Research Topics
Genomes and Genes | Alasdair C StevenSummaryAffiliation: National Institutes of Health Country: USA Publications
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Detail Information
Publications
Structure, assembly, and antigenicity of hepatitis B virus capsid proteinsAlasdair C Steven
Laboratory of Structural Biology, National Institute of Arthritis, Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA
Adv Virus Res 64:125-64. 2005- Biochemistry. Viral glycoproteins and an evolutionary conundrumAlasdair C Steven
Laboratory of Structural Biology, National Institute of Arthritis and Musculoskeletal and Skin Diseases, 50 South Drive, Bethesda, MD 20892, USA
Science 313:177-8. 2006 
Structural changes in Influenza virus at low pH characterized by cryo-electron tomographyJuan Fontana
Laboratory of Structural Biology, National Institute of Arthritis, Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, Maryland, USA
J Virol 86:2919-29. 2012..However, it appears desirable for productive infection that fusion should proceed before the RNPs become coagulated with matrix protein, as eventually happens at low pH...- Allosteric signaling and a nuclear exit strategy: binding of UL25/UL17 heterodimers to DNA-Filled HSV-1 capsidsBenes L Trus
Laboratory of Structural Biology Research, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, MD 20892, USA
Mol Cell 26:479-89. 2007..We infer that binding of the ordered population reflects structural changes induced on the outer surface as pressure builds up inside the capsid during DNA packaging. Its binding may signal that the C-capsid is ready to exit the nucleus... - Visualization of the two-step fusion process of the retrovirus avian sarcoma/leukosis virus by cryo-electron tomographyGiovanni Cardone
Laboratory of Structural Biology, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, Maryland, USA
J Virol 86:12129-37. 2012..In addition, some of the products presented a density layer underlying and resolved from the viral membrane, which may represent detachment of the matrix protein to facilitate the fusion process... - Visualization of the herpes simplex virus portal in situ by cryo-electron tomographyGiovanni Cardone
Laboratory of Structural Biology Research, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, MD 20892 8025, USA
Virology 361:426-34. 2007..This distinction may be indicative of divergence at the level of portal-related functions other than its role as a DNA channel... - ClpA and ClpX ATPases bind simultaneously to opposite ends of ClpP peptidase to form active hybrid complexesJoaquin Ortega
Laboratory of Structural Biology, National Institute of Arthritis, Musculoskeletal and Skin Diseases, Bethesda, MD 20892, USA
J Struct Biol 146:217-26. 2004..Thus, ClpXAP is a bifunctional protease whose two ends can independently target different classes of substrates... - Packaging accessory protein P7 and polymerase P2 have mutually occluding binding sites inside the bacteriophage 6 procapsidDaniel Nemecek
Laboratory of Structural Biology, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, Maryland, USA
J Virol 86:11616-24. 2012..Thus, P7 may promote packaging either by interacting directly with incoming RNA or by modulating the structure of the translocation pore... - A free energy cascade with locks drives assembly and maturation of bacteriophage HK97 capsidPhilip D Ross
Laboratory of Molecular Biology, National Institute of Diabetes, Digestive and Kidney Diseases, Bethesda, MD 20892, USA
J Mol Biol 364:512-25. 2006..To explain the whiffleball phenotype, we suggest that these effects propagate to the capsomer periphery in such a way as to differentially affect the stability or solubility of dissociated pentamers, leaving only hexamers to reassemble... - Local and global mobility in the ClpA AAA+ chaperone detected by cryo-electron microscopy: functional connotationsGrégory Effantin
Laboratory of Structural Biology Research, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, MD 20892, USA
Structure 18:553-62. 2010..Based on these observations, we present a pseudo-atomic model of ClpAP holoenzyme, a dynamic proteolytic nanomachine... - Molecular basis for the high degree of antigenic cross-reactivity between hepatitis B virus capsids (HBcAg) and dimeric capsid-related protein (HBeAg): insights into the enigmatic nature of the e-antigenNorman R Watts
Protein Expression Laboratory, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, MD 20892, USA
J Mol Biol 398:530-41. 2010..These results suggest new approaches for the isolation of the authentic e-antigen, its biological assay, and its stabilization as an immune complex for structural studies... - The UL36 tegument protein of herpes simplex virus 1 has a composite binding site at the capsid verticesGiovanni Cardone
