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neils's Jang [3 articles]

 
Recent papers posted to neils's library by the author Jang. You can also see everyone's Jang.
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The Protein Interaction Network of Extracellular Vesicles Derived from Human Colorectal Cancer Cells

  [CiTO]
J. Proteome Res. In Journal of Proteome Research, Vol. 11, No. 2. (13 December 2011), pp. 1144-1151, doi:10.1021/pr200842h

Abstract

Various mammalian cells including tumor cells secrete extracellular vesicles (EVs), otherwise known as exosomes and microvesicles. EVs are nanosized bilayered proteolipids and play multiple roles in intercellular communication. Although many vesicular proteins have been identified, their functional interrelationships and the mechanisms of EV biogenesis remain unknown. By interrogating proteomic data using systems approaches, we have created a protein interaction network of human colorectal cancer cell-derived EVs which comprises 1491 interactions between 957 vesicular proteins. We discovered that EVs have well-connected clusters ...

 

Protein complex prediction based on simultaneous protein interaction network

  [CiTO]
Bioinformatics In Bioinformatics, Vol. 26, No. 3. (1 February 2010), pp. 385-391, doi:10.1093/bioinformatics/btp668
posted to clustering complex interaction network prediction protein-protein by neils  on 2010-02-03 00:11:36 ** along with 10 people cabbagesofdoom dakelley ess30 fleurxq guhjy jjray johanneskoester phoenixzxl poirel zwang

Abstract

Motivation: The increase in the amount of available protein-protein interaction (PPI) data enables us to develop computational methods for protein complex predictions. A protein complex is a group of proteins that interact with each other at the same time and place. The protein complex generally corresponds to a cluster in PPI network (PPIN). However, clusters correspond not only to protein complexes but also to sets of proteins that interact dynamically with each other. As a result, conventional graph-theoretic clustering methods that ...

 

How to lose a kink and gain a helix: pH independent conformational changes of the fusion domains from influenza hemagglutinin in heterogeneous lipid bilayers

  [CiTO]
Proteins: Structure, Function, and Bioinformatics, Vol. 9999, No. 9999. (2008), NA, doi:10.1002/prot.21925

Abstract

We have simulated two conformations of the fusion domain of influenza hemagglutinin (HA) within explicit water, salt, and heterogeneous lipid bilayers composed of POPC:POPG (4:1). Each conformation has seven different starting points in which the initial peptide structure is the same for each conformation, but the location across the membrane normal and lipid arrangement around the peptide are varied, giving a combined total simulation time of 140 ns. For the HA5 conformation (primary structure from recent NMR spectroscopy at pH = ...

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