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3-nitro-2-pyridinesulfenyl

Known as: 3-nitro-2-pyridinesulfenyl chloride, Npys, Npys-Cl 
National Institutes of Health

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Broader (1)

Pyridines

Papers overview

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Highly Cited
2009
Highly Cited
2009
3-nitro-2-pyridinesulfenyl (Npys) group. A novel selective protecting group which can be activated for peptide bond formation.
The novel 3-nitro-2-pyridinesulfenyl (Npys) group, which is useful for the protection and the activation of amino and hydroxyl… 
Highly Cited
2009
Highly Cited
2009
Use of the Npys thiol protection in solid phase peptide synthesis. Application to direct peptide-protein conjugation through cysteine residues.
The protection of the thiol function of cysteine with the 3-nitro-2-pyridylsulfenyl (Npys) group has been successfully applied in… 
2009
2009
Controlled peptide-protein conjugation by means of 3-nitro-2-pyridinesulfenyl protection-activation.
The disulfide bond in S-3-nitro-2-pyridinesulfenyl (S-Npys) compounds is stable towards the acid treatment used in solid-phase… 
2009
2009
Sulfur protection with the 3-nitro-2-pyridine sulfenyl group in solid-phase peptide synthesis.
The 3-nitro-2-pyridinesulfenyl (Npys) group has been used successfully for side chain protection of cysteine during the stepwise… 
2002
2002
The direct stimulation of Gi proteins by neuropeptide Y (NPY) in the rat left ventricle.
Review
2001
Review
2001
Discriminative disulfide-bonding affinity labeling of opioid receptor subtypes.
1992
1992
Compatibility of the S-(3-nitro-2-pyridinesulfenyl) protecting group with DCC/HOBt coupling chemistry.
Two recent reports on the partial lability of the 3-nitro-2-pyridinesulfenyl (Npys) thiol protecting group towards 1-hydroxy… 
1990
1990
Plasmin-induced platelet aggregation is accompanied by cleavage of aggregin and indirectly mediated by calpain.
We recently reported that thrombin-induced platelet aggregation 1) is accompanied by cleavage of aggregin, a 100-kDa membrane… 
1989
1989
A synthetic strategy for simultaneous purification-conjugation of antigenic peptides.
Highly Cited
1982
Highly Cited
1982
Modification of the catalytic subunit of bovine heart cAMP-dependent protein kinase with affinity labels related to peptide substrates.
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