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  1. Article: X-ray diffraction studies of amyloid structure.

    Makin, O Sumner / Serpell, Louise C

    Methods in molecular biology (Clifton, N.J.)

    2005  Volume 299, Page(s) 67–80

    Abstract: Elucidation of the underlying core structure of amyloid fibrils is essential for understanding the mechanism by which amyloid fibrils are formed and deposited. Conventional methods of X-ray crystallography and NMR cannot be used, since the fibers are ... ...

    Abstract Elucidation of the underlying core structure of amyloid fibrils is essential for understanding the mechanism by which amyloid fibrils are formed and deposited. Conventional methods of X-ray crystallography and NMR cannot be used, since the fibers are insoluble and heterogeneous. X-ray fiber diffraction is one method that has been successfully used to examine the structure of these insoluble fibers. The procedure involves the formation of suitable, ordered amyloid fibrils and characterization (by electron microscopy), partial alignment of fibers, X-ray data collection, data analysis, and finally, model building.
    MeSH term(s) Amyloid/chemistry ; Amyloid/ultrastructure ; Animals ; Chemistry Techniques, Analytical/instrumentation ; Chemistry Techniques, Analytical/methods ; Humans ; Microscopy, Electron/methods ; X-Ray Diffraction/instrumentation ; X-Ray Diffraction/methods
    Chemical Substances Amyloid
    Language English
    Publishing date 2005-09-01
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 1064-3745
    ISSN 1064-3745
    DOI 10.1385/1-59259-874-9:067
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  2. Article: Structures for amyloid fibrils.

    Makin, O Sumner / Serpell, Louise C

    The FEBS journal

    2005  Volume 272, Issue 23, Page(s) 5950–5961

    Abstract: Alzheimer's disease and Creutzfeldt-Jakob disease are the best-known examples of a group of diseases known as the amyloidoses. They are characterized by the extracellular deposition of toxic, insoluble amyloid fibrils. Knowledge of the structure of these ...

    Abstract Alzheimer's disease and Creutzfeldt-Jakob disease are the best-known examples of a group of diseases known as the amyloidoses. They are characterized by the extracellular deposition of toxic, insoluble amyloid fibrils. Knowledge of the structure of these fibrils is essential for understanding the process of pathology of the amyloidoses and for the rational design of drugs to inhibit or reverse amyloid formation. Structural models have been built using information from a wide variety of techniques, including X-ray diffraction, electron microscopy, solid state NMR and EPR. Recent advances have been made in understanding the architecture of the amyloid fibril. Here, we describe and compare postulated structural models for the mature amyloid fibril and discuss how the ordered structure of amyloid contributes to its stability.
    MeSH term(s) Alzheimer Disease/metabolism ; Amyloid/chemistry ; Amyloid/ultrastructure ; Amyloidosis/metabolism ; Creutzfeldt-Jakob Syndrome/metabolism ; Humans ; Models, Molecular ; Molecular Structure ; Protein Conformation ; X-Ray Diffraction
    Chemical Substances Amyloid
    Language English
    Publishing date 2005-12
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2173655-8
    ISSN 1742-4658 ; 1742-464X
    ISSN (online) 1742-4658
    ISSN 1742-464X
    DOI 10.1111/j.1742-4658.2005.05025.x
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    In stock of ZB MED Cologne/Königswinter

    Zs.A 260: Show issues Location:
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  3. Article: Structural characterisation of islet amyloid polypeptide fibrils.

    Sumner Makin, O / Serpell, Louise C

    Journal of molecular biology

    2003  Volume 335, Issue 5, Page(s) 1279–1288

    Abstract: Islet amyloid is found in many patients suffering from type 2 diabetes. Amyloid fibrils found deposited in the pancreatic islets are composed of a 37-residue peptide, known as islet amyloid polypeptide (IAPP) (also known as amylin) and are similar to ... ...

