Imperial College London

ProfessorMarinvan Heel

Faculty of Natural SciencesDepartment of Life Sciences

Visiting Professor
 
 
 
//

Contact

 

+44 (0)20 7594 5316m.vanheel Website

 
 
//

Assistant

 

Dr Audrey Geffen +44 (0)20 7594 5323

 
//

Location

 

G20Flowers buildingSouth Kensington Campus

//

Summary

 

Publications

Publication Type
Year
to

89 results found

Stewart L, Manvell M, Hillery E, Etheridge CJ, Cooper RG, Stark H, van-Heel M, Preuss M, Alton EWFW, Miller ADet al., 2001, Cationic lipids for gene therapy part 4 - Physico-chemical analysis of cationic liposome-DNA complexes (lipoplexes) with respect to in vitro and in vivo gene delivery efficiency, JOURNAL OF THE CHEMICAL SOCIETY-PERKIN TRANSACTIONS 2, Pages: 624-632, ISSN: 1472-779X

Journal article

van Heel M, 2001, Do single (ribosome) molecules phase themselves?, COLD SPRING HARBOR SYMPOSIA ON QUANTITATIVE BIOLOGY, Vol: 66, Pages: 77-86, ISSN: 0091-7451

Journal article

Finn RD, Orlova EV, Gowen B, Buck M, van Heel Met al., 2000, Escherichia coli RNA polymerase cove and holoenzyme structures, EMBO JOURNAL, Vol: 19, Pages: 6833-6844, ISSN: 0261-4189

Journal article

Zhang XD, Shaw A, Bates PA, Newman RH, Gowen B, Orlova E, Gorman MA, Kondo H, Dokurno P, Lally J, Leonard G, Meyer H, van Heel M, Freemont PSet al., 2000, Structure of the AAA ATPase p97, MOLECULAR CELL, Vol: 6, Pages: 1473-1484, ISSN: 1097-2765

Journal article

van Heel M, Gowen B, Matadeen R, Orlova EV, Finn R, Pape T, Cohen D, Stark H, Schmidt R, Schatz M, Patwardhan Aet al., 2000, Single-particle electron cryo-microscopy: towards atomic resolution, QUARTERLY REVIEWS OF BIOPHYSICS, Vol: 33, Pages: 307-369, ISSN: 0033-5835

Journal article

Royer WE, Strand K, van Heel M, Hendrickson WAet al., 2000, Structural hierarchy in erythrocruorin, the giant respiratory assemblage of annelids, PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, Vol: 97, Pages: 7107-7111, ISSN: 0027-8424

Journal article

Dolly JO, Akhtar S, Shamotienko O, Papakosta M, Stark H, Booy F, Orlova E, van Heel M, Weir Met al., 2000, Kv1 channels subtypes from brain: recreation by expression of their different alpha/beta subunit combinations, JOURNAL OF PHYSIOLOGY-LONDON, Vol: 525, Pages: 24S-24S, ISSN: 0022-3751

Journal article

Ashton AC, Rahman MA, Volynski KE, Manser C, Orlova EV, Matsushita H, Davletov BA, van Heel M, Grishin EV, Ushkaryov YAet al., 2000, Tetramerisation of alpha-latrotoxin by divalent cations is responsible for toxin-induced non-vesicular release and contributes to the Ca2+-dependent vesicular exocytosis from synaptosomes, BIOCHIMIE, Vol: 82, Pages: 453-468, ISSN: 0300-9084

Journal article

Mueller F, Sommer I, Baranov P, Matadeen R, Stoldt M, Wohnert J, Gorlach M, van Heel M, Brimacombe Ret al., 2000, The 3D arrangement of the 23 S and 5 S rRNA in the Escherichia coli 50 S ribosomal subunit based on a cryo-electron microscopic reconstruction at 7.5 angstrom resolution, JOURNAL OF MOLECULAR BIOLOGY, Vol: 298, Pages: 35-59, ISSN: 0022-2836

Journal article

van Heel M, 2000, Unveiling ribosomal structures: the final phases, CURRENT OPINION IN STRUCTURAL BIOLOGY, Vol: 10, Pages: 259-264, ISSN: 0959-440X

