Relevant bibliographies by topics / Interactions peptides amyloides

Contents

  1. Journal articles
  2. Dissertations / Theses
  3. Book chapters
  4. Conference papers

Academic literature on the topic 'Interactions peptides amyloides'

Author: Grafiati
Published: 4 June 2021
Last updated: 10 February 2022

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Consult the lists of relevant articles, books, theses, conference reports, and other scholarly sources on the topic 'Interactions peptides amyloides.'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Journal articles on the topic "Interactions peptides amyloides"

1

Yang, Yanlian, and Chen Wang. "Single-molecule studies on individual peptides and peptide assemblies on surfaces." Philosophical Transactions of the Royal Society A: Mathematical, Physical and Engineering Sciences 371, no. 2000 (2013): 20120311. http://dx.doi.org/10.1098/rsta.2012.0311.

Full text
Abstract:
This review is intended to reflect the recent progress in single-molecule studies of individual peptides and peptide assemblies on surfaces. The structures and the mechanism of peptide assembly are discussed in detail. The contents include the following topics: structural analysis of single peptide molecules, adsorption and assembly of peptides on surfaces, folding structures of the amyloid peptides, interaction between amyloid peptides and dye or drug molecules, and modulation of peptide assemblies by small molecules. The explorations of peptide adsorption and assembly will benefit the unders
APA, Harvard, Vancouver, ISO, and other styles
2

TOMIYAMA, Takami, Hideshi KANEKO, Ken-ichiro KATAOKA, Satoshi ASANO, and Noriaki ENDO. "Rifampicin inhibits the toxicity of pre-aggregated amyloid peptides by binding to peptide fibrils and preventing amyloid-cell interaction." Biochemical Journal 322, no. 3 (1997): 859–65. http://dx.doi.org/10.1042/bj3220859.

Full text
Abstract:
Rifampicin and its analogues,p-benzoquinone and hydroquinone, inhibited the toxicity of preformed aggregates of human islet amyloid polypeptide, amylin, to rat pheochromocytoma PC12 cells, when preincubated with the aggregated peptide before addition to cell cultures. Immunofluorescence microscopy showed that they prevented the adhesion of amylin aggregates to the cell surface, and this effect was induced probably by their binding to peptide fibrils during preincubation. Other quinone derivatives, i.e., p-methoxyphenol, AA-861 and idebenone, failed to inhibit the toxicity and cell-surface adhe
APA, Harvard, Vancouver, ISO, and other styles
3

Ciccone, Lidia, Chenghui Shi, Davide di Lorenzo, Anne-Cécile Van Baelen та Nicolo Tonali. "The Positive Side of the Alzheimer’s Disease Amyloid Cross-Interactions: The Case of the Aβ 1-42 Peptide with Tau, TTR, CysC, and ApoA1". Molecules 25, № 10 (2020): 2439. http://dx.doi.org/10.3390/molecules25102439.

Full text
Abstract:
Alzheimer’s disease (AD) represents a progressive amyloidogenic disorder whose advancement is widely recognized to be connected to amyloid-β peptides and Tau aggregation. However, several other processes likely contribute to the development of AD and some of them might be related to protein-protein interactions. Amyloid aggregates usually contain not only single type of amyloid protein, but also other type of proteins and this phenomenon can be rationally explained by the process of protein cross-seeding and co-assembly. Amyloid cross-interaction is ubiquitous in amyloid fibril formation and s
APA, Harvard, Vancouver, ISO, and other styles
4

Roth, Aileen, Fabian Gärtner, Katja Mayer та ін. "CK1δ-Derived Peptides as Novel Tools Inhibiting the Interactions between CK1δ and APP695 to Modulate the Pathogenic Metabolism of APP". International Journal of Molecular Sciences 22, № 12 (2021): 6423. http://dx.doi.org/10.3390/ijms22126423.

Full text
Abstract:
Alzheimer’s disease (AD) is the major cause of dementia, and affected individuals suffer from severe cognitive, mental, and functional impairment. Histologically, AD brains are basically characterized by the presence of amyloid plaques and neurofibrillary tangles. Previous reports demonstrated that protein kinase CK1δ influences the metabolism of amyloid precursor protein (APP) by inducing the generation of amyloid-β (Aβ), finally contributing to the formation of amyloid plaques and neuronal cell death. We therefore considered CK1δ as a promising therapeutic target and suggested an innovative
APA, Harvard, Vancouver, ISO, and other styles
5

Mishra, Rahul, and Ashwani K. Thakur. "Amyloid nanospheres from polyglutamine rich peptides: assemblage through an intermolecular salt bridge interaction." Organic & Biomolecular Chemistry 13, no. 14 (2015): 4155–59. http://dx.doi.org/10.1039/c4ob02589j.

