Mass spectrometric analysis of the HIV-1 integrase-pyridoxal 5'-phosphate complex reveals a new binding site for a nucleotide inhibitor.
about
New Class of HIV-1 Integrase (IN) Inhibitors with a Dual Mode of ActionVinylogous ureas as a novel class of inhibitors of reverse transcriptase-associated ribonuclease H activityHIV-1 IN inhibitors: 2010 update and perspectivesDiscovery of a small-molecule HIV-1 integrase inhibitor-binding siteAllosteric inhibitor development targeting HIV-1 integrase.Interaction between Reverse Transcriptase and Integrase Is Required for Reverse Transcription during HIV-1 Replication.Probing conformational changes of human DNA polymerase lambda using mass spectrometry-based protein footprintingHIV-1 Integrase-DNA Recognition Mechanisms.Prospective strategies for targeting HIV-1 integrase function.Inactivation of NEIL2 DNA glycosylase by pyridoxal phosphate reveals a loop important for substrate binding.Mechanistic and pharmacological analyses of HIV-1 integration.Identification of pyridoxal phosphate modified proteins using mass spectrometry.
P2860
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P2860
Mass spectrometric analysis of the HIV-1 integrase-pyridoxal 5'-phosphate complex reveals a new binding site for a nucleotide inhibitor.
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name
Mass spectrometric analysis of ...... te for a nucleotide inhibitor.
@en
type
label
Mass spectrometric analysis of ...... te for a nucleotide inhibitor.
@en
prefLabel
Mass spectrometric analysis of ...... te for a nucleotide inhibitor.
@en
P2093
P2860
P356
P1476
Mass spectrometric analysis of ...... ite for a nucleotide inhibitor
@en
P2093
Kerry L Williams
Mamuka Kvaratskhelia
Nana Kotrikadze
Nick Shkriabai
Rajeshri G Karki
Robert Craigie
Sonja Hess
Stuart F J Le Grice
Yijun Zhang
P2860
P304
P356
10.1074/JBC.M413579200
P407
P577
2004-12-22T00:00:00Z