Skip Header

1 - 25 of 29 results for author:"Harel M." in Literature citations

Page of 2 | Next »

to top of page·  

Results Customize

› Repeat search in UniProtKB (16)

The crystal structure of the alpha-neurexin-1 extracellular region reveals a hinge point for mediating synaptic adhesion and function.

Miller M.T., Mileni M., Comoletti D., Stevens R.C., Harel M., Taylor P.

Structure 19:767-778(2011) · UniProtKB (1)

The familial Mediterranean fever gene as a modifier of periodic fever, aphthous stomatitis, pharyngitis, and adenopathy syndrome.

Berkun Y., Levy R., Hurwitz A., Meir-Harel M., Lidar M., Livneh A., Padeh S.

Semin. Arthritis Rheum. 40:467-472(2011) · Mapped (6)

Acetylcholinesterase: from 3D structure to function.

Dvir H., Silman I., Harel M., Rosenberry T.L., Sussman J.L.

Chem. Biol. Interact. 187:10-22(2010) · Mapped (3)

Crystal structure of thioflavin T bound to the peripheral site of Torpedo californica acetylcholinesterase reveals how thioflavin T acts as a sensitive fluorescent reporter of ligand binding to the acylation site.

Harel M., Sonoda L.K., Silman I., Sussman J.L., Rosenberry T.L.

J. Am. Chem. Soc. 130:7856-7861(2008) · Mapped (1)

Atomic interactions of neonicotinoid agonists with AChBP: molecular recognition of the distinctive electronegative pharmacophore.

Talley T.T., Harel M., Hibbs R.E., Radic Z., Tomizawa M., Casida J.E., Taylor P.

Proc. Natl. Acad. Sci. U.S.A. 105:7606-7611(2008) · UniProtKB (1)

The crystal structure of the complex of the anticancer prodrug 7-ethyl-10-[4-(1-piperidino)-1-piperidino]-carbonyloxycamptothecin (CPT-11) with Torpedo californica acetylcholinesterase provides a molecular explanation for its cholinergic action.

Harel M., Hyatt J.L., Brumshtein B., Morton C.L., Yoon K.J., Wadkins R.M., Silman I., Sussman J.L., Potter P.M.

Mol. Pharmacol. 67:1874-1881(2005) · UniProtKB (1)

The synaptic acetylcholinesterase tetramer assembles around a polyproline II helix.

Dvir H., Harel M., Bon S., Liu W.-Q., Vidal M., Garbay C., Sussman J.L., Massoulie J., Silman I.

EMBO J. 23:4394-4405(2004) · UniProtKB (2)

Isolation of two aspartyl proteases from Trichoderma asperellum expressed during colonization of cucumber roots.

Viterbo A., Harel M., Chet I.

FEMS Microbiol. Lett. 238:151-158(2004) · UniProtKB (3)

Structure and evolution of the serum paraoxonase family of detoxifying and anti-atherosclerotic enzymes.

Harel M., Aharoni A., Gaidukov L., Brumshtein B., Khersonsky O., Meged R., Dvir H., Ravelli R.B.G., McCarthy A., Toker L. et al.

Nat. Struct. Mol. Biol. 11:412-419(2004) · UniProtKB (1)

X-ray structure of human acid-beta-glucosidase, the defective enzyme in Gaucher disease.

Dvir H., Harel M., McCarthy A.A., Toker L., Silman I., Futerman A.H., Sussman J.L.

EMBO Rep. 4:704-709(2003) · UniProtKB (1)

Structure of a complex of the potent and specific inhibitor BW284C51 with Torpedo californica acetylcholinesterase.

Felder C.E., Harel M., Silman I., Sussman J.L.

Acta Crystallogr. D Biol. Crystallogr. 58:1765-1771(2002) · Mapped (1)

A distinct family of acetylcholinesterases is secreted by Nippostrongylus brasiliensis.

Hussein A.S., Harel M., Selkirk M.E.

Mol. Biochem. Parasitol. 123:125-134(2002) · UniProtKB (1)

X-ray structures of Torpedo californica acetylcholinesterase complexed with (+)-huperzine A and (-)-huperzine B: structural evidence for an active site rearrangement.

