Published in Virology on July 23, 2011
Multiple functional roles of the accessory I-domain of bacteriophage P22 coat protein revealed by NMR structure and CryoEM modeling. Structure (2014) 1.07
Decoding bacteriophage P22 assembly: identification of two charged residues in scaffolding protein responsible for coat protein interaction. Virology (2011) 0.93
Nature's favorite building block: Deciphering folding and capsid assembly of proteins with the HK97-fold. Virology (2015) 0.91
A Molecular Staple: D-Loops in the I Domain of Bacteriophage P22 Coat Protein Make Important Intercapsomer Contacts Required for Procapsid Assembly. J Virol (2015) 0.86
Unraveling the role of the C-terminal helix turn helix of the coat-binding domain of bacteriophage P22 scaffolding protein. J Biol Chem (2012) 0.84
Highly specific salt bridges govern bacteriophage P22 icosahedral capsid assembly: identification of the site in coat protein responsible for interaction with scaffolding protein. J Virol (2014) 0.83
NMR assignments for the telokin-like domain of bacteriophage P22 coat protein. Biomol NMR Assign (2012) 0.82
The energetic contributions of scaffolding and coat proteins to the assembly of bacteriophage procapsids. Virology (2012) 0.82
Acquiring Structural Information on Virus Particles with Charge Detection Mass Spectrometry. J Am Soc Mass Spectrom (2016) 0.79
Transient contacts on the exterior of the HK97 procapsid that are essential for capsid assembly. J Mol Biol (2014) 0.78
Mechanism of Protein Denaturation: Partial Unfolding of the P22 Coat Protein I-Domain by Urea Binding. Biophys J (2015) 0.77
Coat protein mutations that alter the flux of morphogenetic intermediates through the φX174 early assembly pathway. J Virol (2017) 0.75
A viral scaffolding protein triggers portal ring oligomerization and incorporation during procapsid assembly. Sci Adv (2017) 0.75
Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal Biochem (1987) 59.79
Physical principles in the construction of regular viruses. Cold Spring Harb Symp Quant Biol (1962) 17.87
FFAS03: a server for profile--profile sequence alignments. Nucleic Acids Res (2005) 4.99
What does structure tell us about virus evolution? Curr Opin Struct Biol (2005) 3.02
Coat protein fold and maturation transition of bacteriophage P22 seen at subnanometer resolutions. Nat Struct Biol (2003) 2.76
Characterization of amber and ochre suppressors in Salmonella typhimurium. J Bacteriol (1979) 2.68
Structural and functional similarities between the capsid proteins of bacteriophages T4 and HK97 point to a common ancestry. Proc Natl Acad Sci U S A (2005) 2.53
Assembly of the head of bacteriophage P22: x-ray diffraction from heads, proheads and related structures. J Mol Biol (1976) 2.32
Three-dimensional transformation of capsids associated with genome packaging in a bacterial virus. J Mol Biol (1993) 2.16
Structural basis for scaffolding-mediated assembly and maturation of a dsDNA virus. Proc Natl Acad Sci U S A (2011) 2.03
Structure of phage P22 coat protein aggregates formed in the absence of the scaffolding protein. J Mol Biol (1978) 1.79
Local rule-based theory of virus shell assembly. Proc Natl Acad Sci U S A (1994) 1.77
Role of the scaffolding protein in P22 procapsid size determination suggested by T = 4 and T = 7 procapsid structures. Biophys J (1998) 1.65
Scaffolding proteins and their role in viral assembly. Cell Mol Life Sci (1999) 1.55
Image reconstruction from cryo-electron micrographs reveals the morphopoietic mechanism in the P2-P4 bacteriophage system. EMBO J (1992) 1.52
P22 coat protein structures reveal a novel mechanism for capsid maturation: stability without auxiliary proteins or chemical crosslinks. Structure (2010) 1.44
Initiation of P22 procapsid assembly in vivo. J Mol Biol (1988) 1.35
Interactions between satellite bacteriophage P4 and its helpers. Annu Rev Genet (1990) 1.35
Structure of the coat protein-binding domain of the scaffolding protein from a double-stranded DNA virus. J Mol Biol (2000) 1.32
'Let the phage do the work': using the phage P22 coat protein structures as a framework to understand its folding and assembly mutants. Virology (2010) 1.32
Assembly of bacteriophage P22: a model for ds-DNA virus assembly. Prog Med Virol (1993) 1.30
Intracellular visualization of precursor capsids in phage P22 mutant infected cells. Virology (1975) 1.27
Functional domains of bacteriophage P22 scaffolding protein. J Mol Biol (1998) 1.23
Capsid size determination by Staphylococcus aureus pathogenicity island SaPI1 involves specific incorporation of SaPI1 proteins into procapsids. J Mol Biol (2008) 1.18
Electrophoresis of bacteriophage T7 and T7 capsids in agarose gels. J Virol (1978) 1.17
Structure and assembly of the capsid of bacteriophage P22. Philos Trans R Soc Lond B Biol Sci (1976) 1.16
Inhibition of viral capsid assembly by 1,1'-bi(4-anilinonaphthalene-5-sulfonic acid). Biochemistry (1993) 1.16
Selective in vivo rescue by GroEL/ES of thermolabile folding intermediates to phage P22 structural proteins. J Biol Chem (1994) 1.16
Binding of scaffolding subunits within the P22 procapsid lattice. Virology (1994) 1.08
A helical coat protein recognition domain of the bacteriophage P22 scaffolding protein. J Mol Biol (1998) 1.07
