Identifying selective inhibitors against the human cytosolic sialidase NEU2 by substrate specificity studies

Yanhong Li; Hongzhi Cao; Hai Yu; Yi Chen; Kam Lau; Jingyao Qu; Vireak Thon; Go Sugiarto; Xi Chen

doi:10.1039/c0mb00244e

Identifying selective inhibitors against the human cytosolic sialidase NEU2 by substrate specificity studies

Molecular BioSystems ◽

10.1039/c0mb00244e ◽

2011 ◽

Vol 7 (4) ◽

pp. 1060 ◽

Cited By ~ 41

Author(s):

Yanhong Li ◽

Hongzhi Cao ◽

Hai Yu ◽

Yi Chen ◽

Kam Lau ◽

...

Keyword(s):

Substrate Specificity ◽

Selective Inhibitors ◽

Cytosolic Sialidase

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Substrate Specificity and Kinetic Studies of PADs 1, 3, and 4 Identify Potent and Selective Inhibitors of Protein Arginine Deiminase 3

Biochemistry ◽

10.1021/bi100363t ◽

2010 ◽

Vol 49 (23) ◽

pp. 4852-4863 ◽

Cited By ~ 97

Author(s):

Bryan Knuckley ◽

Corey P. Causey ◽

Justin E. Jones ◽

Monica Bhatia ◽

Christina J. Dreyton ◽

...

Keyword(s):

Substrate Specificity ◽

Kinetic Studies ◽

Arginine Deiminase ◽

Selective Inhibitors ◽

Protein Arginine Deiminase

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Substrate Specificity and Novel Selective Inhibitors of TNF-α Converting Enzyme (TACE) from Two-Dimensional Substrate Mapping

Combinatorial Chemistry & High Throughput Screening ◽

10.2174/1386207054020840 ◽

2005 ◽

Vol 8 (4) ◽

pp. 327-339 ◽

Cited By ~ 21

Author(s):

Millard Lambert ◽

R. Blackburn ◽

Theresa Seaton ◽

Daniel Kassel ◽

Daniel Kinder ◽

...

Keyword(s):

Substrate Specificity ◽

Two Dimensional ◽

Converting Enzyme ◽

Selective Inhibitors

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Synthesis of selective inhibitors against V. cholerae sialidase and human cytosolic sialidase NEU2

Organic & Biomolecular Chemistry ◽

10.1039/c2ob25335f ◽

2012 ◽

Vol 10 (30) ◽

pp. 6112 ◽

Cited By ~ 15

Author(s):

Zahra Khedri ◽

Yanhong Li ◽

Hongzhi Cao ◽

Jingyao Qu ◽

Hai Yu ◽

...

Keyword(s):

Selective Inhibitors ◽

Cytosolic Sialidase

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Rat-liver lysosomal sialidase. Solubilization, substrate specificity and comparison with the cytosolic sialidase

European Journal of Biochemistry ◽

10.1111/j.1432-1033.1984.tb08159.x ◽

1984 ◽

Vol 141 (1) ◽

pp. 75-81 ◽

Cited By ~ 80

Author(s):

Taeko MIYAGI ◽

Shigeru TSUIKI

Keyword(s):

Substrate Specificity ◽

Rat Liver ◽

Cytosolic Sialidase ◽

Lysosomal Sialidase

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Substrate specificity and inducibility of TACE (tumour necrosis factor α-converting enzyme) revisited: the Ala-Val preference, and induced intrinsic activity

Biochemical Society Symposium ◽

10.1042/bss0700039 ◽

2003 ◽

Vol 70 ◽

pp. 39-52 ◽

Cited By ~ 54

Author(s):

Roy A. Black ◽

John R. Doedens ◽

Rajeev Mahimkar ◽

Richard Johnson ◽

Lin Guo ◽

...

Keyword(s):

Substrate Specificity ◽

Recent Work ◽

Tumour Necrosis Factor ◽

Tumour Necrosis ◽

Transforming Growth Factor ◽

Intrinsic Activity ◽

Converting Enzyme ◽

Tumour Necrosis Factor Α ◽

Factor Α ◽

Necrosis Factor

Tumour necrosis factor α (TNFα)-converting enzyme (TACE/ADAM-17, where ADAM stands for a disintegrin and metalloproteinase) releases from the cell surface the extracellular domains of TNF and several other proteins. Previous studies have found that, while purified TACE preferentially cleaves peptides representing the processing sites in TNF and transforming growth factor α, the cellular enzyme nonetheless also sheds proteins with divergent cleavage sites very efficiently. More recent work, identifying the cleavage site in the p75 TNF receptor, quantifying the susceptibility of additional peptides to cleavage by TACE and identifying additional protein substrates, underlines the complexity of TACE-substrate interactions. In addition to substrate specificity, the mechanism underlying the increased rate of shedding caused by agents that activate cells remains poorly understood. Recent work in this area, utilizing a peptide substrate as a probe for cellular TACE activity, indicates that the intrinsic activity of the enzyme is somehow increased.

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