Full text
Abstract:
Amyloid fiber formation by two polyglutamine peptides through a nucleation polymerization pathway. An intermolecular salt bridge between the positively charged lysine and the negatively charged glutamate induces the formation of nanospherical amyloids through a non-nucleated pathway.
APA, Harvard, Vancouver, ISO, and other styles
6

Rapsinski, Glenn J., Tiffanny N. Newman, Gertrude O. Oppong, Jos P. M. van Putten, and Çagla Tükel. "CD14 Protein Acts as an Adaptor Molecule for the Immune Recognition of Salmonella Curli Fibers." Journal of Biological Chemistry 288, no. 20 (2013): 14178–88. http://dx.doi.org/10.1074/jbc.m112.447060.

Full text
Abstract:
Amyloids, protein aggregates with a cross β-sheet structure, contribute to inflammation in debilitating disorders, including Alzheimer's disease. Enteric bacteria also produce amyloids, termed curli, contributing to inflammation during infection. It has been demonstrated that curli and β-amyloid are recognized by the immune system via the Toll-like receptor (TLR) 2/TLR1 complex. Here we investigated the role of CD14 in the immune recognition of bacterial amyloids. We used HeLa 57A cells, a human cervical cancer cell line containing a luciferase reporter gene under the control of an NF-κB promo
APA, Harvard, Vancouver, ISO, and other styles
7

Sharoyan, Svetlana, Alvard Antonyan, Sona Mardanyan, et al. "Interaction of dipeptydil peptidase IV with amyloid peptides." Neurochemistry International 62, no. 8 (2013): 1048–54. http://dx.doi.org/10.1016/j.neuint.2013.03.017.

Full text
APA, Harvard, Vancouver, ISO, and other styles
8

Wang, Lan, Qian Liu, Jin-Chun Chen, et al. "Antimicrobial activity of human islet amyloid polypeptides: an insight into amyloid peptides’ connection with antimicrobial peptides." Biological Chemistry 393, no. 7 (2012): 641–46. http://dx.doi.org/10.1515/hsz-2012-0107.

Full text
Abstract:
Abstract Human islet amyloid polypeptide (hIAPP) shows an antimicrobial activity towards two types of clinically relevant bacteria. The potency of hIAPP varies with its aggregation states. Circular dichroism was employed to determine the interaction between hIAPP and bacteria lipid membrane mimic. The antimicrobial activity of each aggregate species is associated with their ability to induce membrane disruption. Our findings provide new evidence revealing the antimicrobial activity of amyloid peptide, which suggest a possible connection between amyloid peptides and antimicrobial peptides.
APA, Harvard, Vancouver, ISO, and other styles
9

Buneeva, O. A., O. V. Gnedenko, M. V. Medvedeva, A. S. Ivanov, and A. E. Medvedev. "The effect of neuroprotector isatin on binding of some model proteins with beta-amyloid peptide: a biosensor study." Biomeditsinskaya Khimiya 62, no. 6 (2016): 720–24. http://dx.doi.org/10.18097/pbmc20166206720.

Full text
Abstract:
The amyloid-beta peptide 1-42 formed during proteolytic processing of the amyloid precursor protein (APP) plays a key role in the development or progression of Alzheimer's disease (AD) and other pathologies associated with formation of protein aggregates in the central nervous system. Recent proteomic profiling of mouse and rat brain preparations by means of beta-amyloid peptide immobilized on Affigel-10 revealed a large group of amyloid-binding proteins (n>80). Many (about 25%) of these proteins were previously identified as isatin-binding proteins. The aim of this study was to validate di
APA, Harvard, Vancouver, ISO, and other styles
10

Chatani, Eri, Keisuke Yuzu, Yumiko Ohhashi, and Yuji Goto. "Current Understanding of the Structure, Stability and Dynamic Properties of Amyloid Fibrils." International Journal of Molecular Sciences 22, no. 9 (2021): 4349. http://dx.doi.org/10.3390/ijms22094349.

