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Mowei Zhou

Researcher at Environmental Molecular Sciences Laboratory

Publications -  79
Citations -  1405

Mowei Zhou is an academic researcher from Environmental Molecular Sciences Laboratory. The author has contributed to research in topics: Medicine & Chemistry. The author has an hindex of 18, co-authored 50 publications receiving 982 citations. Previous affiliations of Mowei Zhou include Center for Drug Evaluation and Research & Pacific Northwest National Laboratory.

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Informed-Proteomics: open-source software package for top-down proteomics

TL;DR: Informed-Proteomics is presented, an open-source software suite for top-down proteomics analysis that consists of an LC-MS feature-finding algorithm, a database search algorithm, and an interactive results viewer that is compared with several other popular tools using human-in-mouse xenograft luminal and basal breast tumor samples.
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Surface Induced Dissociation: Dissecting Noncovalent Protein Complexes in the Gas phase

TL;DR: This work has shown that SID can be a complementary gas-phase tool providing useful information for studying quaternary structures of noncovalent protein complexes, with emphasis on the more recent work on the combination of ion mobility (IM) with SID.
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Protein Subunits Released by Surface Collisions of Noncovalent Complexes: Nativelike Compact Structures Revealed by Ion Mobility Mass Spectrometry

TL;DR: Zhou et al. as discussed by the authors presented the first IM measurements on the SID products of several protein complexes, along with comparison to CID products, by using a modified quadrupole/IM/time offlight (Q/IM)/TOF) instrument.
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Dissecting the large noncovalent protein complex GroEL with surface-induced dissociation and ion mobility-mass spectrometry.

TL;DR: SID can be very useful for quaternary structure studies of large noncovalent protein complexes, as manifested by the GroEL data where the tetradecamer dissociates into heptamers, reflecting the native topology of the complex.
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Impact of charge state on gas-phase behaviors of noncovalent protein complexes in collision induced dissociation and surface induced dissociation

TL;DR: The data presented here suggest that charge manipulation can be used to "tune" the dissociation behavior of noncovalent protein complexes in order to obtain the most useful information desired for structural analysis.