Laboratory of Structural Biology, National Institutes of Health, Bethesda, Maryland, USA
J Virol 86:4058-64. 2012..They also indicate how sequential conformational changes in the maturing nucleocapsid control the ordered binding, first of UL25/UL17 and then of UL36... - Architecture of Ure2p prion filaments: the N-terminal domains form a central core fiberUlrich Baxa
Laboratories of Structural Biology, National Institute of Arthritis, Musculoskeletal, and Skin Diseases, and Biochemistry and Genetics, NIDDK, National Institutes of Health, Bethesda, Maryland 20892, USA
J Biol Chem 278:43717-27. 2003.... - Suppression of a morphogenic mutant in Rous sarcoma virus capsid protein by a second-site mutation: a cryoelectron tomography studyCarmen Butan
Laboratory of Structural Biology, National Institute for Arthritis, Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda Maryland 20892, USA
J Virol 84:6377-86. 2010..We conclude that the wild-type CA protein sequence represents an evolutionary compromise between competing requirements for optimization of Gag assembly (of the immature virion) and CA assembly (in the maturing virion)... - Procapsid assembly, maturation, nuclear exit: dynamic steps in the production of infectious herpesvirionsGiovanni Cardone
National Institute for Arthritis, Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, MD 20892, USA
Adv Exp Med Biol 726:423-39. 2012.... - Characterization of beta-sheet structure in Ure2p1-89 yeast prion fibrils by solid-state nuclear magnetic resonanceUlrich Baxa
Laboratory of Structural Biology, National Institute of Arthritis, Musculoskeletal, and Skin Diseases, National Institutes of Health, Bethesda, Maryland 20892 8025, USA
Biochemistry 46:13149-62. 2007.... - Filaments of the Ure2p prion protein have a cross-beta core structureUlrich Baxa
Laboratory of Structural Biology, National Institute of Arthritis, Musculoskeletal, and Skin Diseases, National Institutes of Health, Bethesda, MD 20892, USA
J Struct Biol 150:170-9. 2005..Local area electron diffraction and X-ray diffraction from partially aligned specimens showed that the 4.7A reflection is meridional and therefore the underlying structure is cross-beta... - RSV capsid polymorphism correlates with polymerization efficiency and envelope glycoprotein content: implications that nucleation controls morphogenesisCarmen Butan
Laboratory of Structural Biology, National Institute for Arthritis, Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, MD 20892, USA
J Mol Biol 376:1168-81. 2008..These observations imply that initiation of CA assembly, in which interactions of spike endodomains with the Gag layer play a role, is a critical determinant of core morphology... - Non-canonical binding of an antibody resembling a naïve B cell receptor immunoglobulin to hepatitis B virus capsidsNorman R Watts
Protein Expression Laboratory, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, MD 20892, USA
J Mol Biol 379:1119-29. 2008..Considerations of conserved sequence motifs in other such molecules suggest that other naïve B cells may interact with HBV capsids in much the same way... - The N-terminal substrate-binding domain of ClpA unfoldase is highly mobile and extends axially from the distal surface of ClpAP proteaseTakashi Ishikawa
Laboratory of Structural Biology Research, National Institute of Arthritis, Musculoskeletal and Skin Diseases, Bethesda, MD 20892 8025, USA
J Struct Biol 146:180-8. 2004.... - Role of the propeptide in controlling conformation and assembly state of hepatitis B virus e-antigenNorman R Watts
Protein Expression Laboratory, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, MD 20892, USA
J Mol Biol 409:202-13. 2011..However, this intercalation distorts the dimer into an assembly-reluctant conformation... - Crosslinking renders bacteriophage HK97 capsid maturation irreversible and effects an essential stabilizationPhilip D Ross
Laboratory of Molecular Biology, National Institute of Diabetes, Digestive and Kidney Diseases, Bethesda, MD, USA
EMBO J 24:1352-63. 2005..At pH 4, most K169Y capsids remain as EI-II, whereas wild-type capsids proceed to EI-III, suggesting that crosslink formation drives maturation by a Brownian ratchet mechanism... - Generation and characterization of a chimeric rabbit/human Fab for co-crystallization of HIV-1 RevStephen J Stahl
Protein Expression Laboratory, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, MD 20892 2775, USA
J Mol Biol 397:697-708. 2010..The corresponding single-chain antibody (scFv) was also prepared, offering the potential of intracellular antibody therapeutics against human immunodeficiency virus type 1... - Dynamics of herpes simplex virus capsid maturation visualized by time-lapse cryo-electron microscopyJ Bernard Heymann