    Abstract Islet amyloid is found in many patients suffering from type 2 diabetes. Amyloid fibrils found deposited in the pancreatic islets are composed of a 37-residue peptide, known as islet amyloid polypeptide (IAPP) (also known as amylin) and are similar to those found in other amyloid diseases. Synthetic IAPP peptide readily forms amyloid fibrils in vitro and this has allowed fibril formation kinetics and the overall morphology of IAPP amyloid to be studied. Here, we use X-ray fibre diffraction, electron microscopy and cryo-electron microscopy to examine the molecular structure of IAPP amyloid fibrils. X-ray diffraction from aligned synthetic amyloid fibrils gave a highly oriented diffraction pattern with layer-lines spaced 4.7 A apart. Electron diffraction also revealed the characteristic 4.7 A meridional signal and the position of the reflection could be compared directly to the image of the diffracting unit. Cryo-electron microscopy revealed the strong signal at 4.7 A that has been previously visualised from a single Abeta fibre. Together, these data build up a picture of how the IAPP fibril is held together by hydrogen bonded beta-sheet structure and contribute to the understanding of the generic structure of amyloid fibrils.
    MeSH term(s) Amyloid/chemistry ; Amyloid/ultrastructure ; Anti-Ulcer Agents/chemistry ; Diabetes Mellitus, Type 2/pathology ; Humans ; Hydrogen Bonding ; Islet Amyloid Polypeptide ; Islets of Langerhans/chemistry ; Islets of Langerhans/ultrastructure ; Microscopy, Electron ; Molecular Structure ; Peptide Fragments/chemistry ; Protein Structure, Secondary ; X-Ray Diffraction
    Chemical Substances Amyloid ; Anti-Ulcer Agents ; Islet Amyloid Polypeptide ; Peptide Fragments
    Language English
    Publishing date 2003-12-12
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 80229-3
    ISSN 1089-8638 ; 0022-2836
    ISSN (online) 1089-8638
    ISSN 0022-2836
    DOI 10.1016/j.jmb.2003.11.048
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    Zs.A 867: Show issues Location:
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  4. Article: Diffraction to study protein and peptide assemblies.

    Makin, O Sumner / Sikorski, Pawel / Serpell, Louise C

    Current opinion in chemical biology

    2006  Volume 10, Issue 5, Page(s) 417–422

    Abstract: Proteins and peptides are able to self-assemble in vivo and in vitro. In vitro, this ability can be exploited to make bionanomaterials with many potential uses. Peptides are capable of forming a wide range of structures including fibres, tubules and ... ...

    Abstract Proteins and peptides are able to self-assemble in vivo and in vitro. In vitro, this ability can be exploited to make bionanomaterials with many potential uses. Peptides are capable of forming a wide range of structures including fibres, tubules and scaffolds. In vivo, proteins assemble to form cellular fibrous proteins, as well as being involved in protein misfolding in disease. Recent advances using X-ray diffraction have highlighted the internal structure of self-assembled proteins and peptides, showing packing of side chain residues and have enabled a deeper understanding of mechanisms of assembly.
    MeSH term(s) Animals ; Humans ; Microscopy, Electron, Transmission ; Models, Molecular ; Particle Size ; Peptides/chemistry ; Protein Structure, Secondary ; Proteins/chemistry ; Sensitivity and Specificity ; X-Ray Diffraction
    Chemical Substances Peptides ; Proteins
    Language English
    Publishing date 2006-10
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 1439176-4
    ISSN 1879-0402 ; 1367-5931
    ISSN (online) 1879-0402
    ISSN 1367-5931
    DOI 10.1016/j.cbpa.2006.08.009
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    Zs.A 4986: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
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  5. Article: A simple algorithm locates beta-strands in the amyloid fibril core of alpha-synuclein, Abeta, and tau using the amino acid sequence alone.

    Zibaee, Shahin / Makin, O Sumner / Goedert, Michel / Serpell, Louise C

    Protein science : a publication of the Protein Society

    2007  Volume 16, Issue 5, Page(s) 906–918

    Abstract: Fibrillar inclusions are a characteristic feature of the neuropathology found in the alpha-synucleinopathies such as Parkinson's disease, dementia with Lewy bodies, and multiple system atrophy. Familial forms of alpha-synucleinopathies have also been ... ...

    Abstract Fibrillar inclusions are a characteristic feature of the neuropathology found in the alpha-synucleinopathies such as Parkinson's disease, dementia with Lewy bodies, and multiple system atrophy. Familial forms of alpha-synucleinopathies have also been linked with missense mutations or gene multiplications that result in higher protein expression levels. In order to form these fibrils, the protein, alpha-synuclein (alpha-syn), must undergo a process of self-assembly in which its native state is converted from a disordered conformer into a beta-sheet-dominated form. Here, we have developed a novel polypeptide property calculator to locate and quantify relative propensities for beta-strand structure in the sequence of alpha-syn. The output of the algorithm, in the form of a simple x-y plot, was found to correlate very well with the location of the beta-sheet core in alpha-syn fibrils. In particular, the plot features three peaks, the largest of which is completely absent for the nonfibrillogenic protein, beta-syn. We also report similar significant correlations for the Alzheimer's disease-related proteins, Abeta and tau. A substantial region of alpha-syn is capable [corrected] of converting from its disordered conformation into a long [corrected] alpha-helical protein. We have developed the aforementioned algorithm to locate and quantify the alpha-helical hydrophobic moment in the amino acid sequence of alpha-syn. As before, the output of the algorithm, in the form of a simple x-y plot, was found to correlate very well with the location of alpha-helical structure in membrane bilayer-associated alpha-syn.
    MeSH term(s) Algorithms ; Amyloid/chemistry ; Amyloid beta-Peptides/chemistry ; Protein Structure, Secondary ; alpha-Synuclein/chemistry ; beta-Synuclein/chemistry ; tau Proteins/chemistry
    Chemical Substances Amyloid ; Amyloid beta-Peptides ; alpha-Synuclein ; beta-Synuclein ; tau Proteins
    Language English
    Publishing date 2007-04-24
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1106283-6
    ISSN 1469-896X ; 0961-8368
    ISSN (online) 1469-896X
    ISSN 0961-8368
    DOI 10.1110/ps.062624507
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    Zs.A 3407: Show issues Location:
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    Zs.MO 1: Show issues

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  6. Article: Molecular basis for amyloid fibril formation and stability.

