onr:"swepub:oai:DiVA.org:umu-42938"
Sökning: onr:"swepub:oai:DiVA.org:umu-42938" > A camelid antibody ...
- 1 av 1
- Föregående post
- Nästa post
- Till träfflistan
| Fältnamn | Indikatorer | Metadata |
|---|---|---|
| 000 | 02819naa a2200421 4500 | |
| 001 | oai:DiVA.org:umu-42938 | |
| 003 | SwePub | |
| 008 | 110414s2003 | |||||||||||000 ||eng| | |
| 024 | 7 | a https://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-429382 URI |
| 024 | 7 | a https://doi.org/10.1038/nature018702 DOI |
| 040 | a (SwePub)umu | |
| 041 | a engb eng | |
| 042 | 9 SwePub | |
| 072 | 7 | a ref2 swepub-contenttype |
| 072 | 7 | a art2 swepub-publicationtype |
| 100 | 1 | a Dumoulin, Mireille4 aut |
| 245 | 1 0 | a A camelid antibody fragment inhibits the formation of amyloid fibrils by human lysozyme. |
| 264 | 1 | b Springer Science and Business Media LLC,c 2003 |
| 338 | a print2 rdacarrier | |
| 520 | a Amyloid diseases are characterized by an aberrant assembly of a specific protein or protein fragment into fibrils and plaques that are deposited in various organs and tissues, often with serious pathological consequences. Non-neuropathic systemic amyloidosis is associated with single point mutations in the gene coding for human lysozyme. Here we report that a single-domain fragment of a camelid antibody raised against wild-type human lysozyme inhibits the in vitro aggregation of its amyloidogenic variant, D67H. Our structural studies reveal that the epitope includes neither the site of mutation nor most residues in the region of the protein structure that is destabilized by the mutation. Instead, the binding of the antibody fragment achieves its effect by restoring the structural cooperativity characteristic of the wild-type protein. This appears to occur at least in part through the transmission of long-range conformational effects to the interface between the two structural domains of the protein. Thus, reducing the ability of an amyloidogenic protein to form partly unfolded species can be an effective method of preventing its aggregation, suggesting approaches to the rational design of therapeutic agents directed against protein deposition diseases. | |
| 700 | 1 | a Last, Alexander M4 aut |
| 700 | 1 | a Desmyter, Aline4 aut |
| 700 | 1 | a Decanniere, Klaas4 aut |
| 700 | 1 | a Canet, Denis4 aut |
| 700 | 1 | a Larsson, Göran4 aut |
| 700 | 1 | a Spencer, Andrew4 aut |
| 700 | 1 | a Archer, David B4 aut |
| 700 | 1 | a Sasse, Jurgen4 aut |
| 700 | 1 | a Muyldermans, Serge4 aut |
| 700 | 1 | a Wyns, Lode4 aut |
| 700 | 1 | a Redfield, Christina4 aut |
| 700 | 1 | a Matagne, André4 aut |
| 700 | 1 | a Robinson, Carol V4 aut |
| 700 | 1 | a Dobson, Christopher M4 aut |
| 773 | 0 | t Natured : Springer Science and Business Media LLCg 424:6950, s. 783-8q 424:6950<783-8x 1476-4687x 0028-0836 |
| 856 | 4 | u https://orbi.uliege.be/bitstream/2268/16642/1/DumoulinNature2003.pdf |
| 856 | 4 8 | u https://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-42938 |
| 856 | 4 8 | u https://doi.org/10.1038/nature01870 |
- 1 av 1
- Föregående post
- Nästa post
- Till träfflistan
Hitta mer i SwePub
- Av författaren/redakt...
- Dumoulin, Mireil ...
- Last, Alexander ...
- Desmyter, Aline
- Decanniere, Klaa ...
- Canet, Denis
- Larsson, Göran
- visa fler...
- Spencer, Andrew
- Archer, David B
- Sasse, Jurgen
- Muyldermans, Ser ...
- Wyns, Lode
- Redfield, Christ ...
- Matagne, André
- Robinson, Carol ...
- Dobson, Christop ...
- visa färre...
- Artiklar i publikationen
- Nature
- Av lärosätet
- Umeå universitet
Sök utanför SwePub
- Sök vidare i:
- Google Book Search
- Google Scholar
Kungliga biblioteket hanterar dina personuppgifter i enlighet med EU:s dataskyddsförordning (2018), GDPR. Läs mer om hur det funkar här.
Så här hanterar KB dina uppgifter vid användning av denna tjänst.
- Copyright © LIBRIS - Nationella bibliotekssystem
- LIBRIS.kb.se