Full text
Abstract:
Amyloid fibrils are supramolecular protein assemblies represented by a cross-β structure and fibrous morphology, whose structural architecture has been previously investigated. While amyloid fibrils are basically a main-chain-dominated structure consisting of a backbone of hydrogen bonds, side-chain interactions also play an important role in determining their detailed structures and physicochemical properties. In amyloid fibrils comprising short peptide segments, a steric zipper where a pair of β-sheets with side chains interdigitate tightly is found as a fundamental motif. In amyloid fibrils
APA, Harvard, Vancouver, ISO, and other styles
More sources

Dissertations / Theses on the topic "Interactions peptides amyloides"

1

Lambert, Eléonore. "Apports de la Microscopie à Force Atomique à l’étude de phénomènes dynamiques en biologie et développement instrumental associé." Thesis, Reims, 2018. http://www.theses.fr/2018REIMS014/document.

Full text
Abstract:
Le Laboratoire de Recherche en Nanosciences EA 4682 s’est récemment équipé de la microscopie à force atomique haute-vitesse (HS-AFM) permettant la visualisation en temps réel des dynamiques d’interactions d’un panel infini d’échantillons biologiques à l’échelle nanométrique. De nombreux champ de recherche nécessite la mise au point de techniques permettant à la fois une imagerie dynamique (vidéomicroscopie) mais également de plus en plus une imagerie haute résolution (microscopie champ proche). Ce couplage a été récemment obtenu grâce au développement de la microscopie à force atomique ultra-r
APA, Harvard, Vancouver, ISO, and other styles
2

Hornshaw, Martin P. "Peptide metal ion interactions in cerebral amyloidoses." Thesis, University of Newcastle Upon Tyne, 1995. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.260931.

Full text
APA, Harvard, Vancouver, ISO, and other styles
3

Chouchane, Karim. "Contrôler l'agrégation de l'insuline à la surface des matériaux via des interactions avec des peptides et la lumière." Thesis, Université Grenoble Alpes (ComUE), 2017. http://www.theses.fr/2017GREAY072/document.

Full text
Abstract:
Le repliement et la stabilité des protéines dépendent des conditions physico-chimiques de leur environnement. En particulier, le pH, la température, l’agitation et les interactions avec d’autres macromolécules ou avec les interfaces (liquide–surfaces des matériaux ; air-liquide ; etc.) sont connues pour induire des phénomènes de dénaturation et d’agrégation des protéines.Le contrôle de la stabilité des protéines thérapeutiques représente un enjeu médical et économique pour l’industrie pharmaceutique. L’insuline, qui est la protéine thérapeutique la plus produite, est connue in vitro pour forme
APA, Harvard, Vancouver, ISO, and other styles
4

Bell, Leonard Gerald. "Interactions between #beta#-amyloid peptide and metal ions in amyloid formation." Thesis, University of Sunderland, 1996. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.337181.

Full text
APA, Harvard, Vancouver, ISO, and other styles
5

Zhang, Mingzhen. "Multiscale Molecular Simulations of Cross-sequence Interactions between Amyloid Peptides." University of Akron / OhioLINK, 2017. http://rave.ohiolink.edu/etdc/view?acc_num=akron1490711960550386.

Full text
APA, Harvard, Vancouver, ISO, and other styles
6

Ma, Xin. "The interaction between amyloid beta peptide and phospholipids." Thesis, University of Edinburgh, 2015. http://hdl.handle.net/1842/29637.

Full text
Abstract:
The aim of the thesis project was to examine what form(s) of Amyloid beta (Aβ) (25-­‐35) peptide interact with phospholipids in vitro and the implications of this for the mechanism of Alzheimer’s Diseases (AD). The mechanism of AD is thought to involve protein folding and misfolding. An increasing amount of evidence has shown that protein misfolding plays an important role in the biological and pathological processes of AD. Although seen as the biomedical markers of those diseases, the roles of amyloid aggregates themselves are still not fully understood. Whether the aggregates, or the monomer
APA, Harvard, Vancouver, ISO, and other styles
7

Widenbrant, Martin Johan Olof. "Investigation of amyloid-beta peptide interactions with membrane lipids /." May be available electronically:, 2007. http://proquest.umi.com/login?COPT=REJTPTU1MTUmSU5UPTAmVkVSPTI=&clientId=12498.

