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Disorder in the lifetime of a protein.

Intrinsically disordered proteins

Uversky VN.
PMID: 28516024
Intrinsically Disord Proteins. 2013 Nov 07;1(1):e26782. doi: 10.4161/idp.26782. eCollection 2013.

Intrinsic disorder is everywhere and is inevitable. The non-folding propensity is inherent for numerous natural polypeptide chains, and many functional proteins and protein regions are intrinsically disordered. Furthermore, at particular moments in their life, most notably during their synthesis...

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Uversky VN. Disorder in the lifetime of a protein. Intrinsically Disord Proteins. 2013;1(1):e26782doi: 10.4161/idp.26782.
Uversky, V. N. (2013). Disorder in the lifetime of a protein. Intrinsically disordered proteins, 1(1), e26782. https://doi.org/10.4161/idp.26782
Uversky, Vladimir N. "Disorder in the lifetime of a protein." Intrinsically disordered proteins vol. 1,1 (2013): e26782. doi: https://doi.org/10.4161/idp.26782
Uversky VN. Disorder in the lifetime of a protein. Intrinsically Disord Proteins. 2013 Nov 07;1(1):e26782. doi: 10.4161/idp.26782. eCollection 2013. PMID: 28516024; PMCID: PMC5424783.
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Structural characterizations of phosphorylatable residues in transmembrane proteins from .

Intrinsically disordered proteins

Xue B, Uversky VN.
PMID: 28516016
Intrinsically Disord Proteins. 2013 Apr 01;1(1):e25713. doi: 10.4161/idp.25713. eCollection 2013.

Phosphorylation is a common post-translational modification that plays important roles in a wide range of biochemical and cellular processes. Many enzymes and receptors can be switched "on" or "off" by conformational changes induced by phosphorylation. The phosphorylation process is...

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Xue B, Uversky VN. Structural characterizations of phosphorylatable residues in transmembrane proteins from . Intrinsically Disord Proteins. 2013;1(1):e25713doi: 10.4161/idp.25713.
Xue, B., & Uversky, V. N. (2013). Structural characterizations of phosphorylatable residues in transmembrane proteins from . Intrinsically disordered proteins, 1(1), e25713. https://doi.org/10.4161/idp.25713
Xue, Bin, and Uversky, Vladimir N. "Structural characterizations of phosphorylatable residues in transmembrane proteins from ." Intrinsically disordered proteins vol. 1,1 (2013): e25713. doi: https://doi.org/10.4161/idp.25713
Xue B, Uversky VN. Structural characterizations of phosphorylatable residues in transmembrane proteins from . Intrinsically Disord Proteins. 2013 Apr 01;1(1):e25713. doi: 10.4161/idp.25713. eCollection 2013. PMID: 28516016; PMCID: PMC5424800.
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Digested disorder: Quarterly intrinsic disorder digest (July-August-September, 2013).

Intrinsically disordered proteins

Reddy KD, DeForte S, Uversky VN.
PMID: 28232877
Intrinsically Disord Proteins. 2014 May 19;2(1):e27833. doi: 10.4161/idp.27833. eCollection 2014.

The current literature on intrinsically disordered proteins grows fast. To keep interested readers up to speed with this literature, we continue a "Digested Disorder" project and represent a new issue of reader's digest of the research papers and reviews...

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Reddy KD, DeForte S, Uversky VN. Digested disorder: Quarterly intrinsic disorder digest (July-August-September, 2013). Intrinsically Disord Proteins. 2014;2(1):e27833doi: 10.4161/idp.27833.
Reddy, K. D., DeForte, S., & Uversky, V. N. (2014). Digested disorder: Quarterly intrinsic disorder digest (July-August-September, 2013). Intrinsically disordered proteins, 2(1), e27833. https://doi.org/10.4161/idp.27833
Reddy, Krishna D, et al. "Digested disorder: Quarterly intrinsic disorder digest (July-August-September, 2013)." Intrinsically disordered proteins vol. 2,1 (2014): e27833. doi: https://doi.org/10.4161/idp.27833
Reddy KD, DeForte S, Uversky VN. Digested disorder: Quarterly intrinsic disorder digest (July-August-September, 2013). Intrinsically Disord Proteins. 2014 May 19;2(1):e27833. doi: 10.4161/idp.27833. eCollection 2014. PMID: 28232877; PMCID: PMC5314876.
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Quarterly intrinsic disorder digest (January-February-March, 2014).