Journal article

Stark H, Rodnina MV, Wieden HJ, van Heel M, Wintermeyer Wet al., 2000, Large-scale movement of elongation factor G and extensive conformational change of the ribosome during translocation, CELL, Vol: 100, Pages: 301-309, ISSN: 0092-8674

Journal article

Orlova EV, Rahman MA, Gowen B, Volynski KE, Ashton AC, Manser C, van Heel M, Ushkaryov YAet al., 2000, Structure of alpha-latrotoxin oligomers reveals that divalent cation-dependent tetramers form membrane pores, NATURE STRUCTURAL BIOLOGY, Vol: 7, Pages: 48-53, ISSN: 1072-8368

Journal article

Ashton AC, Rahman MA, Volynski KE, Manser C, Orlova EV, Matsushita H, van Heel M, Ushkaryov YAet al., 2000, Molecular mechanisms of latrotoxin action, EUROPEAN JOURNAL OF NEUROSCIENCE, Vol: 12, Pages: 16-16, ISSN: 0953-816X

Journal article

Nield J, Orlova EV, Morris EP, Gowen B, van Heel M, Barber Jet al., 2000, 3D map of the plant photosystem II supercomplex obtained by cryoelectron microscopy and single particle analysis, NATURE STRUCTURAL BIOLOGY, Vol: 7, Pages: 44-47, ISSN: 1072-8368

Journal article

Pape T, Stark H, Matadeen R, Orlova EV, van Heel Met al., 2000, Visualization of the translational elongation cycle by cryo-electron microscopy, International Ribosome Conference, Publisher: AMER SOC MICROBIOLOGY, Pages: 37-44

Conference paper

Nield J, Orlova, E etc, 2000, Three-dimensional structure of the spinach photosystem II core complex

Conference paper

Bottcher C, Ludwig K, Herrmann A, van Heel M, Stark Het al., 1999, Structure of influenza haemagglutinin at neutral and at fusogenic pH by electron cryo-microscopy, FEBS LETTERS, Vol: 463, Pages: 255-259, ISSN: 1873-3468

Journal article

Matadeen R, Patwardhan A, Gowen B, Orlova EV, Pape T, Cuff M, Mueller F, Brimacombe R, van Heel Met al., 1999, The Escherichia coli large ribosomal subunit at 7.5 angstrom resolution, STRUCTURE WITH FOLDING & DESIGN, Vol: 7, Pages: 1575-1583, ISSN: 0969-2126

Journal article

Serysheva II, Schatz M, van Heel M, Chiu W, Hamilton SLet al., 1999, Structure of the skeletal muscle calcium release channel activated with Ca2+ and AMP-PCP., Biophys J, Vol: 77, Pages: 1936-1944, ISSN: 0006-3495

The functional state of the skeletal muscle Ca2+ release channel is modulated by a number of endogenous molecules during excitation-contraction. Using electron cryomicroscopy and angular reconstitution techniques, we determined the three-dimensional (3D) structure of the skeletal muscle Ca2+ release channel activated by a nonhydrolyzable analog of ATP in the presence of Ca2+. These ligands together produce almost maximum activation of the channel and drive the channel population toward a predominately open state. The resulting 30-A 3D reconstruction reveals long-range conformational changes in the cytoplasmic region that might affect the interaction of the Ca2+ release channel with the t-tubule voltage sensor. In addition, a central opening and mass movements, detected in the transmembrane domain of both the Ca(2+)- and the Ca2+/nucleotide-activated channels, suggest a mechanism for channel opening similar to opening-closing of the iris in a camera diaphragm.