Full text
APA, Harvard, Vancouver, ISO, and other styles
8

Turner, Matthew. "Modelling platinum(II) interactions with the Amyloid-b peptide." Thesis, Cardiff University, 2018. http://orca.cf.ac.uk/109924/.

Full text
Abstract:
The Ab peptide is a key molecule in the development of Alzheimer’s Disease - Ab peptides form toxic aggregates in the brain. Density functional theory (DFT), Parametric Model 7 (PM7) and ligand-Field Molecular Mechanics (LFMM) methods have been used to model the interactions of a series of potential therapeutic PtII(ligand) complexes with various fragments of the Ab peptide. LFMM calculations with the AMBER forcefield were used to generate conformations of PtII-Ab6-14 via LowMode MD and results validated against BHandH. While LFMM showed insufficient agreement with DFT, the semi-empirical PM7
APA, Harvard, Vancouver, ISO, and other styles
9

Kamaloo, Elaheh. "Supported lipid bilayer interactions with nanoparticles, peptides and polymers." Digital WPI, 2018. https://digitalcommons.wpi.edu/etd-dissertations/38.

Full text
Abstract:
Supported lipid bilayers (SLBs) are one of the most common model membranes used in the field of cell membrane biology as they provide a well-defined model membrane platform for determination of molecular-level interactions between different biomolecules (e.g. proteins, peptides) and lipid membrane. Compared to model organisms, the use of SLB is preferable since it mimics cell plasma membrane in a very simple and well-controlled way. Therefore, molecular structure of membrane and experimental conditions (e.g. solution chemistry, temperature, and pH) can be easily adjusted to the required condi
APA, Harvard, Vancouver, ISO, and other styles
10

Senyah, Nancy Akosuah. "The interactions of Alzheimer's amyloid peptides with artificial and biological membranes." Thesis, University of Essex, 1999. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.284610.

Full text
APA, Harvard, Vancouver, ISO, and other styles
More sources

Book chapters on the topic "Interactions peptides amyloides"

1

Tooyama, Ikuo. "Interactions of α2-macroglobulin and amyloid β peptide." In Neuroinflammatory Mechanisms in Alzheimer’s Disease Basic and Clinical Research. Birkhäuser Basel, 2001. http://dx.doi.org/10.1007/978-3-0348-8350-4_7.

Full text
APA, Harvard, Vancouver, ISO, and other styles
2

Malishev, Ravit, Sofiya Kolusheva, and Raz Jelinek. "Vesicle-Based Assays to Study Membrane Interactions of Amyloid Peptides." In Methods in Molecular Biology. Springer New York, 2018. http://dx.doi.org/10.1007/978-1-4939-8820-4_3.

Full text
APA, Harvard, Vancouver, ISO, and other styles
3

Webster, Scott D. "Amyloid β peptide interactions with the classical pathway of complement." In Neuroinflammatory Mechanisms in Alzheimer’s Disease Basic and Clinical Research. Birkhäuser Basel, 2001. http://dx.doi.org/10.1007/978-3-0348-8350-4_5.

Full text
APA, Harvard, Vancouver, ISO, and other styles
4

Bateman, David A., and Avijit Chakrabartty. "Interaction of Alzheimer Amyloid Peptide with Cell Surfaces and Artificial Membranes." In Lipids and Cellular Membranes in Amyloid Diseases. Wiley-VCH Verlag GmbH & Co. KGaA, 2011. http://dx.doi.org/10.1002/9783527634323.ch11.

Full text
APA, Harvard, Vancouver, ISO, and other styles
5

Gröbner, Gerhard, Clemens Glaubitz, Philip T. F. Williamson, Timothy Hadingham, and Anthony Watts. "Structural insight into the interaction of amyloid-β peptide with biological membranes by solid state NMR." In Focus on Structural Biology. Springer Netherlands, 2001. http://dx.doi.org/10.1007/978-94-017-2579-8_18.

Full text
APA, Harvard, Vancouver, ISO, and other styles
6

Sonawane, Kailas Dashrath, and Maruti Jayram Dhanavade. "Molecular Docking Technique to Understand Enzyme-Ligand Interactions." In Methods and Algorithms for Molecular Docking-Based Drug Design and Discovery. IGI Global, 2016. http://dx.doi.org/10.4018/978-1-5225-0115-2.ch010.

