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Items: 1 to 20 of 98

1.

Caught in self-interaction: evolutionary and functional mechanisms of protein homooligomerization.

Hashimoto K, Nishi H, Bryant S, Panchenko AR.

Phys Biol. 2011 Jun;8(3):035007. doi: 10.1088/1478-3975/8/3/035007. Review.

2.

Evolutionary, physicochemical, and functional mechanisms of protein homooligomerization.

Nishi H, Hashimoto K, Madej T, Panchenko AR.

Prog Mol Biol Transl Sci. 2013;117:3-24. doi: 10.1016/B978-0-12-386931-9.00001-5. Review.

3.

Mechanisms of protein oligomerization, the critical role of insertions and deletions in maintaining different oligomeric states.

Hashimoto K, Panchenko AR.

Proc Natl Acad Sci U S A. 2010 Nov 23;107(47):20352-7. doi: 10.1073/pnas.1012999107.

4.

Prediction of protein-protein interactions: unifying evolution and structure at protein interfaces.

Tuncbag N, Gursoy A, Keskin O.

Phys Biol. 2011 Jun;8(3):035006. doi: 10.1088/1478-3975/8/3/035006. Review.

PMID:
21572173
5.

Macromolecular crowding: chemistry and physics meet biology (Ascona, Switzerland, 10-14 June 2012).

Foffi G, Pastore A, Piazza F, Temussi PA.

Phys Biol. 2013 Aug 2;10(4):040301. [Epub ahead of print]

PMID:
23912807
6.

Evolution of protein interactions: from interactomes to interfaces.

Andreani J, Guerois R.

Arch Biochem Biophys. 2014 Jul 15;554:65-75. doi: 10.1016/j.abb.2014.05.010. Review.

PMID:
24853495
7.

Joint evolutionary trees: a large-scale method to predict protein interfaces based on sequence sampling.

Engelen S, Trojan LA, Sacquin-Mora S, Lavery R, Carbone A.

PLoS Comput Biol. 2009 Jan;5(1):e1000267. doi: 10.1371/journal.pcbi.1000267.

8.

Oligomerization of G protein-coupled receptors: computational methods.

Selent J, Kaczor AA.

Curr Med Chem. 2011;18(30):4588-605. Review.

PMID:
21864281
9.

Evolutionary conservation in multiple faces of protein interaction.

Choi YS, Yang JS, Choi Y, Ryu SH, Kim S.

Proteins. 2009 Oct;77(1):14-25. doi: 10.1002/prot.22410.

PMID:
19350617
10.

The functional importance of co-evolving residues in proteins.

Sandler I, Zigdon N, Levy E, Aharoni A.

Cell Mol Life Sci. 2014 Feb;71(4):673-82. doi: 10.1007/s00018-013-1458-2. Review.

PMID:
23995987
11.

Oligomerisation status and evolutionary conservation of interfaces of protein structural domain superfamilies.

Sukhwal A, Sowdhamini R.

Mol Biosyst. 2013 Jul;9(7):1652-61. doi: 10.1039/c3mb25484d.

PMID:
23532342
12.
13.

Towards the prediction of protein interaction partners using physical docking.

Wass MN, Fuentes G, Pons C, Pazos F, Valencia A.

Mol Syst Biol. 2011 Feb 15;7:469. doi: 10.1038/msb.2011.3.

14.

The unfoldomics decade: an update on intrinsically disordered proteins.

Dunker AK, Oldfield CJ, Meng J, Romero P, Yang JY, Chen JW, Vacic V, Obradovic Z, Uversky VN.

BMC Genomics. 2008 Sep 16;9 Suppl 2:S1. doi: 10.1186/1471-2164-9-S2-S1.

15.

Probing the mutational interplay between primary and promiscuous protein functions: a computational-experimental approach.

Garcia-Seisdedos H, Ibarra-Molero B, Sanchez-Ruiz JM.

PLoS Comput Biol. 2012;8(6):e1002558. doi: 10.1371/journal.pcbi.1002558.

16.

Dimers, oligomers, everywhere.

Matthews JM, Sunde M.

Adv Exp Med Biol. 2012;747:1-18. doi: 10.1007/978-1-4614-3229-6_1. Review.

PMID:
22949108
17.

Structural, evolutionary, and assembly principles of protein oligomerization.

Levy ED, Teichmann S.

Prog Mol Biol Transl Sci. 2013;117:25-51. doi: 10.1016/B978-0-12-386931-9.00002-7. Review.

PMID:
23663964
18.

Protein interactions in 3D: from interface evolution to drug discovery.

Winter C, Henschel A, Tuukkanen A, Schroeder M.

J Struct Biol. 2012 Sep;179(3):347-58. doi: 10.1016/j.jsb.2012.04.009. Review.

PMID:
22595401
19.

Interplay between protein order, disorder and oligomericity in receptor signaling.

Sigalov AB.

Adv Exp Med Biol. 2012;725:50-73. doi: 10.1007/978-1-4614-0659-4_4.

PMID:
22399318
20.

Regulation of protein-protein binding by coupling between phosphorylation and intrinsic disorder: analysis of human protein complexes.

Nishi H, Fong JH, Chang C, Teichmann SA, Panchenko AR.

Mol Biosyst. 2013 Jul;9(7):1620-6. doi: 10.1039/c3mb25514j.

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