The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

Editor

Share

Personal info

View

Links

Table of contents

About

Terms

 

Chemical Compound Review: 

SureCN95324     1-[4-(2,5-dioxopyrrol-1- yl)phenyl]pyrrole...

Synonyms: CHEMBL576594, P23989_ALDRICH, AG-E-98394, AG-J-58149, ACMC-209hvr, ...
 
 
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.
 

High impact information on NSC 81257

  • In the present study, we tested this prediction by using either unmodified S-1 or S-1 chemically modified with N,N'-p-phenylenedimaleimide (pPDM X S-1) so that functionally it acts like S-1.ATP, although it does not hydrolyze ATP [1].
  • Using the pyrene-labeled Mg forms of yeast and muscle actins, we demonstrate that under low ionic strength conditions, P.IB causes formation of filamentous actin assemblies, although they, unlike F-actin, cannot be internally cross-linked with N,N'-4-phenylenedimaleimide (PDM) [2].
  • Rate constants for the reactions of Cys-697 and Cys-707 of skeletal muscle myosin subfragment 1 (S1) with N,N'-p-phenylenedimaleimide (pPDM) and its monofunctional analog phenylmaleimide (PM) were measured for S1 and S1 bound to nucleotides and/or actin [3].
  • NANDP was trapped in nearly stoichiometric amounts at the active site by cross-linking SH1 and SH2 with N,N'-p-phenylenedimaleimide (pPDM) or by chelation with cobalt (III) phenanthroline [Wells, J., & Yount, R. (1979) Proc. Natl. Acad. Sci. U.S.A. 76, 4966] [4].
  • The effect of N,N'-p-phenylenedimaleimide (PMD) on deoxygenation-induced K loss in sickle erythrocytes [5].
 

Analytical, diagnostic and therapeutic context of NSC 81257

References

  1. Regulation of actomyosin ATPase activity by troponin-tropomyosin: effect of the binding of the myosin subfragment 1 (S-1).ATP complex. Greene, L.E., Williams, D.L., Eisenberg, E. Proc. Natl. Acad. Sci. U.S.A. (1987) [Pubmed]
  2. Interaction of the gonococcal porin P.IB with G- and F-actin. Wen, K.K., Giardina, P.C., Blake, M.S., Edwards, J., Apicella, M.A., Rubenstein, P.A. Biochemistry (2000) [Pubmed]
  3. Kinetic investigation of the ligand dependence of rabbit skeletal muscle myosin subfragment 1 Cys-697 and Cys-707 reactivities. Polosukhina, K., Highsmith, S. Biochemistry (1997) [Pubmed]
  4. 2-[(4-Azido-2-nitrophenyl)amino]ethyl triphosphate, a novel chromophoric and photoaffinity analogue of ATP. Synthesis, characterization, and interaction with myosin subfragment 1. Nakamaye, K.L., Wells, J.A., Bridenbaugh, R.L., Okamoto, Y., Yount, R.G. Biochemistry (1985) [Pubmed]
  5. The effect of N,N'-p-phenylenedimaleimide (PMD) on deoxygenation-induced K loss in sickle erythrocytes. Wall, S.N., Berkowitz, L.R. Am. J. Med. Sci. (1987) [Pubmed]
  6. Changes in the thermal unfolding of p-phenylenedimaleimide-modified myosin subfragment 1 induced by its 'weak' binding to F-actin. Kaspieva, O.V., Nikolaeva, O.P., Orlov, V.N., Ponomarev, M.A., Drachev, V.A., Levitsky, D.I. FEBS Lett. (2001) [Pubmed]
Contributions to this collaborative article are from individual authors of WikiGenes or mined by the WikiGenes Data Mining Engine from MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.About WikiGenesOpen Access LicencePrivacy PolicyTerms of Useapsburg
 
WikiGenes - Universities