Intrinsically disordered proteins

DeForte S, Reddy KD, Uversky VN.
PMID: 28232896
Intrinsically Disord Proteins. 2016 Feb 12;4(1):e1153395. doi: 10.1080/21690707.2016.1153395. eCollection 2016.

This is the 5

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DeForte S, Reddy KD, Uversky VN. Quarterly intrinsic disorder digest (January-February-March, 2014). Intrinsically Disord Proteins. 2016;4(1):e1153395doi: 10.1080/21690707.2016.1153395.
DeForte, S., Reddy, K. D., & Uversky, V. N. (2016). Quarterly intrinsic disorder digest (January-February-March, 2014). Intrinsically disordered proteins, 4(1), e1153395. https://doi.org/10.1080/21690707.2016.1153395
DeForte, Shelly, et al. "Quarterly intrinsic disorder digest (January-February-March, 2014)." Intrinsically disordered proteins vol. 4,1 (2016): e1153395. doi: https://doi.org/10.1080/21690707.2016.1153395
DeForte S, Reddy KD, Uversky VN. Quarterly intrinsic disorder digest (January-February-March, 2014). Intrinsically Disord Proteins. 2016 Feb 12;4(1):e1153395. doi: 10.1080/21690707.2016.1153395. eCollection 2016. PMID: 28232896; PMCID: PMC5314902.
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How disordered is my protein and what is its disorder for? A guide through the "dark side" of the protein universe.

Intrinsically disordered proteins

Lieutaud P, Ferron F, Uversky AV, Kurgan L, Uversky VN, Longhi S.
PMID: 28232901
Intrinsically Disord Proteins. 2016 Dec 21;4(1):e1259708. doi: 10.1080/21690707.2016.1259708. eCollection 2016.

In the last 2 decades it has become increasingly evident that a large number of proteins are either fully or partially disordered. Intrinsically disordered proteins lack a stable 3D structure, are ubiquitous and fulfill essential biological functions. Their conformational...

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Lieutaud P, Ferron F, Uversky AV, et al. How disordered is my protein and what is its disorder for? A guide through the "dark side" of the protein universe. Intrinsically Disord Proteins. 2016;4(1):e1259708doi: 10.1080/21690707.2016.1259708.
Lieutaud, P., Ferron, F., Uversky, A. V., Kurgan, L., Uversky, V. N., & Longhi, S. (2016). How disordered is my protein and what is its disorder for? A guide through the "dark side" of the protein universe. Intrinsically disordered proteins, 4(1), e1259708. https://doi.org/10.1080/21690707.2016.1259708
Lieutaud, Philippe, et al. "How disordered is my protein and what is its disorder for? A guide through the "dark side" of the protein universe." Intrinsically disordered proteins vol. 4,1 (2016): e1259708. doi: https://doi.org/10.1080/21690707.2016.1259708
Lieutaud P, Ferron F, Uversky AV, Kurgan L, Uversky VN, Longhi S. How disordered is my protein and what is its disorder for? A guide through the "dark side" of the protein universe. Intrinsically Disord Proteins. 2016 Dec 21;4(1):e1259708. doi: 10.1080/21690707.2016.1259708. eCollection 2016. PMID: 28232901; PMCID: PMC5314888.
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Looking at the recent advances in understanding α-synuclein and its aggregation through the proteoform prism.

