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- Publications
- Influence
Polyglutamine disruption of the huntingtin exon1 N-terminus triggers a complex aggregation mechanism
- A. Thakur, Murali Jayaraman, +9 authors R. Wetzel
- Chemistry, Medicine
- Nature Structural &Molecular Biology
- 2 February 2009
Simple polyglutamine (polyQ) peptides aggregate in vitro via a nucleated growth pathway directly yielding amyloid-like aggregates. We show here that the 17-amino-acid flanking sequence (HTTNT)… Expand
Genomic and structural analysis of Syn9, a cyanophage infecting marine Prochlorococcus and Synechococcus.
- Peter R Weigele, Welkin H Pope, +7 authors R. Hendrix
- Biology, Medicine
- Environmental microbiology
- 1 July 2007
Cyanobacteriophage Syn9 is a large, contractile-tailed bacteriophage infecting the widespread, numerically dominant marine cyanobacteria of the genera Prochlorococcus and Synechococcus. Its 177,300… Expand
Molecular Tectonic Model of Virus Structural Transitions: the Putative Cell Entry States of Poliovirus
ABSTRACT Upon interacting with its receptor, poliovirus undergoes conformational changes that are implicated in cell entry, including the externalization of the viral protein VP4 and the N terminus… Expand
Methods for reconstructing density maps of "single" particles from cryoelectron micrographs to subnanometer resolution.
Recently the resolution attainable in density maps calculated from cryo-electron micrographs of free-standing virus capsids has advanced to resolutions below 1 nm. This represents a significant… Expand
Bacteriophage T5 structure reveals similarities with HK97 and T4 suggesting evolutionary relationships.
- G. Effantin, P. Boulanger, E. Neumann, L. Letellier, J. Conway
- Biology, Medicine
- Journal of molecular biology
- 1 September 2006
Evolutionary relationships between viruses may be obscure by protein sequence but unmasked by structure. Analysis of bacteriophage T5 by cryo-electron microscopy and protein sequence analysis reveals… Expand
Proteolytic and conformational control of virus capsid maturation: the bacteriophage HK97 system.
- J. Conway, R. Duda, N. Cheng, R. Hendrix, A. Steven
- Biology, Medicine
- Journal of molecular biology
- 13 October 1995
Bacteriophage capsid assembly pathways provide excellent model systems to study large-scale conformational changes and other mechanisms that regulate the formation of macromolecular complexes. These… Expand
Dimorphism of hepatitis B virus capsids is strongly influenced by the C-terminus of the capsid protein.
- A. Zlotnick, N. Cheng, +4 authors P. Wingfield
- Biology, Medicine
- Biochemistry
- 11 June 1996
Hepatitis B virus (HBV) is an enveloped virus with an icosahedral capsid. Its homodimeric capsid protein ("core antigen") assembles into particles of two sizes, one with T = 3 icosahedral symmetry… Expand
Filamentous hemagglutinin of Bordetella pertussis. A bacterial adhesin formed as a 50-nm monomeric rigid rod based on a 19-residue repeat motif rich in beta strands and turns.
- A. Makhov, J. H. Hannah, +6 authors A. Steven
- Biology, Medicine
- Journal of molecular biology
- 4 August 1994
The filamentous hemagglutinin (FHA) of Bordetella pertussis is an adhesin that binds the bacteria to cells of the respiratory epithelium in whooping-cough infections. Mature FHA is a 220 kDa… Expand
The Herpes Simplex Virus 1 UL17 Protein Is the Second Constituent of the Capsid Vertex-Specific Component Required for DNA Packaging and Retention
- Katerina Toropova, J. Huffman, F. Homa, J. Conway
- Biology, Medicine
- Journal of Virology
- 1 June 2011
ABSTRACT The herpes simplex virus (HSV) UL17 and UL25 minor capsid proteins are essential for DNA packaging. They are thought to comprise a molecule arrayed in five copies around each of the capsid… Expand
The cellular receptor to human rhinovirus 2 binds around the 5‐fold axis and not in the canyon: a structural view
- E. Hewat, E. Neumann, +4 authors D. Blaas
- Biology, Medicine
- The EMBO journal
- 1 December 2000
Human rhinovirus serotype 2 (HRV2) belongs to the minor group of HRVs that bind to members of the LDL‐receptor family including the very low density lipoprotein (VLDL)‐receptor (VLDL‐R). We have… Expand