Fibril - OmicsDI

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UNIPROT ID/AC

P01258 (1)
P08473 (1)
P05067 (1)
9685.ENSFCAP00000000151 (1)
9685.ENSFCAP00000000248 (1)
9685.ENSFCAP00000000262 (1)
9685.ENSFCAP00000000263 (1)
9685.ENSFCAP00000000264 (1)
9685.ENSFCAP00000000265 (1)
9685.ENSFCAP00000000266 (1)
9685.ENSFCAP00000000268 (1)
9685.ENSFCAP00000000269 (1)
9685.ENSFCAP00000000272 (1)
9685.ENSFCAP00000000275 (1)
9685.ENSFCAP00000000295 (1)
9685.ENSFCAP00000000561 (1)
9685.ENSFCAP00000000816 (1)
9685.ENSFCAP00000000920 (1)
9685.ENSFCAP00000001179 (1)
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9685.ENSFCAP00000001692 (1)
9685.ENSFCAP00000001790 (1)
9685.ENSFCAP00000001993 (1)
9685.ENSFCAP00000002741 (1)
9685.ENSFCAP00000002944 (1)
9685.ENSFCAP00000003079 (1)
9685.ENSFCAP00000003529 (1)
9685.ENSFCAP00000004423 (1)
9685.ENSFCAP00000004671 (1)
9685.ENSFCAP00000005343 (1)

CHEBI ID

CHEBI:15366 (4)
CHEBI:17790 (4)
CHEBI:30751 (4)
CHEBI:1148 (4)
CHEBI:15354 (4)
CHEBI:15428 (4)
CHEBI:32816 (4)
CHEBI:16856 (4)
CHEBI:15422 (4)
CHEBI:15891 (4)
CHEBI:17170 (3)
CHEBI:15347 (3)
CHEBI:15344 (3)
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CHEBI:18295 (3)
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CHEBI:78320 (3)
CHEBI:15996 (3)
CHEBI:16449 (3)
CHEBI:25017 (3)
CHEBI:24898 (3)
CHEBI:18323 (3)
CHEBI:16870 (3)
CHEBI:17268 (3)
CHEBI:21547 (3)
CHEBI:16811 (3)
CHEBI:16737 (3)
CHEBI:26986 (3)
CHEBI:60425 (2)
CHEBI:64645 (1)

Metabolite Name

Taurine (4)
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Valine (3)
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Pi-Methylhistidine (2)
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O-Acetylcarnitine (2)
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First Public Date

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Modelling Approach

Ordinary differential equation model (5)

Lab affiliation

Bio-X Institutes, Key Laboratory for the Genetics of Developmental and Neuropsychiatric Disorders (Ministry of Education), Shanghai Jiao Tong University, Shanghai, China (5)
School of Automation and Intelligent Sensing, Shanghai Jiao Tong University (5)
IMSB, ETH Zurich (4)
1 Interdisciplinary Research Center on Biology and Chemistry, State Key Laboratory of Chemical Biology, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai 201210, China 2 Shanghai Academy of Natural Sciences (SANS), Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai 201210, China (2)
CRIBL Unit, UMR CNRS 7276 INSERM 1262, University of Limoges (2)
Department of Structural Biology and Developmental Neurobiology, St. Jude Children's Research Hospital, Memphis, TN 38105, USA (2)
MRC Laboratory of Molecular Biology, Cambridge, UK (2)
Tianjin Key Laboratory of Biosensing and Molecular Recognition, Research Center for Analytical Science, Frontiers Science Center for New Organic Matter, College of Chemistry, Nankai University, Tianjin 300071, China (2)
1 Interdisciplinary Research Center on Biology and Chemistry, State Key Laboratory of Chemical Biology, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai 201210, China 2 Shanghai Academy of Natural Sciences (SANS), Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai 201210, China (lab head) (1)
1Department of Chemistry, Michigan State University, 578 S Shaw Lane, East Lansing, Michigan 48824, USA (1)
Amyloidosis Treatment and Research Center, Fondazione IRCCS Policlinico San Matteo and University of Pavia, Italy (1)
Associate Professor Regional Centre for Biotechnology (1)
Astbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, LS2 9JT, United Kingdom (1)
Bio-X Institutes, Key Laboratory for the Genetics of Developmental and Neuropsychiatric Disorders, Ministry of Education, Shanghai Jiao Tong University, Shanghai, China (1)
Biological Imaging Laboratory for Disease and Exposure Research (BILDER), Department of Chemistry, North Carolina State University, Raleigh, NC, 27695, USA (1)
Cell Biology, Faculty of Science, Utrecht University (1)
Center for Molecular Medicine, Molecular Cancer Research, University Medical Center Utrecht, Universiteitsweg 100, 3584CG Utrecht, The Netherlands. (1)
Center of Basic Science, Biomedical Research Foundation of the Academy of Athens, Athens, Greece (1)
Centre de Recherche des Cordeliers, Sorbonne Université, INSERM, Université de Paris, Oral Molecular Pathophysiology, F-75006, France (1)
Chronic Disease Programme (UFIEC), Instituto de Salud Carlos III, Majadahonda, E-28220 Madrid, Spain. (1)
Dana Farber Cancer Institute, Boston, MA Harvard Medical School, Boston, MA (1)
Departement of Veterinary Medicine and Animal Sciences (1)
Department of Biomedical Sciences, University of Copenhagen, Denmark (1)
Department of Molecular Medicine, University of Pavia, Pavia, Italy Amyloidosis Research and Treatment Center, Fondazione IRCCS Policlinico San Matteo, Pavia, Italy (1)
Department of Molecular and Cellular Biology, University of Geneva, Geneva, Switzerland (1)
Department of Pathology and Medicine, University of California at San Diego, La Jolla, CA 92093, USA (1)
Department of Structural Biology, St. Jude Children's Research Hospital, Memphis, TN, USA (1)
Dept. of Biological Chemistry, Institute of Life Sciences, The Hebrew University of Jerusalem, Jerusalem, Israel (1)
Dr. Sascha Martens, Max Perutz Labs, University of Vienna, Vienna BioCenter, Vienna, Austria (1)
EDyP (1)

