Caged HIV-1 protease

Dimerization is independent of the ionization state of the active site aspartates

Glenn F. Short, Michiel Lodder, Andrei L. Laikhter, Tuncer Arslan, Sidney Hecht

Research output: Contribution to journalArticle

28 Citations (Scopus)
Original languageEnglish (US)
Pages (from-to)478-479
Number of pages2
JournalJournal of the American Chemical Society
Volume121
Issue number2
DOIs
StatePublished - Jan 20 1999
Externally publishedYes

Fingerprint

Dimerization
Aspartic Acid
Ionization
Catalytic Domain
Human immunodeficiency virus 1 p16 protease
Peptide Hydrolases

ASJC Scopus subject areas

  • Chemistry(all)

Cite this

Caged HIV-1 protease : Dimerization is independent of the ionization state of the active site aspartates. / Short, Glenn F.; Lodder, Michiel; Laikhter, Andrei L.; Arslan, Tuncer; Hecht, Sidney.

In: Journal of the American Chemical Society, Vol. 121, No. 2, 20.01.1999, p. 478-479.

Research output: Contribution to journalArticle

Short, Glenn F. ; Lodder, Michiel ; Laikhter, Andrei L. ; Arslan, Tuncer ; Hecht, Sidney. / Caged HIV-1 protease : Dimerization is independent of the ionization state of the active site aspartates. In: Journal of the American Chemical Society. 1999 ; Vol. 121, No. 2. pp. 478-479.
@article{0ee94e6dbbc547a597e59b5a5bed613b,
title = "Caged HIV-1 protease: Dimerization is independent of the ionization state of the active site aspartates",
author = "Short, {Glenn F.} and Michiel Lodder and Laikhter, {Andrei L.} and Tuncer Arslan and Sidney Hecht",
year = "1999",
month = "1",
day = "20",
doi = "10.1021/ja9838054",
language = "English (US)",
volume = "121",
pages = "478--479",
journal = "Journal of the American Chemical Society",
issn = "0002-7863",
publisher = "American Chemical Society",
number = "2",

}

TY - JOUR

T1 - Caged HIV-1 protease

T2 - Dimerization is independent of the ionization state of the active site aspartates

AU - Short, Glenn F.

AU - Lodder, Michiel

AU - Laikhter, Andrei L.

AU - Arslan, Tuncer

AU - Hecht, Sidney

PY - 1999/1/20

Y1 - 1999/1/20

UR - http://www.scopus.com/inward/record.url?scp=0033585614&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0033585614&partnerID=8YFLogxK

U2 - 10.1021/ja9838054

DO - 10.1021/ja9838054

M3 - Article

VL - 121

SP - 478

EP - 479

JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

SN - 0002-7863

IS - 2

ER -