5OQV
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NEAR-ATOMIC RESOLUTION FIBRIL STRUCTURE OF COMPLETE AMYLOID-BETA(1-42) BY CRYO-EM
Descriptor:Amyloid beta A4 protein
Authors:Gremer, L., Schoelzel, D., Schenk, C., Reinartz, E., Labahn, J., Ravelli, R., Tusche, M., Lopez-Iglesias, C., Hoyer, W., Heise, H., Willbold, D., Schroeder, G.F.
Deposit date:2017-08-14
Release date:2017-09-13
Last modified:2017-10-18
Method:ELECTRON MICROSCOPY (4 Å)
Cite:Fibril structure of amyloid-beta (1-42) by cryo-electron microscopy.
Science, 358, 2017
5KK3
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ATOMIC RESOLUTION STRUCTURE OF MONOMORPHIC AB42 AMYLOID FIBRILS
Descriptor:Beta-amyloid protein 42
Authors:Colvin, M.T., Silvers, R., Zhe Ni, Q., Can, T.V., Sergeyev, I., Rosay, M., Donovan, K.J., Michael, B., Wall, J., Linse, S., Griffin, R.G.
Deposit date:2016-06-20
Release date:2016-07-13
Last modified:2017-09-27
Method:SOLID-STATE NMR
Cite:Atomic Resolution Structure of Monomorphic A beta 42 Amyloid Fibrils.
J.Am.Chem.Soc., 138, 2016
2NAO
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ATOMIC RESOLUTION STRUCTURE OF A DISEASE-RELEVANT ABETA(1-42) AMYLOID FIBRIL
Descriptor:Beta-amyloid protein 42
Authors:Waelti, M.A., Ravotti, F., Arai, H., Glabe, C., Wall, J., Bockmann, A., Guntert, P., Meier, B.H., Riek, R.
Deposit date:2016-01-07
Release date:2016-07-27
Last modified:2016-09-07
Method:SOLUTION NMR
Cite:Atomic-resolution structure of a disease-relevant A beta (1-42) amyloid fibril.
Proc.Natl.Acad.Sci.USA, 113, 2016
2MXU
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42-RESIDUE BETA AMYLOID FIBRIL
Descriptor:Amyloid beta A4 protein
Authors:Xiao, Y., Ma, B., McElheny, D., Parthasarathy, S., Long, F., Hoshi, M., Nussinov, R., Ishii, Y.
Deposit date:2015-01-14
Release date:2015-05-06
Last modified:2015-06-17
Method:SOLID-STATE NMR
Cite:A beta (1-42) fibril structure illuminates self-recognition and replication of amyloid in Alzheimer's disease.
Nat.Struct.Mol.Biol., 22, 2015
2LP1
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THE SOLUTION NMR STRUCTURE OF THE TRANSMEMBRANE C-TERMINAL DOMAIN OF THE AMYLOID PRECURSOR PROTEIN (C99)
Descriptor:C99
Authors:Barrett, P.J., Song, Y., Van Horn, W.D., Hustedt, E.J., Schafer, J.M., Hadziselimovic, A., Beel, A.J., Sanders, C.R.
Deposit date:2012-01-30
Release date:2012-06-06
Last modified:2012-06-20
Method:SOLUTION NMR
Cite:The amyloid precursor protein has a flexible transmembrane domain and binds cholesterol.
Science, 336, 2012
2WK3
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CRYSTAL STRUCTURE OF HUMAN INSULIN-DEGRADING ENZYME IN COMPLEX WITH AMYLOID-BETA (1-42)
Descriptor:INSULIN DEGRADING ENZYME, BETA-AMYLOID PROTEIN 42, ZINC ION
Authors:Guo, Q., Tang, W.J.
Deposit date:2009-06-05
Release date:2009-11-03
Last modified:2011-07-13
Method:X-RAY DIFFRACTION (2.59 Å)
Cite:Molecular Basis for the Recognition and Cleavages of Igf-II, Tgf-Alpha, and Amylin by Human Insulin Degrading Enzyme.
J.Mol.Biol., 395, 2010
2BEG
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3D STRUCTURE OF ALZHEIMER'S ABETA(1-42) FIBRILS
Descriptor:Amyloid beta A4 protein
Authors:Luhrs, T., Ritter, C., Adrian, M., Riek-Loher, D., Bohrmann, B., Dobeli, H., Schubert, D., Riek, R.
Deposit date:2005-10-24
Release date:2005-11-22
Last modified:2011-07-13
Method:SOLUTION NMR
Cite:3D structure of Alzheimer's amyloid-{beta}(1-42) fibrils.
Proc.Natl.Acad.Sci.Usa, 102, 2005
1Z0Q
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AQUEOUS SOLUTION STRUCTURE OF THE ALZHEIMER'S DISEASE ABETA PEPTIDE (1-42)
Descriptor:Alzheimer's disease amyloid
Authors:Tomaselli, S., Esposito, V., Vangone, P., van Nuland, N.A., Bonvin, A.M., Guerrini, R., Tancredi, T., Temussi, P.A., Picone, D.
Deposit date:2005-03-02
Release date:2006-05-23
Last modified:2011-07-13
Method:SOLUTION NMR
Cite:The alpha-to-beta Conformational Transition of Alzheimer's Abeta-(1-42) Peptide in Aqueous Media is Reversible: A Step by Step Conformational Analysis Suggests the Location of beta Conformation Seeding
Chembiochem, 7, 2006
1IYT
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SOLUTION STRUCTURE OF THE ALZHEIMER'S DISEASE AMYLOID BETA-PEPTIDE (1-42)
Descriptor:Alzheimer's disease amyloid
Authors:Crescenzi, O., Tomaselli, S., Guerrini, R., Salvadori, S., D'Ursi, A.M., Temussi, P.A., Picone, D.
Deposit date:2002-09-06
Release date:2003-02-11
Last modified:2011-07-13
Method:SOLUTION NMR
Cite:Solution structure of the Alzheimer amyloid beta-peptide (1-42) in an apolar microenvironment. Similarity with a virus fusion domain.
EUR.J.BIOCHEM., 269, 2002
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