Molecular genetics of bacteriophage P22 scaffolding protein's functional domains. J Mol Biol (2005) 1.06
Identification of subunit-subunit interactions in bacteriophage P22 procapsids by chemical cross-linking and mass spectrometry. J Proteome Res (2006) 1.05
Bacteriophage P22 scaffolding protein forms oligomers in solution. J Mol Biol (1997) 1.05
Freedom and restraint: themes in virus capsid assembly. Structure (2000) 1.04
Polyhead formation in phage P22 pinpoints a region in coat protein required for conformational switching. Mol Microbiol (2007) 1.02
Determinants of bacteriophage P22 polyhead formation: the role of coat protein flexibility in conformational switching. Mol Microbiol (2010) 0.98
Identification of additional coat-scaffolding interactions in a bacteriophage P22 mutant defective in maturation. J Virol (2000) 0.96
Cryo-reconstructions of P22 polyheads suggest that phage assembly is nucleated by trimeric interactions among coat proteins. Phys Biol (2010) 0.95
Identification and characterization of the domain structure of bacteriophage P22 coat protein. Biochemistry (1999) 0.94
Folding of phage P22 coat protein monomers: kinetic and thermodynamic properties. Virology (2003) 0.93
Single amino acid substitutions globally suppress the folding defects of temperature-sensitive folding mutants of phage P22 coat protein. J Biol Chem (1999) 0.93
Interactions between coat and scaffolding proteins of phage P22 are altered in vitro by amino acid substitutions in coat protein that cause a cold-sensitive phenotype. Biochemistry (1996) 0.88
Structure and inherent properties of the bacteriophage lambda head shell. VII. Molecular design of the form-determining major capsid protein. J Mol Biol (1990) 0.86
Lesser known large dsDNA viruses. Preface. Curr Top Microbiol Immunol (2009) 0.81
Crystallization and preliminary X-ray analysis of the dsDNA bacteriophage HK97 mature empty capsid. Virology (1998) 0.79
P22 coat protein structures reveal a novel mechanism for capsid maturation: stability without auxiliary proteins or chemical crosslinks. Structure (2010) 1.44
Electrostatic interactions govern both nucleation and elongation during phage P22 procapsid assembly. Virology (2005) 1.14
Quantitative analysis of multi-component spherical virus assembly: scaffolding protein contributes to the global stability of phage P22 procapsids. J Mol Biol (2006) 1.14
ATPase activity of Mycobacterium tuberculosis SecA1 and SecA2 proteins and its importance for SecA2 function in macrophages. J Bacteriol (2008) 1.05
Phage P22 procapsids equilibrate with free coat protein subunits. J Mol Biol (2006) 1.05
Polyhead formation in phage P22 pinpoints a region in coat protein required for conformational switching. Mol Microbiol (2007) 1.02
Determinants of bacteriophage P22 polyhead formation: the role of coat protein flexibility in conformational switching. Mol Microbiol (2010) 0.98
An intramolecular chaperone inserted in bacteriophage P22 coat protein mediates its chaperonin-independent folding. J Biol Chem (2013) 0.95
Cryo-reconstructions of P22 polyheads suggest that phage assembly is nucleated by trimeric interactions among coat proteins. Phys Biol (2010) 0.95
Decoding bacteriophage P22 assembly: identification of two charged residues in scaffolding protein responsible for coat protein interaction. Virology (2011) 0.93
Folding of phage P22 coat protein monomers: kinetic and thermodynamic properties. Virology (2003) 0.93
A second-site suppressor of a folding defect functions via interactions with a chaperone network to improve folding and assembly in vivo. Mol Microbiol (2004) 0.91
Conformational changes in bacteriophage P22 scaffolding protein induced by interaction with coat protein. J Mol Biol (2011) 0.87
Unraveling the role of the C-terminal helix turn helix of the coat-binding domain of bacteriophage P22 scaffolding protein. J Biol Chem (2012) 0.84
Highly specific salt bridges govern bacteriophage P22 icosahedral capsid assembly: identification of the site in coat protein responsible for interaction with scaffolding protein. J Virol (2014) 0.83
SecA folding kinetics: a large dimeric protein rapidly forms multiple native states. J Mol Biol (2004) 0.83
Stepwise molecular display utilizing icosahedral and helical complexes of phage coat and decoration proteins in the development of robust nanoscale display vehicles. Biomaterials (2012) 0.82
The energetic contributions of scaffolding and coat proteins to the assembly of bacteriophage procapsids. Virology (2012) 0.82
NMR assignments for the telokin-like domain of bacteriophage P22 coat protein. Biomol NMR Assign (2012) 0.82
Rapid unfolding of a domain populates an aggregation-prone intermediate that can be recognized by GroEL. J Mol Biol (2003) 0.81
GroEL/S substrate specificity based on substrate unfolding propensity. Cell Stress Chaperones (2007) 0.80
A concerted mechanism for the suppression of a folding defect through interactions with chaperones. J Biol Chem (2004) 0.79
ADP-dependent conformational changes distinguish Mycobacterium tuberculosis SecA2 from SecA1. J Biol Chem (2013) 0.78
Molecular glue to cement a phage. Structure (2006) 0.75