Laboratory of Structural Biology, National Institute of Arthritis, Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA
Nat Struct Biol 10:334-41. 2003..The primary mechanism underlying maturation is relative rotations of domains of VP5, the major capsid protein... - Cryo-EM study of Hepatitis B virus core antigen capsids decorated with antibodies from a human patientEaazhisai Kandiah
Laboratory of Structural Biology Research, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, MD 20892, USA
J Struct Biol 177:145-51. 2012..These results show that epitopes on the floor, far (~30 Å) from the immunodominant loop, are clinically relevant and that murine anti-cAg antibodies afford a good model for the human system... - Visualization of a missing link in retrovirus capsid assemblyGiovanni Cardone
Laboratory of Structural Biology, National Institute for Arthritis, Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA
Nature 457:694-8. 2009.... - Virus maturation: dynamics and mechanism of a stabilizing structural transition that leads to infectivityAlasdair C Steven
Laboratory of Structural Biology Research, National Institute of Arthritis, Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, MD 20892, USA
Curr Opin Struct Biol 15:227-36. 2005..Moreover, it has been possible to visualize maturation at the submolecular level in movies based on time-resolved cryo-electron microscopy... - Binding of the ClpA unfoldase opens the axial gate of ClpP peptidaseGrégory Effantin
Laboratory of Structural Biology Research, NIAMS, National Institutes of Health, Bethesda, Maryland 20892, USA
J Biol Chem 285:14834-40. 2010..Based on these observations, we propose that access to the ClpP degradation chamber is controlled allosterically by hinged movements of its N-terminal loops, which the symmetry-mismatched binding of ClpA suffices to induce... - Three-dimensional structure of herpes simplex virus from cryo-electron tomographyKay Grünewald
Laboratory of Structural Biology, National Institute of Arthritis, Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, MD 20892, USA
Science 302:1396-8. 2003..The envelope contained 600 to 750 glycoprotein spikes that varied in length, spacing, and in the angles at which they emerge from the membrane. Their distribution was nonrandom, suggesting functional clustering... - Stepwise expansion of the bacteriophage ϕ6 procapsid: possible packaging intermediatesDaniel Nemecek
National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, MD 20892, USA
J Mol Biol 414:260-71. 2011.... - Structural engineering of a phage lysin that targets gram-negative pathogensPetra Lukacik
Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA
Proc Natl Acad Sci U S A 109:9857-62. 2012.... - A resolution criterion for electron tomography based on cross-validationGiovanni Cardone
Laboratory of Structural Biology, National Institute of Arthritis, Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, MD 20892, USA
J Struct Biol 151:117-29. 2005..Applicable to entire tomograms or selected structures, NLOO has also been tested on experimental tomographic data... - Functional architecture of the retromer cargo-recognition complexAitor Hierro
Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, US Department of Health and Human Services, Bethesda, Maryland 20892, USA
Nature 449:1063-7. 2007..This extended structure presents multiple binding sites for the SNX complex and receptor cargo, and appears capable of flexing to conform to curved vesicular membranes... - Structural dependence of HET-s amyloid fibril infectivity assessed by cryoelectron microscopyNaoko Mizuno
Laboratory of Structural Biology, National Institute of Arthritis, Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, MD 20892, USA
Proc Natl Acad Sci U S A 108:3252-7. 2011..In triplets, this surface is occluded, blocking nucleation and thereby explaining their lack of infectivity... - Poliovirus 2C protein forms homo-oligomeric structures required for ATPase activityPeter Adams
NIAID, National Institutes of Health, Bethesda, MD 20892 8011, USA
J Biol Chem 284:22012-21. 2009..Finally, deletion of the N-terminal 38 amino acids blocked oligomerization of the fusion protein and eliminated ATPase activity, despite retention of an unaltered nucleotide-binding domain... - Structure and polymorphism of the UL6 portal protein of herpes simplex virus type 1Benes L Trus
Laboratory of Structural Biology Research, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, Building 50, Room 1517, MSC 8025, 50 South Drive, Bethesda, MD 20892 8025, USA
J Virol 78:12668-71. 2004..Its architecture resembles those of bacteriophage portal/connector proteins... - Electron microscopic evidence in support of alpha-solenoid models of proteasomal subunits Rpn1 and Rpn2Grégory Effantin