F1000Research

Uversky VN.
PMID: 28491292
F1000Res. 2017 Apr 20;6:525. doi: 10.12688/f1000research.10536.1. eCollection 2017.

Despite attracting the close attention of multiple researchers for the past 25 years, α-synuclein continues to be an enigma, hiding sacred truth related to its structure, function, and dysfunction, concealing mechanisms of its pathological spread within the affected brain...

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Uversky VN. Looking at the recent advances in understanding α-synuclein and its aggregation through the proteoform prism. F1000Res. 2017;6:525doi: 10.12688/f1000research.10536.1.
Uversky, V. N. (2017). Looking at the recent advances in understanding α-synuclein and its aggregation through the proteoform prism. F1000Research, 6525. https://doi.org/10.12688/f1000research.10536.1
Uversky, Vladimir N. "Looking at the recent advances in understanding α-synuclein and its aggregation through the proteoform prism." F1000Research vol. 6 (2017): 525. doi: https://doi.org/10.12688/f1000research.10536.1
Uversky VN. Looking at the recent advances in understanding α-synuclein and its aggregation through the proteoform prism. F1000Res. 2017 Apr 20;6:525. doi: 10.12688/f1000research.10536.1. eCollection 2017. PMID: 28491292; PMCID: PMC5399969.
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On the potential of using peculiarities of the protein intrinsic disorder distribution in mitochondrial cytochrome .

Intrinsically disordered proteins

Yacoub HA, Sadek MA, Uversky VN.
PMID: 28331777
Intrinsically Disord Proteins. 2017 Mar 07;5(1):e1264350. doi: 10.1080/21690707.2016.1264350. eCollection 2017.

This study was conducted to identify the source of animal meat based on the peculiarities of protein intrinsic disorder distribution in mitochondrial cytochrome

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Yacoub HA, Sadek MA, Uversky VN. On the potential of using peculiarities of the protein intrinsic disorder distribution in mitochondrial cytochrome . Intrinsically Disord Proteins. 2017;5(1):e1264350doi: 10.1080/21690707.2016.1264350.
Yacoub, H. A., Sadek, M. A., & Uversky, V. N. (2017). On the potential of using peculiarities of the protein intrinsic disorder distribution in mitochondrial cytochrome . Intrinsically disordered proteins, 5(1), e1264350. https://doi.org/10.1080/21690707.2016.1264350
Yacoub, Haitham A, et al. "On the potential of using peculiarities of the protein intrinsic disorder distribution in mitochondrial cytochrome ." Intrinsically disordered proteins vol. 5,1 (2017): e1264350. doi: https://doi.org/10.1080/21690707.2016.1264350
Yacoub HA, Sadek MA, Uversky VN. On the potential of using peculiarities of the protein intrinsic disorder distribution in mitochondrial cytochrome . Intrinsically Disord Proteins. 2017 Mar 07;5(1):e1264350. doi: 10.1080/21690707.2016.1264350. eCollection 2017. PMID: 28331777; PMCID: PMC5351768.
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Prediction of Intrinsic Disorder in MERS-CoV/HCoV-EMC Supports a High Oral-Fecal Transmission.

PLoS currents

Goh GK, Dunker AK, Uversky V.
PMID: 24270586
PLoS Curr. 2013 Nov 13;5. doi: 10.1371/currents.outbreaks.22254b58675cdebc256dbe3c5aa6498b.

A novel coronavirus, MERS-CoV (NCoV, HCoV-EMC/2012), originating from the Middle-East, has been discovered. Incoming data reveal that the virus is highly virulent to humans. A model that categorizes coronaviuses according to the hardness of their shells was developed before...

