Skip to search form
Skip to main content
Skip to account menu
Semantic Scholar
Semantic Scholar's Logo
Search 225,190,171 papers from all fields of science
Search
Sign In
Create Free Account
ALOX5AP gene
Known as:
FLAP
, MK-886-binding protein
, ALOX5AP
Expand
National Institutes of Health
Create Alert
Alert
Related topics
Related topics
2 relations
5-Lipoxygenase-Activating Proteins
ALOXE3 gene
Papers overview
Semantic Scholar uses AI to extract papers important to this topic.
2012
2012
Transplantation of engineered cardiac muscle flaps in syngeneic rats.
R. Tee
,
W. Morrison
,
+4 authors
R. Dilley
Tissue Engineering. Part A
2012
Corpus ID: 24794332
Cardiac tissue engineering offers the prospect of a novel treatment for acquired or congenital heart defects. Previously, our…
Expand
Highly Cited
2009
Highly Cited
2009
ACTIVE AERODYNAMIC BLADE CONTROL DESIGN FOR LOAD REDUCTION ON LARGE WIND TURBINES
D. Wilson
,
D. Berg
,
M. Barone
,
J. Berg
,
B. Resor
,
D. Lobitz
2009
Corpus ID: 54766577
Through numerical simulations that use trailing edge flaps as active aerodynamic load control devices on wind turbines that range…
Expand
Highly Cited
2006
Highly Cited
2006
Closing of the flaps of HIV-1 protease induced by substrate binding: a model of a flap closing mechanism in retroviral aspartic proteases.
G. Tóth
,
A. Borics
Biochemistry
2006
Corpus ID: 38037119
The active site of aspartic proteases is covered by one or more flaps, which control access to the active site and play a…
Expand
Highly Cited
2002
Highly Cited
2002
Use of a lentiviral flap vector for induction of CTL immunity against melanoma. Perspectives for immunotherapy
H. Firat
,
Véronique Zennou
,
+6 authors
P. Charneau
Journal of Gene Medicine
2002
Corpus ID: 12069228
A central triple‐stranded DNA structure created during HIV‐1 reverse transcription, the central flap, acts as a cis‐active…
Expand
2000
2000
Dynamics of the metallo-beta-lactamase from Bacteroides fragilis in the presence and absence of a tight-binding inhibitor.
J. J. Huntley
,
S. Scrofani
,
M. J. Osborne
,
P. Wright
,
H. Dyson
Biochemistry
2000
Corpus ID: 30011335
A significant determinant for the broad substrate specificity of the metallo-beta-lactamases from Bacteroides fragilis and other…
Expand
1998
1998
Partial Functional Deficiency of E160D Flap Endonuclease-1 Mutantin Vitro and in Vivo Is Due to Defective Cleavage of DNA Substrates*
Geoffrey Frank
,
J. Qiu
,
+4 authors
B. Shen
Journal of Biological Chemistry
1998
Corpus ID: 39661350
To assess the roles of the active site residues Glu160 and Asp181 of human FEN-1 nuclease in binding and catalysis of the flap…
Expand
Review
1997
Review
1997
Design of a high-efficiency discrete servo-flap actuator for helicopter rotor control
E. Prechtl
,
S. Hall
Smart Structures
1997
Corpus ID: 110193538
Discrete trailing edge servo-flap actuator designs for use in rotor control applications are considered. A survey was conducted…
Expand
Highly Cited
1996
Highly Cited
1996
Kinetic analysis of human flap endonuclease-1 by flow cytometry.
J. Nolan
,
B. Shen
,
M. Park
,
L. Sklar
Biochemistry
1996
Corpus ID: 38803831
Human flap endonuclease-1 (FEN-1) is a structure-specific endonuclease and exonuclease which is essential for DNA replication and…
Expand
Highly Cited
1994
Highly Cited
1994
Induced strain actuation of composite beams and rotor blades with embedded piezoceramic elements
Peter C. Chen
,
I. Chopra
Smart Structures
1994
Corpus ID: 117566527
The objective of this research is to develop a dynamically scaled (Froude scale) helicopter rotor blade with embedded…
Expand
Highly Cited
1993
Highly Cited
1993
Feasibility study to build a smart rotor: trailing edge flap actuation
D. Samak
,
I. Chopra
Smart Structures
1993
Corpus ID: 109719820
This paper presents an experimental study on the development of a Froude scale helicopter rotor blade with trailing edge flap as…
Expand
By clicking accept or continuing to use the site, you agree to the terms outlined in our
Privacy Policy
(opens in a new tab)
,
Terms of Service
(opens in a new tab)
, and
Dataset License
(opens in a new tab)
ACCEPT & CONTINUE