Laboratory of Structural Biology Research, National Institute of Arthritis, Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, MD 20892, USA
J Mol Biol 386:1204-11. 2009..The results support the alpha-solenoid model, except that they indicate that the repeats are organized not as symmetrical circular toroids but in less regular horseshoe-like structures... - Computational resources for cryo-electron tomography in BsoftJ Bernard Heymann
Laboratory of Structural Biology, National Institute of Arthritis, Musculoskeletal and Skin Diseases, National Institutes of Health, Building 50, Room 1515, 50 South Drive MSC 8025, Bethesda, MD 20892 8025, USA
J Struct Biol 161:232-42. 2008..Resources are also included that allow resolution assessment by cross-validation (NLOO2D); denoising and interpretation; and the extraction, mutual alignment, and averaging of tomographic sub-volumes... - HIV-1 maturation inhibitor bevirimat stabilizes the immature Gag latticePaul W Keller
Laboratory of Structural Biology Research, National Institute of Arthritis and Musculoskeletal and Skin Diseases, NIH, Building 50, Room 1517, 50 South Drive, MSC 8025, Bethesda, MD 20892, USA
J Virol 85:1420-8. 2011..In both cases, the observed failure to assemble mature capsids correlates with the loss of infectivity... - Cryo-electron tomography of bacteriophage phi6 procapsids shows random occupancy of the binding sites for RNA polymerase and packaging NTPaseDaniel Nemecek
National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, 50 South Dr, Bethesda, MD 20892, USA
J Struct Biol 171:389-96. 2010..These observations indicate that although P2 and P4 act sequentially on the same substrates there is no direct physical coupling between their activities... - Initial location of the RNA-dependent RNA polymerase in the bacteriophage Phi6 procapsid determined by cryo-electron microscopyAnindito Sen
Laboratory of Structural Biology Research, NIAMS, National Institutes of Health, Bethesda, Maryland 20892, USA
J Biol Chem 283:12227-31. 2008..We propose that, during maturation, the P2 molecules rotate to occupy positions closer to adjacent 5-fold vertices where they conduct replication and transcription... - Arrangement of L2 within the papillomavirus capsidChristopher B Buck
Laboratory of Cellular Oncology, Center for Cancer Research, National Cancer Institute, NIH, Bethesda, Maryland 20892 5624, USA
J Virol 82:5190-7. 2008..This structural information should facilitate investigation of L2 function during the assembly and entry phases of the papillomavirus life cycle... - Multiple modes of endophilin-mediated conversion of lipid vesicles into coated tubes: implications for synaptic endocytosisNaoko Mizuno
Laboratory of Structural Biology, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA
J Biol Chem 285:23351-8. 2010..Our findings suggest that the adaptability of endophilin-lipid interactions underlies dynamic changes of endocytic membranes... - Molecular mechanisms in bacteriophage T7 procapsid assembly, maturation, and DNA containmentMario E Cerritelli
Laboratory of Structural Biology, National Institute of Arthritis, Musculoskeletal, and Skin Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA
Adv Protein Chem 64:301-23. 2003..In the mature T7 head, the DNA is organized as a tightly wound coaxial spool, with the DNA coiled around the core in at least four and perhaps as many as six concentric shells... - Co-assembly of envoplakin and periplakin into oligomers and Ca(2+)-dependent vesicle binding: implications for cornified cell envelope formation in stratified squamous epitheliaAndrey E Kalinin
Laboratory of Skin Biology and Laboratory of Structural Biology, NIAMS, National Institutes of Health, Bethesda, Maryland 20892, USA
J Biol Chem 279:22773-80. 2004.... - Is the prion domain of soluble Ure2p unstructured?Michael M Pierce
Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, Bethesda, Maryland 20892 0830, USA
Biochemistry 44:321-8. 2005..These results suggest that the N-terminal prion domain is unstructured in the soluble protein and does not have a specific interaction with the C-terminus... - A second symmetry mismatch at the portal vertex of bacteriophage T7: 8-fold symmetry in the procapsid coreMario E Cerritelli
Laboratory of Structural Biology, National Institute of Arthritis, Musculoskeletal and Skin Diseases, Building 50, Room 1517, MSC 8025, Bethesda, MD 20892-8025, USA
J Mol Biol 327:1-6. 2003..We have investigated the core structure by cryo-electron microscopy and image analysis of procapsids and find that it observes 8-fold symmetry. Stoichiometry data indicate that its major constituent is an octamer of gp15... - Molecular dynamics of protein complexes from four-dimensional cryo-electron microscopyJ Bernard Heymann
Laboratory of Structural Biology, National Institute of Arthritis, Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, MD 20892, USA