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Goh GK, Dunker AK, Uversky V. Prediction of Intrinsic Disorder in MERS-CoV/HCoV-EMC Supports a High Oral-Fecal Transmission. PLoS Curr. 2013;5doi: 10.1371/currents.outbreaks.22254b58675cdebc256dbe3c5aa6498b.
Goh, G. K., Dunker, A. K., & Uversky, V. (2013). Prediction of Intrinsic Disorder in MERS-CoV/HCoV-EMC Supports a High Oral-Fecal Transmission. PLoS currents, 5. https://doi.org/10.1371/currents.outbreaks.22254b58675cdebc256dbe3c5aa6498b
Goh, Gerard Kian-Meng, et al. "Prediction of Intrinsic Disorder in MERS-CoV/HCoV-EMC Supports a High Oral-Fecal Transmission." PLoS currents vol. 5 (2013). doi: https://doi.org/10.1371/currents.outbreaks.22254b58675cdebc256dbe3c5aa6498b
Goh GK, Dunker AK, Uversky V. Prediction of Intrinsic Disorder in MERS-CoV/HCoV-EMC Supports a High Oral-Fecal Transmission. PLoS Curr. 2013 Nov 13;5. doi: 10.1371/currents.outbreaks.22254b58675cdebc256dbe3c5aa6498b. PMID: 24270586; PMCID: PMC3828228.
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On the intrinsic disorder status of the major players in programmed cell death pathways.

F1000Research

Uversky AV, Xue B, Peng Z, Kurgan L, Uversky VN.
PMID: 24358900
F1000Res. 2013 Sep 17;2:190. doi: 10.12688/f1000research.2-190.v1. eCollection 2013.

Earlier computational and bioinformatics analysis of several large protein datasets across 28 species showed that proteins involved in regulation and execution of programmed cell death (PCD) possess substantial amounts of intrinsic disorder. Based on the comprehensive analysis of these...

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Uversky AV, Xue B, Peng Z, et al. On the intrinsic disorder status of the major players in programmed cell death pathways. F1000Res. 2013;2:190doi: 10.12688/f1000research.2-190.v1.
Uversky, A. V., Xue, B., Peng, Z., Kurgan, L., & Uversky, V. N. (2013). On the intrinsic disorder status of the major players in programmed cell death pathways. F1000Research, 2190. https://doi.org/10.12688/f1000research.2-190.v1
Uversky, Alexey V, et al. "On the intrinsic disorder status of the major players in programmed cell death pathways." F1000Research vol. 2 (2013): 190. doi: https://doi.org/10.12688/f1000research.2-190.v1
Uversky AV, Xue B, Peng Z, Kurgan L, Uversky VN. On the intrinsic disorder status of the major players in programmed cell death pathways. F1000Res. 2013 Sep 17;2:190. doi: 10.12688/f1000research.2-190.v1. eCollection 2013. PMID: 24358900; PMCID: PMC3829196.
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Prediction of intrinsic disorder in proteins using MFDp2.

Methods in molecular biology (Clifton, N.J.)

Mizianty MJ, Uversky V, Kurgan L.
PMID: 24573480
Methods Mol Biol. 2014;1137:147-62. doi: 10.1007/978-1-4939-0366-5_11.

Intrinsically disordered proteins (IDPs) are either entirely disordered or contain disordered regions in their native state. IDPs were found to be abundant across all kingdoms of life, particularly in eukaryotes, and are implicated in numerous cellular processes. Experimental annotation...

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Mizianty MJ, Uversky V, Kurgan L. Prediction of intrinsic disorder in proteins using MFDp2. Methods Mol Biol. 2014;1137:147-62doi: 10.1007/978-1-4939-0366-5_11.
Mizianty, M. J., Uversky, V., & Kurgan, L. (2014). Prediction of intrinsic disorder in proteins using MFDp2. Methods in molecular biology (Clifton, N.J.), 1137147-62. https://doi.org/10.1007/978-1-4939-0366-5_11
Mizianty, Marcin J, et al. "Prediction of intrinsic disorder in proteins using MFDp2." Methods in molecular biology (Clifton, N.J.) vol. 1137 (2014): 147-62. doi: https://doi.org/10.1007/978-1-4939-0366-5_11
Mizianty MJ, Uversky V, Kurgan L. Prediction of intrinsic disorder in proteins using MFDp2. Methods Mol Biol. 2014;1137:147-62. doi: 10.1007/978-1-4939-0366-5_11. PMID: 24573480.
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MultIDIMensionality of IDIMs: intrinsic disorder in autoinhibition.

