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Wei-Chiang Shen

Researcher at National Taiwan University

Publications -  181
Citations -  12102

Wei-Chiang Shen is an academic researcher from National Taiwan University. The author has contributed to research in topics: Fusion protein & Transferrin. The author has an hindex of 44, co-authored 175 publications receiving 10528 citations. Previous affiliations of Wei-Chiang Shen include Harvard University & Tufts University.

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Journal ArticleDOI

Guidelines for the use and interpretation of assays for monitoring autophagy

Daniel J. Klionsky, +1287 more
- 01 Apr 2012 - 
TL;DR: These guidelines are presented for the selection and interpretation of methods for use by investigators who aim to examine macroautophagy and related processes, as well as for reviewers who need to provide realistic and reasonable critiques of papers that are focused on these processes.
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Fusion protein linkers: Property, design and functionality

Xiaoying Chen, +2 more
- 15 Oct 2013 - 
TL;DR: This review covers the current knowledge of fusion protein linkers and summarizes examples for their design and application and considers the general properties of linkers derived from naturally-occurring multi-domain proteins as the foundation in linker design.
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Cell Penetrating Peptides: Intracellular Pathways and Pharmaceutical Perspectives

Leena N. Patel, +2 more
- 19 Apr 2007 - 
TL;DR: Some of the methodology concerns are highlighted, focus more on the internalization pathway and a novel perspective about the intracellular processing of CPPs is provided, which is a crucial aspect to consider when selecting a cell penetrating peptide as a drug delivery system.
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Cis-aconityl spacer between daunomycin and macromolecular carriers: A model of pH-sensitive linkage releasing drug from a lysosomotropic conjugate

Wei-Chiang Shen, +1 more
- 15 Oct 1981 - 
TL;DR: It is concluded that unlike the Affi-Gel conjugate, N- cis -aconityl daunomycin-poly(D-lysine) enters cells and reaches the lysosomal compartment, and that the cis -aconsityl spacer releases dauncycin from poly(D -lysine] in the acidic milieu of lysOSomes due to the participation of a free cis -carboxylic group.
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Cleavage of disulfide bonds in endocytosed macromolecules. A processing not associated with lysosomes or endosomes.

E. P. Feener, +2 more
- 05 Nov 1990 - 
TL;DR: Subcellular fractionation and kinetic analysis indicated that neither lysosomes nor endosomes were participating in that phase, leaving the Golgi apparatus as the most probable site of endocytic disulfide cleavage.