J Struct Biol 147:291-301. 2004.... - Antigenic switching of hepatitis B virus by alternative dimerization of the capsid proteinMichael A DiMattia
Division of Structural Biology, Henry Wellcome Building for Genomic Medicine, University of Oxford, Roosevelt Drive, Headington OX3 7BN, UK Laboratory of Structural Biology Research, National Institute of Arthritis and Musculoskeletal and Skin Diseases National Institutes of Health, Bethesda, MD 20892, USA
Structure 21:133-42. 2013..The structure offers insight into how HBeAg may establish immune tolerance for HBcAg while evading its robust immunogenicity... - Remodeling of lipid vesicles into cylindrical micelles by α-synuclein in an extended α-helical conformationNaoko Mizuno
Laboratory of Structural Biology, NIAMS, National Institutes of Health, Bethesda, MD 20892, USA
J Biol Chem 287:29301-11. 2012..The observed geometrical relationship between αS and the micelle suggests that the wedging of its long α-helix into the outer leaflet of a membrane may cause curvature and an anisotropic partition of lipids, leading to tube formation... - Prions of Saccharomyces and PodosporaUlrich Baxa
Laboratory of Biochemistry, National Institute of Diabetes, Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD, USA
Contrib Microbiol 11:50-71. 2004 - Visualization of the binding of Hsc70 ATPase to clathrin baskets: implications for an uncoating mechanismJ Bernard Heymann
Laboratory of Structural Biology, NIAMS, National Institutes of Health, Bethesda, MD, USA
J Biol Chem 280:7156-61. 2005..Three Hsc70s remain bound to the dissociated triskelion, close to its trimerization hub... - Influenza virus pleiomorphy characterized by cryoelectron tomographyAudray Harris
Laboratory of Structural Biology, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, MD 20892, USA
Proc Natl Acad Sci U S A 103:19123-7. 2006.... - In Sup35p filaments (the [PSI+] prion), the globular C-terminal domains are widely offset from the amyloid fibril backboneUlrich Baxa
Laboratory of Structural Biology, National Institute of Arthritis, Musculoskeletal, and Skin Diseases, National Institutes of Health, Bethesda, MD 20892, USA
Mol Microbiol 79:523-32. 2011.... - Mass analysis by scanning transmission electron microscopy and electron diffraction validate predictions of stacked beta-solenoid model of HET-s prion fibrilsAnindito Sen
Laboratory of Structural Biology, National Institute of Arthritis, Musculoskeletal, and Skin Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA
J Biol Chem 282:5545-50. 2007..This is half the packing density of approximately 1 subunit per 0.47 nm previously obtained for fibrils of the yeast prion proteins, Ure2p and Sup35p, whence it follows that the respective amyloid architectures are basically different... - Specificity of an anti-capsid antibody associated with Hepatitis B Virus-related acute liver failureWeimin Wu
Laboratory of Structural Biology, National Institute for Arthritis, Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, MD 20892, United States
J Struct Biol 181:53-60. 2013.... - Extensive proteolysis of head and inner body proteins by a morphogenetic protease in the giant Pseudomonas aeruginosa phage φKZJulie A Thomas
Biochemistry and Molecular Biology, University of Maryland Baltimore, MD 21201, USA
Mol Microbiol 84:324-39. 2012..Together the six abundant proteins sum to the estimated mass of the inner body (15-20 MDa). The identification of these proteins is important for future studies on the composition and function of the inner body... - Structure, function, and amyloidogenesis of fungal prions: filament polymorphism and prion variantsUlrich Baxa
Laboratory of Structural Biology, National Institute of Arthritis, Musculoskeletal, and Skin Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA
Adv Protein Chem 73:125-80. 2006..We discuss a possible structural basis for this phenomenon... - Bubblegrams reveal the inner body of bacteriophage φKZWeimin Wu
Laboratory of Structural Biology, National Institute of Arthritis and Musculoskeletal and Skin Diseases NIAMS, National Institutes of Health, Bethesda, MD 20892, USA
Science 335:182. 2012..Here, we present a differential mapping procedure, based on the physical principle of protein's greater sensitivity to radiation damage compared with that of nucleic acid... - The cryptophycin-tubulin ring structure indicates two points of curvature in the tubulin dimerNorman R Watts
Protein Expression Laboratory, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA
Biochemistry 41:12662-9. 2002..We conclude that drug binding to one subunit (beta) results in two bends per dimer, affecting both subunits... - Signal transduction at a protein synapseAlasdair C Steven
