CEE4-41E1-A12A-2514E07728D2Q36535768-DF83F440-3A14-42ED-B7B6-CF3D024EE2E2Q36984496-DFCE856A-8368-467C-9382-2AFE2C36CBADQ37315269-EFC97597-5B9B-49FB-8CEC-0597BE023F1DQ37512778-22CAA0BF-EB4A-441B-B3C0-B04A896DF9BAQ40247054-7712B6E9-D9AB-45B4-BFEF-130BC9BDAD2DQ41616901-69B1D793-42BB-45E2-87CB-D21CF398B12CQ41622697-732ADD0D-695F-4ECD-A047-83E7326CBFB2Q41634301-D789C6BD-5C21-4A9F-BBF0-284F26009E70Q41634987-30EA409C-F92C-472E-B1E9-4467E0E4A8B7Q41635055-08C51442-439A-4506-BCBD-803C4B42ED52Q41990469-09DC93F4-37EB-41A4-BA90-2252548A27FEQ42284119-E3C11F3F-058F-4DC4-9634-D0EDCEE00653Q43163516-DB4B3FD7-5C45-4635-8F58-69D72D12042BQ43985898-405F33DB-E652-4838-8897-601BC990860CQ44238064-D27E2DCB-CA75-4A11-AEBF-F21FE3E49D32Q44522553-C1EABFC0-1F68-4D9B-B367-DD8D026D7393Q44591096-F9572113-7A2F-46D1-A8E2-FB3C0F494C7AQ44890099-8E5F4B82-D1E0-4D89-AC76-0E869B3C54F0Q45707633-F711B86F-DF5B-4A34-B8B5-31104B4593B7Q47113240-EDB19B6B-1D48-49EA-8419-BCCB53E45177Q54453475-BD30D691-C6B3-46AA-8FD8-976E18E8B5EAQ54656205-C9739D29-EFD0-4CF3-AA2A-D3E31BDD7C4FQ55518860-8C754390-6D3A-4494-B024-44DC06F42940Q57036186-4973DD63-B459-4BA1-A96D-5863B41CC8C9Q57036210-6F0C35CF-434E-458D-BF30-A797D98D62D1Q57036235-3DC5E0FD-1608-4D8B-BF88-C6E0F63DD550Q89759501-57DF08CC-5656-4F03-AFB2-C0E6F3D6DCCD
P50
description
hulumtues
@sq
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
Terje Dokland
@ast
Terje Dokland
@en
Terje Dokland
@es
Terje Dokland
@sl
type
label
Terje Dokland
@ast
Terje Dokland
@en
Terje Dokland
@es
Terje Dokland
@sl
prefLabel
Terje Dokland
@ast
Terje Dokland
@en
Terje Dokland
@es
Terje Dokland
@sl
P106
P21
P31
P496
0000-0001-5655-4123
P569
2000-01-01T00:00:00Z