scholarly article | Q13442814 |
P356 | DOI | 10.1007/978-3-319-57348-9_8 |
P698 | PubMed publication ID | 28971419 |
P50 | author | Nikolaos N Louros | Q59687651 |
Stavros J Hamodrakas | Q96069964 | ||
P2093 | author name string | Vassiliki A Iconomidou | |
Paraskevi L Tsiolaki | |||
Katerina C Nastou | |||
P2860 | cites work | Clusterin is an ATP-independent chaperone with very broad substrate specificity that stabilizes stressed proteins in a folding-competent state | Q24290651 |
The pentapeptide LQVVR plays a pivotal role in human cystatin C fibrillization | Q24308267 | ||
Identification of a novel 'aggregation-prone'/'amyloidogenic determinant' peptide in the sequence of the highly amyloidogenic human calcitonin | Q24315813 | ||
Cytoscape: a software environment for integrated models of biomolecular interaction networks | Q24515682 | ||
Network biology: understanding the cell's functional organization | Q27861027 | ||
Protein misfolding, functional amyloid, and human disease | Q28131732 | ||
The BioGRID interaction database: 2015 update | Q28252221 | ||
Clusterin, a binding protein with a molten globule-like region | Q28909721 | ||
BiNGO: a Cytoscape plugin to assess overrepresentation of gene ontology categories in biological networks | Q29547427 | ||
UniProt: a hub for protein information | Q29547457 | ||
Activities at the Universal Protein Resource (UniProt) | Q29617787 | ||
From the globular to the fibrous state: protein structure and structural conversion in amyloid formation. | Q30431328 | ||
Amyloidogenic determinants are usually not buried | Q33480337 | ||
The amyloid stretch hypothesis: recruiting proteins toward the dark side | Q34133256 | ||
Clusterin/apolipoprotein J in human aging and cancer | Q34146411 | ||
A consensus method for the prediction of 'aggregation-prone' peptides in globular proteins | Q34552231 | ||
Conformational constraints for amyloid fibrillation: the importance of being unfolded | Q35768731 | ||
From the polymorphism of amyloid fibrils to their assembly mechanism and cytotoxicity | Q36693078 | ||
Short protein segments can drive a non-fibrillizing protein into the amyloid state | Q37285515 | ||
Clusterin: a forgotten player in Alzheimer's disease | Q37570713 | ||
Chapter 9: Oxidative stress in malignant progression: The role of Clusterin, a sensitive cellular biosensor of free radicals | Q37624996 | ||
Evidence that clusterin has discrete chaperone and ligand binding sites. | Q38293431 | ||
Structural studies and cytotoxicity assays of "aggregation-prone" IAPP(8-16) and its non-amyloidogenic variants suggest its important role in fibrillogenesis and cytotoxicity of human amylin | Q38882209 | ||
An amyloidogenic determinant in N-terminal pro-brain natriuretic peptide (NT-proBNP): Implications for cardiac amyloidoses | Q39724371 | ||
Exploring the 'aggregation-prone' core of human Cystatin C: A structural study | Q40667591 | ||
Chameleon 'aggregation-prone' segments of apoA-I: A model of amyloid fibrils formed in apoA-I amyloidosis | Q40863460 | ||
Determination of protein secondary structure by Fourier transform infrared spectroscopy: a critical assessment | Q40869927 | ||
Identification of a penta- and hexapeptide of islet amyloid polypeptide (IAPP) with amyloidogenic and cytotoxic properties | Q40902557 | ||
Hereditary cerebral hemorrhage with amyloidosis-Dutch type (HCHWA-D): II--A review of histopathological aspects | Q41061808 | ||
Apolipoprotein J: structure and tissue distribution | Q41731295 | ||
Identification of the disulfide bonds in human plasma protein SP-40,40 (apolipoprotein-J) | Q44957308 | ||
An N-terminal pro-atrial natriuretic peptide (NT-proANP) 'aggregation-prone' segment involved in isolated atrial amyloidosis. | Q45910987 | ||
Computing topological parameters of biological networks | Q51900389 | ||
Deposition of apolipoproteins E and J in senile plaques is topographically determined in both Alzheimer's disease and Down's syndrome brain | Q52207172 | ||
SP-40,40 is a constituent of Alzheimer's amyloid | Q53179261 | ||
Do Extracellular Chaperone Proteins in Plasma have Potential as Alzheimer‘s Disease Biomarkers? | Q53314970 | ||
Clusterin Has Chaperone-like Activity Similar to That of Small Heat Shock Proteins | Q57639622 | ||
P407 | language of work or name | English | Q1860 |
P921 | main subject | bioinformatics | Q128570 |
P304 | page(s) | 93-107 | |
P577 | publication date | 2017-01-01 | |
P1433 | published in | Advances in Experimental Medicine and Biology | Q4686385 |
P1476 | title | Exploring Amyloidogenicity of Clusterin: A Structural and Bioinformatics Analysis | |
P478 | volume | 989 |
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