Laboratory of Structural Biology, NIAMS, Building 50, Room 1517, 50 South Drive MSC 8025, National Institutes of Health, Bethesda, MD 20892, USA
Cell 118:403-4. 2004.... - Subdomain organization of the Acanthamoeba myosin IC tail from cryo-electron microscopyTakashi Ishikawa
Laboratory of Structural Biology Research, National Institute of Arthritis, Musculoskeletal, and Skin Diseases, and Laboratory of Cell Biology, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892, USA
Proc Natl Acad Sci U S A 101:12189-94. 2004..The outer face of the BR is strategically exposed for membrane or vesicle binding... - The axial channel of the 20S proteasome opens upon binding of the PA200 activatorJoaquin Ortega
Laboratory of Structural Biology, National Institute of Arthritis, Musculoskeletal and Skin Diseases, National Institutes of Health, Bldg 50, Room 1517, 50 South Drive MSC 8025, Bethesda, MD 20892-8025, USA
J Mol Biol 346:1221-7. 2005..Thus, the activation mechanism of PA200 is expressed via its allosteric effects on the 20 S core particle, perhaps facilitating release of digestion products or the entrance of substrates... - The N-terminal prion domain of Ure2p converts from an unfolded to a thermally resistant conformation upon filament formationUlrich Baxa
Laboratory of Structural Biology, National Institute of Arthritis, Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, MD 20892, USA
J Mol Biol 339:259-64. 2004..In contrast, no thermal signal was associated with the N-terminal domains: in the soluble state of Ure2p, because they are unfolded; in the filamentous state, because their robust amyloid conformation resists heating to 100 degrees C... - Mechanism of inactivation on prion conversion of the Saccharomyces cerevisiae Ure2 proteinUlrich Baxa
Laboratory of Structural Biology, National Institute of Arthritis, Musculoskeletal, and Skin Diseases, National Institutes of Health, Bethesda, MD 20892, USA
Proc Natl Acad Sci U S A 99:5253-60. 2002..These observations suggest that the amyloid content of these filaments is confined to their prion domain-containing backbones and imply that Ure2p is inactivated in [URE3] cells by a steric blocking mechanism... - Handedness of the herpes simplex virus capsid and procapsidNaiqian Cheng
Laboratory of Structural Biology, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA
J Virol 76:7855-9. 2002..We have determined the handedness of both the herpes simplex virus type 1 capsid and its precursor procapsid by a cryoelectron microscopic tilting method... - The morphogenic linker peptide of HBV capsid protein forms a mobile array on the interior surfaceNorman R Watts
Protein Expression Laboratory, National Institute of Arthritis, Musculoskeletal and Skin Diseases, Building 50, Room 1517, 50 South Drive MSC 8025, National Institutes of Health, Bethesda, MD 20892-8025, USA
EMBO J 21:876-84. 2002..We propose that linker peptides are attached to the capsid inner surface as hinged struts, forming a mobile array, an arrangement with implications for morphogenesis and the management of encapsidated nucleic acid... - Recombinant HA1 produced in E. coli forms functional oligomers and generates strain-specific SRID potency antibodies for pandemic influenza vaccinesSurender Khurana
Division of Viral Products, Center for Biologics Evaluation and Research CBER, Food and Drug Administration, Bethesda, MD 20892, USA
Vaccine 29:5657-65. 2011..We conclude that bacterially expressed recombinant HA1 proteins can be produced rapidly and used to generate SRID potency reagents shortly after new influenza strains with pandemic potential are identified... - Initial stages of V(D)J recombination: the organization of RAG1/2 and RSS DNA in the postcleavage complexGabrielle J Grundy
Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA
Mol Cell 35:217-27. 2009..These first images of the V(D)J recombinase in its postcleavage state provide a framework for modeling RAG domains and their interactions with DNA... - Human immunodeficiency virus type 1 N-terminal capsid mutants containing cores with abnormally high levels of capsid protein and virtually no reverse transcriptaseShixing Tang
Laboratory of Molecular Genetics, National Institute of Child Health and Human Development, Bethesda, Maryland 20892, USA
J Virol 77:12592-602. 2003..Thus, taken together with the almost complete absence of RT in mutant cores, these findings can account for the failure of the three CA mutants to synthesize viral DNA following virus entry into cells... - Cryo-electron microscopy of trichocyte (hard alpha-keratin) intermediate filaments reveals a low-density coreNorman R Watts
Laboratory of Structural Biology Research, National Institutes of Health, Bethesda, Maryland 20892 8025, USA
J Struct Biol 137:109-18. 2002..3 nm. These filaments appear to represent IF coated with associated proteins-perhaps, "high-sulfur" proteins-readied for incorporation into the filament-matrix biocomposite of the mature hair... - The next ice age: cryo-electron tomography of intact cellsAlasdair C Steven
Laboratory of Structural Biology, National Institute of Arthritis, Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, MD 20892, USA
Trends Cell Biol 13:107-10. 2003..Cryo-tomograms of Dictyostelium cells depict distinct populations of ribosomes, proteasomes and networks of actin filaments interconnected by branching or bundling, apparently controlled by strategically placed actin-associated proteins... - Functional proteolytic complexes of the human mitochondrial ATP-dependent protease, hClpXPSung Gyun Kang
Laboratory of Cell Biology, NCI and Laboratory of Structural Biology, NIAMS, National Institutes of Health, Bethesda, Maryland 20892, USA
J Biol Chem 277:21095-102. 2002..Our data also indicate that human ClpP has conserved sites required for interaction with eClpX but not eClpA, implying that the modes of interaction with ClpP may not be identical for ClpA and ClpX... - Quasi-normal cornified cell envelopes in loricrin knockout mice imply the existence of a loricrin backup systemMichal Jarnik
Laboratory of Structural Biology, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, Maryland 20892 8025, USA
J Invest Dermatol 118:102-9. 2002..These observations imply that, in the absence of loricrin, the mechanisms that govern cell envelope assembly function normally but employ different building-blocks... - Alternating translocation of protein substrates from both ends of ClpXP proteaseJoaquin Ortega
Laboratory of Structural Biology, National Institute of Arthritis, Musculoskeletal and Skin Diseases and Laboratory of Cell Biology, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA
EMBO J 21:4938-49. 2002.... - The Sm-like Hfq protein increases OxyS RNA interaction with target mRNAsAixia Zhang
Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, Bethesda, MD 20892, USA
Mol Cell 9:11-22. 2002..We also show that Hfq increases the OxyS RNA interaction with its target messages and propose that the enhancement of RNA-RNA pairing may be a general function of Hfq, Sm, and Sm-like proteins... - mtCLIC/CLIC4, an organellular chloride channel protein, is increased by DNA damage and participates in the apoptotic response to p53Ester Fernandez-Salas
Laboratory of Cellular Carcinogenesis and Tumor Promotion, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892, USA
Mol Cell Biol 22:3610-20. 2002.... - High-resolution mass spectrometry of viral assemblies: molecular composition and stability of dimorphic hepatitis B virus capsidsCharlotte Uetrecht
Biomolecular Mass Spectrometry and Proteomics Group, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Sorbonnelaan 16, 3584 CA, Utrecht, The Netherlands
Proc Natl Acad Sci U S A 105:9216-20. 2008..4 GPa. This experimental approach, anchored on very precise and accurate mass measurements, appears to hold considerable potential for elucidating the assembly of viruses and other macromolecular particles... - Stability and shape of hepatitis B virus capsids in vacuoCharlotte Uetrecht
Biomolecular Mass Spectrometry and Proteomics Group, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Sorbonnelaan 16, 3584 CA Utrecht, The Netherlands
Angew Chem Int Ed Engl 47:6247-51. 2008 - Time-resolved molecular dynamics of bacteriophage HK97 capsid maturation interpreted by electron cryo-microscopy and X-ray crystallographyWilliam R Wikoff
Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA
J Struct Biol 153:300-6. 2006.... - The structure of the poliovirus 135S cell entry intermediate at 10-angstrom resolution reveals the location of an externalized polypeptide that binds to membranesDoryen Bubeck
Department of Chemistry and Biochemistry, Brigham Young University, Provo, UT 84602, USA
J Virol 79:7745-55. 2005..These observations have forced a reexamination of current models for the role of the 135S particle in transmembrane pore formation and suggest testable alternatives... - Structural and functional similarities between the capsid proteins of bacteriophages T4 and HK97 point to a common ancestryAndrei Fokine
Department of Biological Sciences, Purdue University, 915 West State Street, West Lafayette, IN 47907, USA
Proc Natl Acad Sci U S A 102:7163-8. 2005..Structural data show that capsid proteins of most tailed phages, and some eukaryotic viruses, may have evolved from a common ancestor... - A novel class of herpesvirus with bivalve hostsAndrew J Davison
MRC Virology Unit, Institute of Virology, Church Street, Glasgow G11 5JR, UK
J Gen Virol 86:41-53. 2005..OsHV-1 thus represents a third major class of the herpesviruses... - The turn of the screw: variations of the abundant beta-solenoid motif in passenger domains of Type V secretory proteinsAndrey V Kajava
Centre de Recherches de Biochimie Macromoleculaire, CNRS FRE 2593, 1919 Route de Mende, 34293 Montpellier, Cedex 5, France
J Struct Biol 155:306-15. 2006..To illustrate model-building from a coil template, we modeled a type-T4 beta-solenoid for TibA of Escherichia coli which is predicted to have two conserved polar residues, Thr and Gln, in interior positions... - Control of crosslinking by quaternary structure changes during bacteriophage HK97 maturationLu Gan
Department of Molecular Biology, The Scripps Research Institute, La Jolla, CA 92037, USA
Mol Cell 14:559-69. 2004..A structure derived from cryo-EM images reveals the free intermediate conformation of penton arms, supporting our model for coordinated movement of hexons and pentons on the capsid lattice... - New HEAT-like repeat motifs in proteins regulating proteasome structure and functionAndrey V Kajava
Centre de Recherches de Biochimie Macromoleculaire, CNRS FRE 2593, 1919 Route de Mende, 34293 Montpellier, Cedex 5, France
J Struct Biol 146:425-30. 2004..Both PA200 and Ecm29 are composed almost entirely of such repeats, and therefore are likely to have alpha-helical solenoid structures. These observations lead us to speculate on how PA200 and Ecm29 may associate with proteasomes... - Control of virus assembly: HK97 "Whiffleball" mutant capsids without pentonsYiyong Li
Department of Biological Sciences, University of Pittsburgh, PA 15260, USA
J Mol Biol 348:167-82. 2005..The data therefore favor a model in which Prohead I assembly is regulated by conformational switching of the hexamer... - Prion and non-prion amyloids of the HET-s prion forming domainRaimon Sabate
Laboratoire de Génétique Moléculaire des Champignons, Institut de Biochimie et de Génétique Cellulaires, UMR 5095 CNRS Université de Bordeaux 2, 1 rue Camille St Saëns, 33077 Bordeaux Cedex, France
J Mol Biol 370:768-83. 2007..The altered properties of the amyloid assembled at pH 2 may arise from a perturbation in the subunit fold or fibrillar stacking... - Structural and enzymatic properties of the AAA protein Drg1p from Saccharomyces cerevisiae. Decoupling of intracellular function from ATPase activity and hexamerizationAndriy Zakalskiy
Institut fur Molekularbiologie, Biochemie und Mikrobiologie, Karl Franzens Universitat Graz, Universitatsplatz 2, A 8010 Graz, Austria
J Biol Chem 277:26788-95. 2002..These observations are discussed in terms of the inter-relationship of ATPase activity per se, oligomeric status, and intracellular function for AAA proteins... - A thermally induced phase transition in a viral capsid transforms the hexamers, leaving the pentamers unchangedJames F Conway
Department of Structural Biology, University of Pittsburgh School of Medicine, Pittsburgh, PA 15260, USA
J Struct Biol 158:224-32. 2007..Pentamers, on the other hand, are more stably anchored and resist this thermal perturbation... - Prospects of electron cryotomography to visualize macromolecular complexes inside cellular compartments: implications of crowdingKay Grünewald
Department of Structural Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18a, D 82152 Martinsried, Germany
Biophys Chem 100:577-91. 2003..An example of the latter-a 5-fold symmetric particle is-given. Second, electron cryotomography offers an incisive probe to examine crowding in different cellular compartments... - Beta-rolls, beta-helices, and other beta-solenoid proteinsAndrey V Kajava
, CNRS FRE-2593, 1919 Route de Mende, 34293 Montpellier Cedex 5, France
Adv Protein Chem 73:55-96. 2006..Thus, identification of genes with putative beta-solenoid domains promises to be a fertile direction in the search for viable targets in the development of new antibiotics and vaccines... - Standard conformations of beta-arches in beta-solenoid proteinsJérôme Hennetin
Centre de Recherches de Biochimie Macromoleculaire, CNRS FRE 2593, 1919 Route de Mende, 34293 Montpellier Cedex 5, France
J Mol Biol 358:1094-105. 2006.... - The parallel superpleated beta-structure as a model for amyloid fibrils of human amylinAndrey V Kajava
Centre de Recherches de Biochimie Macromoleculaire, CNRS FRE 2593, 1919 Route de Mende, 34293 Montpellier Cedex 5, France
J Mol Biol 348:247-52. 2005..The model is consistent with current biophysical, biochemical and genetic data and, in particular, affords a plausible explanation for why rodent amylin does not form fibrils... - A model for Ure2p prion filaments and other amyloids: the parallel superpleated beta-structureAndrey V Kajava
, Centre National de la Recherche Scientifique FRE-2593, 1919 Route de Mende, 34293 Montpellier 5, France
Proc Natl Acad Sci U S A 101:7885-90. 2004..47 nm) and is readily adaptable to other amyloids, for instance the core of Sup35p filaments and glutamine expansions in huntingtin...