scispace - formally typeset
B

Bryan R. Cullen

Researcher at Duke University

Publications -  376
Citations -  52946

Bryan R. Cullen is an academic researcher from Duke University. The author has contributed to research in topics: RNA & Gene. The author has an hindex of 121, co-authored 371 publications receiving 50901 citations. Previous affiliations of Bryan R. Cullen include Hoffmann-La Roche & University of Medicine and Dentistry of New Jersey.

Papers
More filters
Journal ArticleDOI

Two Closely Related Human Nuclear Export Factors Utilize Entirely Distinct Export Pathways

TL;DR: It is demonstrated that NXF3, a human RNA binding protein related to TAP, lacks a carboxy-terminal domain yet retains the ability to export tethered RNA transcripts and to shuttle between the nucleus and the cytoplasm.
Journal ArticleDOI

Is RNA interference a physiologically relevant innate antiviral immune response in mammals

TL;DR: Three recent papers provide evidence that either favors or challenges the antiviral role of RNA interference in mammals, and are discussed in the context of previous research.
Journal ArticleDOI

Amphibian transcription factor iiia proteins contain a sequence element functionally equivalent to the nuclear export signal of human immunodeficiency virus type 1 rev

TL;DR: It is reported that amphibian TFIIIA proteins contain a sequence element with homology to the Rev activation domain that effectively substitutes for this domain in inducing the nuclear export of late HIV-1 mRNAs and 5S rRNA transcripts.
Journal ArticleDOI

The VP16 transcription activation domain is functional when targeted to a promoter-proximal RNA sequence.

TL;DR: It is suggested that VP16, like Tat, can act on steps subsequent to the formation of the HIV-1 LTR preinitiation complex and the finding that the activation domains of VP16 and Tat are functionally interchangeable raises the possibility that these apparently disparate viral trans-activators may nevertheless act via similar mechanisms.
Journal ArticleDOI

Mutational analysis of the transcription activation domain of RelA: identification of a highly synergistic minimal acidic activation module.

TL;DR: The data demonstrate that the biological activity of the RelA activation domain is dependent on acidic activator sequences that are closely comparable to those detected in the activation domain of the viral VP16 regulatory protein.