Cellular strategies for regulating functional and nonfunctional protein aggregation.
about
Classification of intrinsically disordered regions and proteinsAdvances in the characterization of RNA-binding proteinsThe contribution of intrinsically disordered regions to protein function, cellular complexity, and human diseaseLegal but lethal: functional protein aggregation at the verge of toxicityOrigin and spread of de novo genes in Drosophila melanogaster populationsAggregation prone regions in human proteome: Insights from large-scale data analyses.Constitutive patterns of gene expression regulated by RNA-binding proteinsInterplay between chaperones and protein disorder promotes the evolution of protein networks.Assemblages: functional units formed by cellular phase separationAsymmetric mRNA localization contributes to fidelity and sensitivity of spatially localized systemsGlobal analysis of protein aggregation in yeast during physiological conditions and arsenite stress.Transcriptional Response to Acute Thermal Exposure in Juvenile Chinook Salmon Determined by RNAseq.Multivalent IDP assemblies: Unique properties of LC8-associated, IDP duplex scaffoldsRegulation of HBEGF by Micro-RNA for Survival of Developing Human Trophoblast Cells.Evolution of Robustness to Protein Mistranslation by Accelerated Protein Turnover.Quantitative nature of overexpression experiments.Structural transformation of the amyloidogenic core region of TDP-43 protein initiates its aggregation and cytoplasmic inclusion.Widespread aggregation and neurodegenerative diseases are associated with supersaturated proteins.Principles of self-organization in biological pathways: a hypothesis on the autogenous association of alpha-synucleinThe spliceosome: disorder and dynamics defined.The ribosome as a hub for protein quality control.Promiscuity as a functional trait: intrinsically disordered regions as central players of interactomes.Heavy metals and metalloids as a cause for protein misfolding and aggregation.Supersaturation is a major driving force for protein aggregation in neurodegenerative diseases.How do disordered regions achieve comparable functions to structured domains?Supramolecular catalysis and dynamic assemblies for medicine.ER stress causes widespread protein aggregation and prion formation.Understanding and predicting protein misfolding and aggregation: Insights from proteomics.Cell-wide analysis of protein thermal unfolding reveals determinants of thermostability.The yin and yang of amyloid aggregation.Protein synthesis rate is the predominant regulator of protein expression during differentiation.A high-throughput approach to profile RNA structure.Distinct stress conditions result in aggregation of proteins with similar properties.Computational analysis of candidate prion-like proteins in bacteria and their role.Proteome response at the edge of protein aggregation.Phase separation in solutions with specific and nonspecific interactions.Fitness costs of minimal sequence alterations causing protein instability and toxicity.Constraints and consequences of the emergence of amino acid repeats in eukaryotic proteins.Proteins evolve on the edge of supramolecular self-assembly.Stoichiometric balance of protein copy numbers is measurable and functionally significant in a protein-protein interaction network for yeast endocytosis.
P2860
Q22061736-C4CEEFE4-0F0A-42B4-BB0B-7EBFAB515AB2Q26738495-D2E889AC-8772-4FF5-907F-029DA2474C8AQ28080017-F5B2D307-1F12-48E6-8BA1-09571BC79D03Q28084859-0EF4B544-E1BD-48BA-9B77-31D8DEF2DE3BQ28306501-B1A5BCEF-CC92-4F54-A6F1-79F4992D18DEQ31170430-2ABBF058-4F8F-4FBE-AF62-F42DF6C34665Q33745315-FEB4B143-836D-4826-B4C1-74F480924B22Q33811809-7FB4B2D7-4C3A-4AAA-8073-CD28BD787764Q34117231-B81AAEAD-1D9F-483D-99AB-921C830EC638Q34205647-D5D62824-7BAD-4AAF-9E5E-4DC8D579F258Q34340978-11A857E5-7404-4BE6-A4C2-4432B0144C43Q35614274-08DA006C-9875-4BE5-8793-91FAAE7B93C8Q36103418-938DF803-9641-42CA-987D-5E72529B1258Q36152760-A2D8F44A-C3A2-45EC-A803-6555712684FBQ36257601-C1DAD106-490F-47DE-B113-5E7D100C471AQ36455398-3041DCE1-EC8C-432F-9960-AC9A2584CB70Q37000560-C1D4B1BB-33EB-4940-933A-C29FF41ABC33Q37442810-6604B20F-2A42-4A20-94DB-DDC6684C2BB2Q37528739-0CA570D1-CDBE-4D46-823A-8DDDD094DCBCQ37704918-EF88617F-2787-44FD-918E-6B8F135037B7Q38080280-C0A0565D-0A48-49C6-9152-7687773DA700Q38132466-5A5D93CE-158E-4EF1-BDB7-68AD797BEABFQ38223690-9D386E8D-A0E7-4387-B442-2F149D948545Q38338129-D67C3994-7B4C-41B7-B750-A7FC03E50991Q38370771-9F3A2C2D-5A5F-432F-98A9-4D8B128AB538Q38636287-C4CFB07F-F500-44A8-BE93-40258DE709ECQ38718411-D4327F27-D053-4DF6-BD34-582DF596431FQ38915018-EAF8ED84-C156-47FD-96EC-9D23071BB879Q38945211-AC42CE19-1B7A-47FB-932E-BA7DC1F804EAQ38970051-4068BC1D-81E2-4562-91B6-E6E0C189D6DAQ39094533-6C439FE0-393A-4618-AB75-0A4740701AF3Q39144550-CE3A4833-8B22-4474-A242-1BDC2C2C6B59Q39844654-B1147960-BF87-421F-8D83-41481E7AC109Q40362652-363A1517-1D57-44BA-B051-C8E9E08E8CF6Q41448210-4A950645-A599-4FD5-AAB9-D56A51413320Q45945132-8E9A86CA-A6A0-4334-B2A8-4EC926C10133Q46265005-CBA30DB5-F384-406B-AA90-0486B86B6F72Q47956508-49AFA978-9834-49A2-AF52-C98576F0D26AQ47982938-EDCB8AC8-CE4B-4E87-981F-3F959919EE4FQ52666816-D3E5BA15-4B45-46C3-BB40-2A4BFCDA0129
P2860
Cellular strategies for regulating functional and nonfunctional protein aggregation.
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
2012年论文
@zh
2012年论文
@zh-cn
name
Cellular strategies for regulating functional and nonfunctional protein aggregation.
@ast
Cellular strategies for regulating functional and nonfunctional protein aggregation.
@en
type
label
Cellular strategies for regulating functional and nonfunctional protein aggregation.
@ast
Cellular strategies for regulating functional and nonfunctional protein aggregation.
@en
prefLabel
Cellular strategies for regulating functional and nonfunctional protein aggregation.
@ast
Cellular strategies for regulating functional and nonfunctional protein aggregation.
@en
P2860
P1433
P1476
Cellular strategies for regulating functional and nonfunctional protein aggregation.
@en
P2093
Jörg Gsponer
P2860
P304
P356
10.1016/J.CELREP.2012.09.036
P577
2012-11-15T00:00:00Z