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Cited by 199

The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.

Inhibitor and NAD+ Binding to Poly(ADP-ribose) Polymerase As Derived from Crystal Structures and Homology Modeling,

Ruf, Armin, de Murcia, Gilbert, Schulz, Georg E.·1998·Biochemistry

Abstract

Inhibitors of poly(ADP-ribose) polymerase (PARP, EC 2.4.2.30) are of clinical interest because they have potential for improving radiation therapy and chemotherapy of cancer. The refined binding structures of four such inhibitors are reported together with the refined structure of the unligated catalytic fragment of the enzyme. Following their design, all inhibitors bind at the position of the nicotinamide moiety of the substrate NAD+. The observed binding mode suggests inhibitor improvements that avoid other NAD(+)-binding enzymes. Because the binding pocket of NAD+ has been strongly conserved during evolution, the homology with ADP-ribosylating bacterial toxins could be used to extend the bound nicotinamide, which is marked by the inhibitors, to the full NAD+ molecule.

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Metadata

Authors
Ruf, A., de Murcia, G., & Schulz, G. E.
Venue
Biochemistry
Published
1998-02-26
Volume
37
Issue
11
Pages
3893-3900
ISSN
  • 0006-2960 (ISSN-L)
  • 1520-4995
OpenAlex
W2146501567
Cited by
199
References
2
FWCI
1.27
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Inhibitor and NAD+ Binding to Poly(ADP-ribose) Polymerase As Derived from Crystal Structures and Homology Modeling,. https://app.cochat.ai/papers/10.1021/bi972383s
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Ruf, A., de Murcia, G., & Schulz, G. E. (1998). Inhibitor and NAD+ Binding to Poly(ADP-ribose) Polymerase As Derived from Crystal Structures and Homology Modeling,. Biochemistry. https://doi.org/10.1021/bi972383s

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