Full text
Abstract:
Molecular docking has advanced to such an extent that one can rapidly and accurately identify pharmaceutically useful lead compounds. It is being used routinely to understand molecular interactions between enzyme and ligand molecules. Several computational approaches are combined with experimental work to investigate molecular mechanisms in detail at the atomic level. Molecular docking method is also useful to investigate proper orientation and interactions between receptor and ligand. In this chapter we have discussed protein-protein approach to understand interactions between enzyme and amyloid beta (Aß) peptide. The Aß peptide is a causative agent of Alzheimer's disease. The Aß peptides can be cleaved specifically by several enzymes. Their interactions with Aß peptide and specific enzyme can be investigated using molecular docking. Thus, the molecular information obtained from docking studies might be useful to design new therapeutic approaches in treatment of Alzheimer's as well as several other diseases.
APA, Harvard, Vancouver, ISO, and other styles
7

Sonawane, Kailas Dashrath, and Maruti Jayram Dhanavade. "Molecular Docking Technique to Understand Enzyme-Ligand Interactions." In Pharmaceutical Sciences. IGI Global, 2017. http://dx.doi.org/10.4018/978-1-5225-1762-7.ch028.

Full text
Abstract:
Molecular docking has advanced to such an extent that one can rapidly and accurately identify pharmaceutically useful lead compounds. It is being used routinely to understand molecular interactions between enzyme and ligand molecules. Several computational approaches are combined with experimental work to investigate molecular mechanisms in detail at the atomic level. Molecular docking method is also useful to investigate proper orientation and interactions between receptor and ligand. In this chapter we have discussed protein-protein approach to understand interactions between enzyme and amyloid beta (Aß) peptide. The Aß peptide is a causative agent of Alzheimer's disease. The Aß peptides can be cleaved specifically by several enzymes. Their interactions with Aß peptide and specific enzyme can be investigated using molecular docking. Thus, the molecular information obtained from docking studies might be useful to design new therapeutic approaches in treatment of Alzheimer's as well as several other diseases.
APA, Harvard, Vancouver, ISO, and other styles
8

Díaz, Mario, and Raquel Marin. "Lipid Rafts and Development of Alzheimer’s Disease." In Cerebral and Cerebellar Cortex – Interaction and Dynamics in Health and Disease. IntechOpen, 2021. http://dx.doi.org/10.5772/intechopen.94608.

Full text
Abstract:
A wealth of evidence accumulated over the last two decades has unambiguously linked lipid rafts to neurodegenerative diseases, in particular to Alzheimer’s disease (AD). These microdomains are highly dynamic membrane platforms with differentiated physicochemical and molecular properties compared to the surrounding membrane microenvironment, and are the locus for a number of central processes in neuronal physiology. Most recent evidence pinpoint to lipid rafts as main players in AD neuropathology. It is now widely accepted that lipid rafts actively participate in the processing of amyloid precursor protein to generate amyloid beta peptides, a main component of amyloid plaques. Current evidence have highlighted the existence of severe alterations in the molecular structure and functionality of lipid rafts in the frontal cortex of human brains affected by Alzheimer’s disease. An exceptionally interesting observation is that lipid raft destabilization can be demonstrated even at the earliest stages of AD neuropathology. In the present review, we will first elaborate on the structure and function of these multifaceted subcellular structures and second to focus on the impact of their alterations in neuronal pathophysiology along the onset and progression of AD continuum.
APA, Harvard, Vancouver, ISO, and other styles
9

Carrotta, Rita, Fabio Librizzi, Maria Rosalia Mangione, Silvia Vilasi, and Oscar Moran. "Amyloid β-peptide interaction with GM1 containing model membrane." In Advances in Biomembranes and Lipid Self-Assembly. Elsevier, 2020. http://dx.doi.org/10.1016/bs.abl.2020.04.001.

Full text
APA, Harvard, Vancouver, ISO, and other styles
10

Miura, Yoshiko, and Tomohiro Fuku. "Interaction and Aggregation of Amyloid β Peptide with Multivalent Sulfonated Sugar." In Amyloidosis - Mechanisms and Prospects for Therapy. InTech, 2011. http://dx.doi.org/10.5772/22271.

