The case for intrinsically disordered proteins playing contributory roles in molecular recognition without a stable 3D structure

Uversky, Vladimir N.; Dunker, A. Keith

doi:10.3410/b5-01

Cited by 14 publications

(15 citation statements)

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“…1C). This may indicate that the autoinhibitory conformation of monomeric PP5 yields an encounter complex with a reduced capacity to interact with the kinases (54). Alternatively, kinase binding sites on HSP90, which regulate HSP90-Akt interactions (55), may facilitate the association of PP5 and ERK1/2 when HSP90 is present.…”

Section: Discussionmentioning

confidence: 99%

Small G Proteins Rac1 and Ras Regulate Serine/Threonine Protein Phosphatase 5 (PP5)·Extracellular Signal-Regulated Kinase (ERK) Complexes Involved in the Feedback Regulation of Raf1

Mazalouskas

Godoy‐Ruiz

Weber

et al. 2014

Journal of Biological Chemistry

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Background: PP5 binds HSP90 and regulates cell growth and stress-induced signaling pathways. Results: PP5 associates with ERKs in a manner facilitated, in part, by HSP90. Rac1 and Ras regulate PP5⅐ERK1/2 complexes. Conclusion: PP5 and ERK play a role in the feedback phosphorylation of PP5-associated Raf1. Significance: Differential responsiveness of PP5-ERK1 and PP5-ERK2 interactions to oncogenic small G proteins may contribute to particular tumor traits.

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Section: Discussionmentioning

confidence: 99%

Small G Proteins Rac1 and Ras Regulate Serine/Threonine Protein Phosphatase 5 (PP5)·Extracellular Signal-Regulated Kinase (ERK) Complexes Involved in the Feedback Regulation of Raf1

Mazalouskas

Godoy‐Ruiz

Weber

et al. 2014

Journal of Biological Chemistry

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“…An interesting discussion eliminating two opposite viewpoints on the phenomenon of protein intrinsic disorder was represented in published side-by-side papers by Uversky and Dunker 32 and Janin and Sternberg 33 . Uversky and Dunker argued that protein intrinsic disorder represents a novel and useful concept that helps better understanding protein functionality and correlation between protein structure and function 32 .…”

Section: Analyzing Functions Of Idps and Idprsmentioning

confidence: 99%

“…Uversky and Dunker argued that protein intrinsic disorder represents a novel and useful concept that helps better understanding protein functionality and correlation between protein structure and function 32 . Janin and Sternberg took an opposing viewpoint, arguing that flexibility, not disorder, is an intrinsic property of proteins, and that most IDPs are in fact proteins waiting for a partner (PWPs), which serve as parts of a multi-component complex that do not fold correctly in the absence of other components 33 …”

Section: Analyzing Functions Of Idps and Idprsmentioning

confidence: 99%

Digested disorder

Uversky

2013

Intrinsically Disordered Proteins

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The current literature on intrinsically disordered proteins is blooming. A simple PubMed search for “intrinsically disordered protein OR natively unfolded protein” returns about 1,800 hits (as of June 17, 2013), with many papers published quite recently. To keep interested readers up to speed with this literature, we are starting a “Digested Disorder” project, which will encompass a series of reader’s digest type of publications aiming at the objective representation of the research papers and reviews on intrinsically disordered proteins. The only two criteria for inclusion in this digest are the publication date (a paper should be published within the covered time frame) and topic (a paper should be dedicated to any aspect of protein intrinsic disorder). The current digest covers papers published during the period of January, February and March of 2013. The papers are grouped hierarchically by topics they cover, and for each of the included paper a short description is given on its major findings.

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“…Others have a degree of structural flexibility that enables them to tailor their shape to the task at hand. (197,198) Hence, it is critical for cells to maintain an efficient quality-control system that ensures the proper production, folding and elimination of proteins. (199,200) When a protein misfolds and evades normal clearance pathways, a pathogenic process can ensue in which the protein aggregates progressively into intracellular and/ or extracellular deposits.…”

Section: Mitochondrial -Lysosomal Dysfunction In Nddmentioning

confidence: 99%

New Insight in The Molecular Mechanisms of Neurodegenerative Disease

2018

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B ACKGROUND:Redox and proteotoxic stress contributes to age-dependent accumulation of dysfunctional mitochondria and protein aggregates, and is associated with neurodegeneration. The free radical theory of aging inspired many studies using reactive species scavengers such as alpha-tocopherol, ascorbate and coenzyme-Q to suppress the initiation of oxidative stress. However, clinical trials have had limited success in the treatment of neurodegenerative diseases (NDDs). CONTENT:The misfolding and aggregation of specific proteins is a seminal occurrence in a remarkable variety of NDDs. In Alzheimer's disease, the two principal aggregating proteins are β-amyloid (Aβ) and tau. The abnormal assemblies formed by conformational variants of these proteins range in size from small oligomers to the characteristic lesions that are visible by optical microscopy, such as senile plaques and neurofibrillary tangles. Pathologic similarities with prion disease suggest that the formation and spread of these proteinaceous lesions might involve a common molecular mechanism, corruptive protein templating. The accumulation of redox modified proteins or organelles cannot be reversed by oxidant intercepting antioxidants and must then be removed by alternative mechanisms. Autophagy serves this essential function in removing damaged or dysfunctional proteins and organelles thus preserving neuronal function and survival.SUMMARY: Senescent cells and their senescenceassociated secretory phenotypes (SASPs) may constitute a novel, understudied, and potentially important contributor to neuro-inflammation and subsequent neurodegeneration. Characterization of cellular senescence in the brain could uncover novel therapeutic targets for the prevention and treatment of chronic age-related NDDs. KEYwORDS

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The case for intrinsically disordered proteins playing contributory roles in molecular recognition without a stable 3D structure

Cited by 14 publications

References 0 publications

Small G Proteins Rac1 and Ras Regulate Serine/Threonine Protein Phosphatase 5 (PP5)·Extracellular Signal-Regulated Kinase (ERK) Complexes Involved in the Feedback Regulation of Raf1

Small G Proteins Rac1 and Ras Regulate Serine/Threonine Protein Phosphatase 5 (PP5)·Extracellular Signal-Regulated Kinase (ERK) Complexes Involved in the Feedback Regulation of Raf1

Digested disorder

New Insight in The Molecular Mechanisms of Neurodegenerative Disease

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