Warning: Undefined array key "mm" in /www/wwwroot/www.ai-bt.com/si.php on line 10 Deprecated: trim(): Passing null to parameter #1 ($string) of type string is deprecated in /www/wwwroot/www.ai-bt.com/si.php on line 10 Successes and challenges with retroviral enzymes.

Literature DB >> 28132482

Successes and challenges with retroviral enzymes.

Anna Marie Skalka¹, Mark D Andrake¹, Richard A Katz¹.

Abstract

Collaborations between the Wlodawer and Skalka laboratories have covered a period of almost 30 years. During that time our groups have co-authored 18 publications, including several much cited journal articles, book chapters, and scholarly reviews. It has therefore been most rewarding for us to share enthusiasm, insights, and expertise with our Frederick colleagues over the years, and also to enjoy lasting friendships.

Entities: Chemical Disease Gene Mutation Species

Mesh：

Substances：
Retroviridae Proteins

Year: 2016 PMID： 28132482 PMCID： PMC6177231

Source DB: PubMed Journal: Postepy Biochem ISSN： 0032-5422

Keyword Cloud
References

29 in total

1. Retroviral integrase functions as a multimer and can turn over catalytically.

Authors: K S Jones; J Coleman; G W Merkel; T M Laue; A M Skalka
Journal: J Biol Chem Date: 1992-08-15 Impact factor: 5.157

2. Structural basis for inactivating mutations and pH-dependent activity of avian sarcoma virus integrase.

Authors: J Lubkowski; F Yang; J Alexandratos; G Merkel; R A Katz; K Gravuer; A M Skalka; A Wlodawer
Journal: J Biol Chem Date: 1998-12-04 Impact factor: 5.157

3. Synthetic peptides as substrates and inhibitors of a retroviral protease.

Authors: M Kotler; R A Katz; W Danho; J Leis; A M Skalka
Journal: Proc Natl Acad Sci U S A Date: 1988-06 Impact factor: 11.205

4. Multimerization determinants reside in both the catalytic core and C terminus of avian sarcoma virus integrase.

Authors: M D Andrake; A M Skalka
Journal: J Biol Chem Date: 1995-12-08 Impact factor: 5.157

5. Architecture of a full-length retroviral integrase monomer and dimer, revealed by small angle X-ray scattering and chemical cross-linking.

Authors: Ravi S Bojja; Mark D Andrake; Steven Weigand; George Merkel; Olya Yarychkivska; Adam Henderson; Marissa Kummerling; Anna Marie Skalka
Journal: J Biol Chem Date: 2011-03-15 Impact factor: 5.157

Successes and challenges with retroviral enzymes.

1. Retroviral integrase functions as a multimer and can turn over catalytically.

2. Structural basis for inactivating mutations and pH-dependent activity of avian sarcoma virus integrase.

3. Synthetic peptides as substrates and inhibitors of a retroviral protease.

4. Multimerization determinants reside in both the catalytic core and C terminus of avian sarcoma virus integrase.

5. Architecture of a full-length retroviral integrase monomer and dimer, revealed by small angle X-ray scattering and chemical cross-linking.

6. Architecture and assembly of HIV integrase multimers in the absence of DNA substrates.

7. Elucidation of the structure of retroviral proteases: a reminiscence.

Review 8. Oligonucleotide-based assays for integrase activity.

9. High-resolution structure of the catalytic domain of avian sarcoma virus integrase.

10. Crystal structure of the Rous sarcoma virus intasome.