Journal article

Orlova EV, Dube P, Beckmann E, Zemlin F, Lurz R, Trautner TA, Tavares P, van Heel Met al., 1999, Structure of the 13-fold symmetric portal protein of bacteriophage SPP1, NATURE STRUCTURAL BIOLOGY, Vol: 6, Pages: 842-846, ISSN: 1072-8368

Journal article

Harms J, Tocilj A, Levin I, Agmon I, Stark H, Kolln I, van Heel M, Cuff M, Schlunzen F, Bashan A, Franceschi F, Yonath Aet al., 1999, Elucidating the medium-resolution structure of ribosomal particles: an interplay between electron cryo-microscopy and X-ray crystallography, STRUCTURE WITH FOLDING & DESIGN, Vol: 7, Pages: 931-941, ISSN: 0969-2126

Journal article

Hamrin SF, Arneri E, Doering-Arjes P, Mosegaard H, Patwardhan A, Sasov A, Schatz M, van Dyck D, Wickstrom H, van Heel Met al., 1999, A new method for three-dimensional otolith analysis, JOURNAL OF FISH BIOLOGY, Vol: 54, Pages: 223-225, ISSN: 0022-1112

Journal article

Sherman MB, Soejima T, Chiu W, van Heel Met al., 1998, Multivariate analysis of single unit cells in electron crystallography, ULTRAMICROSCOPY, Vol: 74, Pages: 179-199, ISSN: 0304-3991

Journal article

Dube P, Bacher G, Stark H, Mueller F, Zemlin F, van Heel M, Brimacombe Ret al., 1998, Correlation of the expansion segments in mammalian rRNA with the fine structure of the 80 S ribosome; a cryoelectron microscopic reconstruction of the rabbit reticulocyte ribosome at 21 angstrom resolution, JOURNAL OF MOLECULAR BIOLOGY, Vol: 279, Pages: 403-421, ISSN: 0022-2836

Journal article

Dube P, Wieske M, Stark H, Schatz M, Stahl J, Zemlin F, Lutsch G, van Heel Met al., 1998, The 80S rat liver ribosome at 25 angstrom resolution by electron cryomicroscopy and angular reconstitution, STRUCTURE, Vol: 6, Pages: 389-399, ISSN: 0969-2126

Journal article

Stark H, Rodnina M, Brimacombe R, Wintermeyer W, van Heel Met al., 1998, Functional states of the 70S E-Coli ribosome by electron cryomicroscopy, 14th International Congress on Electron Microscopy, Publisher: IOP PUBLISHING LTD, Pages: 719-720

Conference paper

Serysheva II, Schatz M, van Heel M, Chiu W, Hamilton SLet al., 1998, Ca2+-induced conformational changes in the 3D structure of the skeletal muscle Ca2+ release channel, 14th International Congress on Electron Microscopy, Publisher: IOP PUBLISHING LTD, Pages: 733-734

Conference paper

Stark H, Rodnina MV, Rinke-Appel J, Brimacombe R, Wintermeyer W, van Heel Met al., 1997, Visualization of elongation factor Tu on the Escherichia coli ribosome., Nature, Vol: 389, Pages: 403-406, ISSN: 0028-0836

The delivery of a specific amino acid to the translating ribosome is fundamental to protein synthesis. The binding of aminoacyl-transfer RNA to the ribosome is catalysed by the elongation factor Tu (EF-Tu). The elongation factor, the aminoacyl-tRNA and GTP form a stable 'ternary' complex that binds to the ribosome. We have used electron cryomicroscopy and angular reconstitution to visualize directly the kirromycin-stalled ternary complex in the A site of the 70S ribosome of Escherichia coli. Electron cryomicroscopy had previously given detailed ribosomal structures at 25 and 23 A resolution, and was used to determine the position of tRNAs on the ribosome. In particular, the structures of pre-translocational (tRNAs in A and P sites) and post-translocational ribosomes (P and E sites occupied) were both visualized at a resolution of approximately 20 A. Our three-dimensional reconstruction at 18 A resolution shows the ternary complex spanning the inter-subunit space with the acceptor domain of the tRNA reaching into the decoding centre. Domain 1 (the G domain) of the EF-Tu is bound both to the L7/L12 stalk and to the 50S body underneath the stalk, whereas domain 2 is oriented towards the S12 region on the 30S subunit.