Full text
APA, Harvard, Vancouver, ISO, and other styles

Conference papers on the topic "Interactions peptides amyloides"

1

Jureschi, Monica. "BINDING OF HEAVY METAL IONS TO AMYLOID-? PEPTIDES: INTERACTIONS WITH NAP PEPTIDES." In 19th SGEM International Multidisciplinary Scientific GeoConference EXPO Proceedings. STEF92 Technology, 2019. http://dx.doi.org/10.5593/sgem2019/6.1/s25.075.

Full text
APA, Harvard, Vancouver, ISO, and other styles
2

Ion, Laura. "AMYLOID-? AND ANTI-AMYLOID PEPTIDES INVOLVED IN ALZHEIMER`S DISEASE: INTERACTIONS WITH METAL IONS." In 19th SGEM International Multidisciplinary Scientific GeoConference EXPO Proceedings. STEF92 Technology, 2019. http://dx.doi.org/10.5593/sgem2019/6.1/s25.067.

Full text
APA, Harvard, Vancouver, ISO, and other styles
3

Benaki, Dimitra, Kostas Stamatakis, Emmanuel Mikros та Maria Pelecanou. "Spectroscopic investigation of the interaction of curcumin with β-amyloid peptide (1-40) with fluorescence, CD, and NMR". У XIIth Conference Biologically Active Peptides. Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, 2011. http://dx.doi.org/10.1135/css201113001.

Full text
APA, Harvard, Vancouver, ISO, and other styles
4

Valensin, Daniela, Henryk Kozlowski, Isabella Tessari та ін. "Interactions of metal ions with α synuclein and amyloid β peptides". У INTERNATIONAL CONFERENCE OF COMPUTATIONAL METHODS IN SCIENCES AND ENGINEERING 2014 (ICCMSE 2014). AIP Publishing LLC, 2014. http://dx.doi.org/10.1063/1.4897691.

Full text
APA, Harvard, Vancouver, ISO, and other styles
5

Neelov, Igor, Dilorom Khamidova, Elena Popova, and Fizali Komilov. "Computer Simulation of Interaction of Lysine Dendrimer with Stack of Amyloid Peptides." In 2017 Fourth International Conference on Mathematics and Computers in Sciences and in Industry (MCSI). IEEE, 2017. http://dx.doi.org/10.1109/mcsi.2017.39.

Full text
APA, Harvard, Vancouver, ISO, and other styles
6

Drochioiu, Gabi, Manuela Murariu, Laura Ion, and Laura Habasescu. "Iron and aluminum interaction with amyloid-beta peptides associated with Alzheimer’s disease." In INTERNATIONAL CONFERENCE OF COMPUTATIONAL METHODS IN SCIENCES AND ENGINEERING 2014 (ICCMSE 2014). AIP Publishing LLC, 2014. http://dx.doi.org/10.1063/1.4897686.

Full text
APA, Harvard, Vancouver, ISO, and other styles
7

Andrade, Stephanie, Joana A. Loureiro, Manuel A. N. Coelho, and Maria do Carmo Pereira. "Interaction studies of amyloid beta-peptide with the natural compound resveratrol." In 2015 IEEE 4th Portuguese Meeting on Bioengineering (ENBENG). IEEE, 2015. http://dx.doi.org/10.1109/enbeng.2015.7088833.

Full text
APA, Harvard, Vancouver, ISO, and other styles
8

Ishimura, Hiromi, Ryushi Kadoya, Kanako Shimamura та ін. "Ab initio fragment molecular orbital calculations on the specific interactions between amyloid-β peptides in an in vivo amyloid-β fibril". У 2016 International Conference On Advanced Informatics: Concepts, Theory And Application (ICAICTA). IEEE, 2016. http://dx.doi.org/10.1109/icaicta.2016.7803094.

Full text
APA, Harvard, Vancouver, ISO, and other styles
9

Ota, Shintaro, Hiromi Ishimura, Mitsuki Fujimori, Noriyuki Kurita та Sergiy Shulga. "Ab initio molecular simulations on specific interactions between amyloid-β peptide and new curcumin derivatives". У 2016 International Conference On Advanced Informatics: Concepts, Theory And Application (ICAICTA). IEEE, 2016. http://dx.doi.org/10.1109/icaicta.2016.7803090.

Full text
APA, Harvard, Vancouver, ISO, and other styles
You might also be interested in the extended bibliographies on the topic 'Interactions peptides amyloides' for particular source types:
Journal articles Dissertations / Theses
We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!

To the bibliography