Intramolecular interactions stabilizing compact conformations of the intrinsically disordered kinase-inhibitor domain of Sic1: a molecular dynamics investigation. (Q41728638)

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scientific article published on 22 November 2012

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English	Intramolecular interactions stabilizing compact conformations of the intrinsically disordered kinase-inhibitor domain of Sic1: a molecular dynamics investigation.	scientific article published on 22 November 2012

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scholarly article

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18 February 2020

Intramolecular interactions stabilizing compact conformations of the intrinsically disordered kinase-inhibitor domain of Sic1: a molecular dynamics investigation (English)

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18 February 2020

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18 February 2020

Stefania Brocca

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18 February 2020

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Matteo Lambrughi

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Lorenzo Testa

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Luca De Gioia

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Rita Grandori

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22 November 2012

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18 February 2020

Frontiers in Physiology

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18 February 2020

A preformed binding interface in the unbound ensemble of an intrinsically disordered protein: evidence from molecular simulations

1 reference

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Sic1 as a timer of Clb cyclin waves in the yeast cell cycle--design principle of not just an inhibitor.

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Microsecond molecular dynamics simulations of intrinsically disordered proteins involved in the oxidative stress response

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Cascades of multisite phosphorylation control Sic1 destruction at the onset of S phase

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Structural analysis of intrinsically disordered proteins by small-angle X-ray scattering

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Intrinsically Disordered Proteins in a Physics-Based World

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Compaction properties of an intrinsically disordered protein: Sic1 and its kinase-inhibitor domain

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Net charge per residue modulates conformational ensembles of intrinsically disordered proteins

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Limitations of induced folding in molecular recognition by intrinsically disordered proteins

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Order propensity of an intrinsically disordered protein, the cyclin-dependent-kinase inhibitor Sic1

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Reconciling binding mechanisms of intrinsically disordered proteins.

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Residual structure within the disordered C-terminal segment of p21(Waf1/Cip1/Sdi1) and its implications for molecular recognition.

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Mapping alpha-helical induced folding within the intrinsically disordered C-terminal domain of the measles virus nucleoprotein by site-directed spin-labeling EPR spectroscopy

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CDK inhibitors: cell cycle regulators and beyond

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Molecular dynamics simulations reveal a disorder-to-order transition on phosphorylation of smooth muscle myosin.

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Cell size at S phase initiation: an emergent property of the G1/S network

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Improved structural characterizations of the drkN SH3 domain unfolded state suggest a compact ensemble with native-like and non-native structure

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Disordered p27Kip1 exhibits intrinsic structure resembling the Cdk2/cyclin A-bound conformation

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The interplay between structure and function in intrinsically unstructured proteins.

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The yeast cyclin-dependent kinase inhibitor Sic1 and mammalian p27Kip1 are functional homologues with a structurally conserved inhibitory domain

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Hog1 mediates cell-cycle arrest in G1 phase by the dual targeting of Sic1.

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Natively unfolded proteins: a point where biology waits for physics

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Detection of multiple protein conformational ensembles in solution via deconvolution of charge-state distributions in ESI MS.

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On the convergence of the conformational coordinates basis set obtained by the essential dynamics analysis of proteins' molecular dynamics simulations

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12 December 2020

based on heuristic

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The cyclin-dependent kinase inhibitory domain of the yeast Sic1 protein is contained within the C-terminal 70 amino acids

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

C-terminal acidic domain of ubiquitin-conjugating enzymes: A multi-functional conserved intrinsically disordered domain in family 3 of E2 enzymes

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Protein disorder prevails under crowded conditions

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https://pubmed.ncbi.nlm.nih.gov/23189058

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Synergistic folding of two intrinsically disordered proteins: searching for conformational selection

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.3389/FPHYS.2012.00435

1 reference

Europe PubMed Central

PMC publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:23189058 AND SRC:MED&resulttype=core&format=json

18 February 2020

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:23189058 AND SRC:MED&resulttype=core&format=json

18 February 2020

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:23189058 AND SRC:MED&resulttype=core&format=json

18 February 2020

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0 references

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