Journal article

Mueller F, Stark H, van Heel M, Rinke-Appel J, Brimacombe Ret al., 1997, A new model for the three-dimensional folding of Escherichia coli 16 S ribosomal RNA. III. The topography of the functional centre., J Mol Biol, Vol: 271, Pages: 566-587, ISSN: 0022-2836

We describe the locations of sites within the 3D model for the 16 S rRNA (described in two accompanying papers) that are implicated in ribosomal function. The relevant experimental data originate from many laboratories and include sites of foot-printing, cross-linking or mutagenesis for various functional ligands. A number of the sites were themselves used as constraints in building the 16 S model. (1) The foot-print sites for A site tRNA are all clustered around the anticodon stem-loop of the tRNA; there is no "allosteric" site. (2) The foot-print sites for P site tRNA that are essential for P site binding are similarly clustered around the P site anticodon stem-loop. The foot-print sites in 16 S rRNA helices 23 and 24 are, however, remote from the P site tRNA. (3) Cross-link sites from specific nucleotides within the anticodon loops of A or P site-bound tRNA are mostly in agreement with the model, whereas those from nucleotides in the elbow region of the tRNA (which also exhibit extensive cross-linking to the 50 S subunit) are more widely spread. Again, cross-links to helix 23 are remote from the tRNAs. (4) The corresponding cross-links from E site tRNA are predominantly in helix 23, and these agree with the model. Electron microscopy data are presented, suggestive of substantial conformational changes in this region of the ribosome. (5) Foot-prints for IF-3 in helices 23 and 24 are at a position with close contact to the 50 S subunit. (6) Foot-prints from IF-1 form a cluster around the anticodon stem-loop of A site tRNA, as do also the sites on 16 S rRNA that have been implicated in termination. (7) Foot-print sites and mutations relating to streptomycin form a compact group on one side of the A site anticodon loop, with the corresponding sites for spectinomycin on the other side. (8) Site-specific cross-links from mRNA (which were instrumental in constructing the 16 S model) fit well both in the upstream and downstream regions of the mRNA, and indicate

Journal article

Orlova EV, Dube P, Harris JR, Beckman E, Zemlin F, Markl J, van Heel Met al., 1997, Structure of keyhole limpet hemocyanin type 1 (KLH1) at 15 A resolution by electron cryomicroscopy and angular reconstitution., J Mol Biol, Vol: 271, Pages: 417-437, ISSN: 0022-2836

A three-dimensional reconstruction of keyhole limpet hemocyanin type 1 (KLH1) has been obtained using electron cryomicroscopy at liquid helium temperatures and single particle image processing. The use of a high-contrast embedding medium, 1% (w/v) glucose and 2% (w/v) ammonium molybdate (pH 7.0), enables high-resolution electron micrographs to be recorded close to focus, i.e. with excellent transfer of high-resolution information, while maintaining enough image contrast to localise the individual macromolecules in the images. When low-pass filtered to approximately 45 A resolution, the new 15 A resolution reconstruction is very similar to the earlier reconstructions of gastropodan hemocyanins of specimens embedded in vitreous ice. The map shows much detail and reveals many new symmetry elements in this very large cylindrical molluscan hemocyanin. The full KLH1 didecamer has D5 pointgroup symmetry, yet within the KLH1 decameric half-molecules local 2-fold axes have emerged that make the wall of the KLH1 decamer, in spite of its having an exact C5 symmetry only, resemble the D5-symmetric wall of the decameric cephalopod hemocyanins. In fact, the outside of each tier of this six-tiered gastropodan hemocyanin was found to have an approximate D5 symmetry. Local 2-fold axes also relate the "functional units" within the dimeric "morphological units" of the wall and the collar areas of the 8 MDa KLH1 molecule. Certain local-symmetry-related surface motifs may be present up to 60 times on the outside wall of this highly symmetric cylindrical hemocyanin. Keyhole limpet hemocyanin is used clinically as an immunostimulant. The very strong immune reaction elicited by this hemocyanin may be associated with its intricate hierarchy of local-symmetry components.

Journal article

This data is extracted from the Web of Science and reproduced under a licence from Thomson Reuters. You may not copy or re-distribute this data in whole or in part without the written consent of the Science business of Thomson Reuters.

Request URL: http://wlsprd.imperial.ac.uk:80/respub/WEB-INF/jsp/search-html.jsp Request URI: /respub/WEB-INF/jsp/search-html.jsp Query String: limit=30&id=00157389&person=true&page=2&respub-action=search.html