    Makin, O Sumner / Atkins, Edward / Sikorski, Pawel / Johansson, Jan / Serpell, Louise C

    Proceedings of the National Academy of Sciences of the United States of America

    2005  Volume 102, Issue 2, Page(s) 315–320

    Abstract: The molecular structure of the amyloid fibril has remained elusive because of the difficulty of growing well diffracting crystals. By using a sequence-designed polypeptide, we have produced crystals of an amyloid fiber. These crystals diffract to high ... ...

    Abstract The molecular structure of the amyloid fibril has remained elusive because of the difficulty of growing well diffracting crystals. By using a sequence-designed polypeptide, we have produced crystals of an amyloid fiber. These crystals diffract to high resolution (1 A) by electron and x-ray diffraction, enabling us to determine a detailed structure for amyloid. The structure reveals that the polypeptides form fibrous crystals composed of antiparallel beta-sheets in a cross-beta arrangement, characteristic of all amyloid fibers, and allows us to determine the side-chain packing within an amyloid fiber. The antiparallel beta-sheets are zipped together by means of pi-bonding between adjacent phenylalanine rings and salt-bridges between charge pairs (glutamic acid-lysine), thus controlling and stabilizing the structure. These interactions are likely to be important in the formation and stability of other amyloid fibrils.
    MeSH term(s) Amyloid/chemistry ; Crystallization ; Microscopy, Electron ; Protein Structure, Secondary ; X-Ray Diffraction
    Chemical Substances Amyloid
    Language English
    Publishing date 2005-01-03
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    DOI 10.1073/pnas.0406847102
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    Zs.A 1148: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
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  7. Article ; Online: The common architecture of cross-beta amyloid.

    Jahn, Thomas R / Makin, O Sumner / Morris, Kyle L / Marshall, Karen E / Tian, Pei / Sikorski, Pawel / Serpell, Louise C

    Journal of molecular biology

    2009  Volume 395, Issue 4, Page(s) 717–727

    Abstract: Amyloid fibril deposition is central to the pathology of more than 30 unrelated diseases including Alzheimer's disease and Type 2 diabetes. It is generally accepted that amyloid fibrils share common structural features despite each disease being ... ...

    Abstract Amyloid fibril deposition is central to the pathology of more than 30 unrelated diseases including Alzheimer's disease and Type 2 diabetes. It is generally accepted that amyloid fibrils share common structural features despite each disease being characterised by the deposition of an unrelated protein or peptide. The structure of amyloid fibrils has been studied using X-ray fibre diffraction and crystallography, solid-state NMR and electron paramagnetic resonance, and many different, sometimes opposing, models have been suggested. Many of these models are based on the original interpretation of the cross-beta diffraction pattern for cross-beta silk in which beta-strands run perpendicular to the fibre axis, although alternative models include beta-helices and natively structured proteins. Here, we have analysed opposing model structures and examined the necessary structural elements within the amyloid core structure, as well as producing idealised models to test the limits of the core conformation. Our work supports the view that amyloid fibrils share a number of common structural features, resulting in characteristic diffraction patterns. This pattern may be satisfied by structures in which the strands align close to perpendicular to the fibre axis and are regularly arranged to form beta-sheet ribbons. Furthermore, the fibril structure contains several beta-sheets that associate via side-chain packing to form the final protofilament structure.
    MeSH term(s) Amino Acid Sequence ; Amyloid/chemistry ; Amyloid/genetics ; Amyloid beta-Peptides/chemistry ; Amyloid beta-Peptides/genetics ; Humans ; In Vitro Techniques ; Models, Molecular ; Peptide Fragments/chemistry ; Peptide Fragments/genetics ; Protein Conformation ; Protein Structure, Secondary ; X-Ray Diffraction
    Chemical Substances Amyloid ; Amyloid beta-Peptides ; Peptide Fragments
    Language English
    Publishing date 2009-09-23
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 80229-3
    ISSN 1089-8638 ; 0022-2836
    ISSN (online) 1089-8638
    ISSN 0022-2836
    DOI 10.1016/j.jmb.2009.09.039
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    Zs.A 867: Show issues Location:
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