IsPrivate

False (5)

Classification

bacteria (1)

Study type

Transcription profiling by array (96)
RNA-seq of coding RNA (13)
RNA-seq of coding RNA from single cells (2)
Unknown experiment type (1)
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Crespo2012 - Kinetics of Amyloid Fibril Formation

Crespo2012 - Kinetics of Amyloid Fibril Formation This model is described in the article: A generic crystallization-like model that describes the kinetics of amyloid fibril formation. Crespo R, Rocha FA, Damas AM, Martins PM. J. Biol. Chem. 2012 Aug; 287(36): 30585-30594...

2024-09-02 | BIOMD0000000531 | BioModels

Cryo-EM structure of a lysozyme-derived amyloid fibril from hereditary amyloidosis

Systemic ALys amyloidosis is a debilitating protein misfolding diseases that arises from the formation of amyloid fibrils from C-type lysozyme. We here present a 2.8 A cryo-electron microscopy structure of an amyloid fibril, which was isolated from the abdominal fat tissue of a patient who expressed...

ORGANISM(S): Homo Sapiens (ncbitaxon:9606)

2024-10-21 | MSV000096142 | MassIVE

Using an NMR metabolomics approach to investigate the pathogenicity of amyloid-beta and alpha-synuclein

INTRODUCTION: The pathogenicity at differing points along the aggregation pathway of many fibril-forming proteins associated with neurodegenerative diseases is unclear. Understanding the effect of different aggregation states of these proteins on cellular processes is essential to enhance understand...

2018-06-11 | MTBLS455 | MetaboLights

Cryo-EM of cardiac AL-224L amyloid reveals shared features in l6 light chain fibril folds

Structural characterization of an amyloid fibril from a patient afected by cardiac light chain amyloidosis.

ORGANISM(S): Homo sapiens (Human)

2026-01-23 | PXD064296 | Pride

Amyloid fibril proteomics of AD brains reveals modifiers of aggregation and toxicity

The accumulation of amyloid beta peptides in fibrils is prerequisite for Alzheimers disease (AD). Our understanding of the proteins that promote Abeta fibril formation and mediate neurotoxicity has been limited due to technical challenges in isolating pure amyloid fibrils from brain extracts.

ORGANISM(S): Rattus Norvegicus (ncbitaxon:10116)

2023-06-29 | MSV000092311 | MassIVE

RNA-seq analysis for mRNA expression change in alpha-synclein fibril-treated cultured oligodendrocyte precursor cells

PRJNA420725 | ENA

Protofibril-Fibril Interactions Inhibit Amyloid Fibril Assembly by Obstructing Secondary Nucleation.

Not available

S-EPMC7898819 | biostudies-literature

Branching in amyloid fibril growth.

Not available

S-EPMC2717229 | biostudies-literature

Physical basis of amyloid fibril polymorphism.

Not available