Structure (London, England : 1993)

Uversky VN.
PMID: 23473663
Structure. 2013 Mar 05;21(3):315-6. doi: 10.1016/j.str.2013.02.009.

Intrinsic disorder (ID) is crucial for the function of many proteins. The activity of some proteins is autoinhibited by their inhibitory modules (IMs). In this issue of Structure, Trudeau and colleagues showed multifarious roles of ID in controlling agility...

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Uversky VN. MultIDIMensionality of IDIMs: intrinsic disorder in autoinhibition. Structure. 2013;21(3):315-6doi: 10.1016/j.str.2013.02.009.
Uversky, V. N. (2013). MultIDIMensionality of IDIMs: intrinsic disorder in autoinhibition. Structure (London, England : 1993), 21(3), 315-6. https://doi.org/10.1016/j.str.2013.02.009
Uversky, Vladimir N. "MultIDIMensionality of IDIMs: intrinsic disorder in autoinhibition." Structure (London, England : 1993) vol. 21,3 (2013): 315-6. doi: https://doi.org/10.1016/j.str.2013.02.009
Uversky VN. MultIDIMensionality of IDIMs: intrinsic disorder in autoinhibition. Structure. 2013 Mar 05;21(3):315-6. doi: 10.1016/j.str.2013.02.009. PMID: 23473663.
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Malleable ribonucleoprotein machine: protein intrinsic disorder in the Saccharomyces cerevisiae spliceosome.

PeerJ

Coelho Ribeiro Mde L, Espinosa J, Islam S, Martinez O, Thanki JJ, Mazariegos S, Nguyen T, Larina M, Xue B, Uversky VN.
PMID: 23638354
PeerJ. 2013 Feb 12;1:e2. doi: 10.7717/peerj.2. Print 2013.

Recent studies revealed that a significant fraction of any given proteome is presented by proteins that do not have unique 3D structures as a whole or in significant parts. These intrinsically disordered proteins possess dramatic structural and functional variability,...

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Coelho Ribeiro Mde L, Espinosa J, Islam S, et al. Malleable ribonucleoprotein machine: protein intrinsic disorder in the Saccharomyces cerevisiae spliceosome. PeerJ. 2013;1:e2doi: 10.7717/peerj.2.
Coelho Ribeiro, M. d. e. . L., Espinosa, J., Islam, S., Martinez, O., Thanki, J. J., Mazariegos, S., Nguyen, T., Larina, M., Xue, B., & Uversky, V. N. (2013). Malleable ribonucleoprotein machine: protein intrinsic disorder in the Saccharomyces cerevisiae spliceosome. PeerJ, 1e2. https://doi.org/10.7717/peerj.2
Coelho Ribeiro, Maria de Lourdes, et al. "Malleable ribonucleoprotein machine: protein intrinsic disorder in the Saccharomyces cerevisiae spliceosome." PeerJ vol. 1 (2013): e2. doi: https://doi.org/10.7717/peerj.2
Coelho Ribeiro Mde L, Espinosa J, Islam S, Martinez O, Thanki JJ, Mazariegos S, Nguyen T, Larina M, Xue B, Uversky VN. Malleable ribonucleoprotein machine: protein intrinsic disorder in the Saccharomyces cerevisiae spliceosome. PeerJ. 2013 Feb 12;1:e2. doi: 10.7717/peerj.2. Print 2013. PMID: 23638354; PMCID: PMC3628832.
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Showing 1 to 12 of 185 entries