Structure of N-terminal domain of ZAP indicates how a zinc-finger protein recognizes complex RNA

Zinc-finger antiviral protein inhibits HIV-1 infection by selectively targeting multiply spliced viral mRNAs for degradation

(2011) Y. Zhu et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

ZAP-mediated mRNA degradation

(2011) Yiping Zhu et al.   RNA Biology

Features and development ofCoot

(2010) P. Emsley et al.   ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

PHENIX: a comprehensive Python-based system for macromolecular structure solution

(2010) Paul D. Adams et al.   ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

Identification of a Dominant Negative Inhibitor of Human Zinc Finger Antiviral Protein Reveals a Functional Endogenous Pool and Critical Homotypic Interactions

(2010) L. M. J. Law et al.   JOURNAL OF VIROLOGY

ZAPS is a potent stimulator of signaling mediated by the RNA helicase RIG-I during antiviral responses

(2010) Sumio Hayakawa et al.   NATURE IMMUNOLOGY

Structural insights into RNA recognition by the alternative-splicing regulator muscleblind-like MBNL1

(2008) Marianna Teplova et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

p72 DEAD box RNA helicase is required for optimal function of the zinc-finger antiviral protein

(2008) G. Chen et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA