| Home > Publications Database > Investigating fibrillar aggregates of Tau protein by atomic force microscopy. > print |
| 001 | 141184 | ||
| 005 | 20250415112942.0 | ||
| 020 | _ | _ | |a 978-1-61779-550-3 (print) |
| 020 | _ | _ | |a 978-1-61779-551-0 (electronic) |
| 024 | 7 | _ | |a 10.1007/978-1-61779-551-0_12 |2 doi |
| 024 | 7 | _ | |a pmid:22528090 |2 pmid |
| 024 | 7 | _ | |a 1064-3745 |2 ISSN |
| 024 | 7 | _ | |a 1940-6029 |2 ISSN |
| 037 | _ | _ | |a DZNE-2020-07506 |
| 041 | _ | _ | |a English |
| 082 | _ | _ | |a 570 |
| 100 | 1 | _ | |a Wegmann, Susanne |0 P:(DE-2719)2812695 |b 0 |u dzne |
| 245 | _ | _ | |a Investigating fibrillar aggregates of Tau protein by atomic force microscopy. |
| 260 | _ | _ | |a [Heidelberg] |c 2012 |b [Springer] |
| 264 | _ | 1 | |3 online |2 Crossref |b Humana Press |c 2012-01-09 |
| 264 | _ | 1 | |3 print |2 Crossref |b Humana Press |c 2012-01-01 |
| 295 | 1 | 0 | |a Amyloid Proteins / Sigurdsson, Einar M. (Editor) ; Totowa, NJ : Humana Press, 2012, Chapter 12 ; ISSN: 1064-3745=1940-6029 ; ISBN: 978-1-61779-550-3=978-1-61779-551-0 ; doi:10.1007/978-1-61779-551-0 |
| 300 | _ | _ | |a 169 - 183 |
| 336 | 7 | _ | |a article |2 DRIVER |
| 336 | 7 | _ | |a Output Types/Journal article |2 DataCite |
| 336 | 7 | _ | |a Book |0 PUB:(DE-HGF)3 |2 PUB:(DE-HGF) |m book |
| 336 | 7 | _ | |a Journal Article |b journal |m journal |0 PUB:(DE-HGF)16 |s 1744709304_6736 |2 PUB:(DE-HGF) |
| 336 | 7 | _ | |a ARTICLE |2 BibTeX |
| 336 | 7 | _ | |a JOURNAL_ARTICLE |2 ORCID |
| 336 | 7 | _ | |a Journal Article |0 0 |2 EndNote |
| 490 | 0 | _ | |a Methods in Molecular Biology |v 849 |
| 520 | _ | _ | |a Atomic force microscopy (AFM) has been used in numerous studies to visualize and analyze the structure and conformation of biological samples, from single molecules to biopolymers to cells. The possibility to analyze native samples without fixation, staining and in physiological buffer conditions, combined with the sub-nanometer resolution, makes AFM a versatile tool for the analysis of protein aggregation and amyloid structures. Here, we describe the application of AFM to study fibrillar Tau protein aggregates. |
| 536 | _ | _ | |a 342 - Disease Mechanisms and Model Systems (POF3-342) |0 G:(DE-HGF)POF3-342 |c POF3-342 |f POF III |x 0 |
| 588 | _ | _ | |a Dataset connected to CrossRef Book Series, PubMed, |
| 650 | _ | 7 | |a Aluminum Silicates |2 NLM Chemicals |
| 650 | _ | 7 | |a tau Proteins |2 NLM Chemicals |
| 650 | _ | 7 | |a Glutaral |0 T3C89M417N |2 NLM Chemicals |
| 650 | _ | 7 | |a mica |0 V8A1AW0880 |2 NLM Chemicals |
| 650 | _ | 2 | |a Adsorption |2 MeSH |
| 650 | _ | 2 | |a Aluminum Silicates: chemistry |2 MeSH |
| 650 | _ | 2 | |a Glutaral: chemistry |2 MeSH |
| 650 | _ | 2 | |a Humans |2 MeSH |
| 650 | _ | 2 | |a Microscopy, Atomic Force: methods |2 MeSH |
| 650 | _ | 2 | |a Protein Multimerization |2 MeSH |
| 650 | _ | 2 | |a Protein Structure, Secondary |2 MeSH |
| 650 | _ | 2 | |a Surface Properties |2 MeSH |
| 650 | _ | 2 | |a Time Factors |2 MeSH |
| 650 | _ | 2 | |a tau Proteins: chemistry |2 MeSH |
| 700 | 1 | _ | |a Muller, Daniel J |0 P:(DE-HGF)0 |b 1 |
| 700 | 1 | _ | |a Mandelkow, Eckhard |0 P:(DE-2719)2541671 |b 2 |e Last author |
| 773 | 1 | 8 | |a 10.1007/978-1-61779-551-0_12 |b : Humana Press, 2012-01-01 |p 169-183 |3 book-chapter |2 Crossref |t Methods in Molecular Biology |y 2012 |x 1064-3745 |
| 773 | _ | _ | |a 10.1007/978-1-61779-551-0_12 |0 PERI:(DE-600)2493551-7 |p 169-183 |t Methods in molecular biology |v 849 |y 2012 |x 1064-3745 |
| 856 | 4 | _ | |u https://pub.dzne.de/record/141184/files/DZNE-2020-07506_Restricted.pdf |
| 856 | 4 | _ | |u https://pub.dzne.de/record/141184/files/DZNE-2020-07506_Restricted.pdf?subformat=pdfa |x pdfa |
| 909 | C | O | |p VDB |o oai:pub.dzne.de:141184 |
| 910 | 1 | _ | |a External Institute |0 I:(DE-HGF)0 |k Extern |b 0 |6 P:(DE-2719)2812695 |
| 910 | 1 | _ | |a Deutsches Zentrum für Neurodegenerative Erkrankungen |0 I:(DE-588)1065079516 |k DZNE |b 2 |6 P:(DE-2719)2541671 |
| 913 | 1 | _ | |a DE-HGF |b Gesundheit |l Erkrankungen des Nervensystems |1 G:(DE-HGF)POF3-340 |0 G:(DE-HGF)POF3-342 |3 G:(DE-HGF)POF3 |2 G:(DE-HGF)POF3-300 |4 G:(DE-HGF)POF |v Disease Mechanisms and Model Systems |x 0 |
| 914 | 1 | _ | |y 2012 |
| 915 | _ | _ | |a DBCoverage |0 StatID:(DE-HGF)0300 |2 StatID |b Medline |d 2020-01-17 |
| 915 | _ | _ | |a DBCoverage |0 StatID:(DE-HGF)0310 |2 StatID |b NCBI Molecular Biology Database |d 2020-01-17 |
| 915 | _ | _ | |a DBCoverage |0 StatID:(DE-HGF)0200 |2 StatID |b SCOPUS |d 2020-01-17 |
| 920 | 1 | _ | |0 I:(DE-2719)1013014 |k AG (Eckhard) Mandelkow |l Structural Principles of Neurodegeneration |x 0 |
| 980 | _ | _ | |a journal |
| 980 | _ | _ | |a VDB |
| 980 | _ | _ | |a book |
| 980 | _ | _ | |a I:(DE-2719)1013014 |
| 980 | _ | _ | |a UNRESTRICTED |
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