Dvir H., Jiang H.L., Wong D.M., Harel M., Chetrit M., He X.C., Jin G.Y., Yu G.L., Tang X.C., Silman I. et al.

Biochemistry 41:10810-10818(2002) · Mapped (1)

Kinetic and structural studies on the interaction of cholinesterases with the anti-Alzheimer drug rivastigmine.

Bar-On P., Millard C.B., Harel M., Dvir H., Enz A., Sussman J.L., Silman I.

Biochemistry 41:3555-3564(2002) · UniProtKB (1) · Mapped (3)

3D structure of Torpedo californica acetylcholinesterase complexed with huprine X at 2.1 A resolution: kinetic and molecular dynamic correlates.

Dvir H., Wong D.M., Harel M., Barril X., Orozco M., Luque F.J., Munoz-Torrero D., Camps P., Rosenberry T.L., Silman I. et al.

Biochemistry 41:2970-2981(2002) · UniProtKB (1)

The binding site of acetylcholine receptor as visualized in the X-ray structure of a complex between alpha-bungarotoxin and a mimotope peptide.

Harel M., Kasher R., Nicolas A., Guss J.M., Balass M., Fridkin M., Smit A.B., Brejc K., Sixma T.K., Katchalski-Katzir E. et al.

Neuron 32:265-275(2001) · UniProtKB (1) · Mapped (1)

Structures of recombinant native and E202Q mutant human acetylcholinesterase complexed with the snake-venom toxin fasciculin-II.

Kryger G., Harel M., Giles K., Toker L., Velan B., Lazar A., Kronman C., Barak D., Ariel N., Shafferman A. et al.

Acta Crystallogr. D 56:1385-1394(2000) · UniProtKB (2) · Mapped (1)

Three-dimensional structures of Drosophila melanogaster acetylcholinesterase and of its complexes with two potent inhibitors.

Harel M., Kryger G., Rosenberry T.L., Mallender W.D., Lewis T., Fletcher R.J., Guss J.M., Silman I., Sussman J.L.

Protein Sci. 9:1063-1072(2000) · UniProtKB (1) · Mapped (2)

Specific chemical and structural damage to proteins produced by synchrotron radiation.

Weik M., Ravelli R.B., Kryger G., McSweeney S., Raves M.L., Harel M., Gros P., Silman I., Kroon J., Sussman J.L.

Proc. Natl. Acad. Sci. U.S.A. 97:623-628(2000) · Mapped (2)

Crystal structures of aged phosphonylated acetylcholinesterase: nerve agent reaction products at the atomic level.

Millard C.B., Kryger G., Ordentlich A., Greenblatt H.M., Harel M., Raves M.L., Segall Y., Barak D., Shafferman A., Silman I. et al.

Biochemistry 38:7032-7039(1999) · UniProtKB (1)

Structure of acetylcholinesterase complexed with the nootropic alkaloid, (-)-huperzine A.

Raves M.L., Harel M., Pang Y.P., Silman I., Kozikowski A.P., Sussman J.L.

Nat. Struct. Biol. 4:57-63(1997) · UniProtKB (1)

Crystal structure of an acetylcholinesterase-fasciculin complex: interaction of a three-fingered toxin from snake venom with its target.

Harel M., Kleywegt G.J., Ravelli R.B., Silman I., Sussman J.L.

Structure 3:1355-1366(1995) · UniProtKB (2)

Insights into protein adaptation to a saturated salt environment from the crystal structure of a halophilic 2Fe-2S ferredoxin.

Frolow F., Harel M., Sussman J.L., Mevarech M., Shoham M.

Nat. Struct. Biol. 3:452-458(1996) · UniProtKB (1)

Quaternary ligand binding to aromatic residues in the active-site gorge of acetylcholinesterase.

Harel M., Schalk I., Ehret-Sabatier L., Bouet F., Goeldner M., Hirth C., Axelsen P.H., Silman I., Sussman J.L.

Proc. Natl. Acad. Sci. U.S.A. 90:9031-9035(1993) · UniProtKB (1)

Structure and dynamics of the active site gorge of acetylcholinesterase: synergistic use of molecular dynamics simulation and X-ray crystallography.

Axelsen P.H., Harel M., Silman I., Sussman J.L.

Protein Sci. 3:188-197(1994) · Mapped (1)

to top of page·

Page of 2 | Next »