Language
English
German
^M
Dutch
Spanish
Title:
Cellular location and activity of Escherichia coli RecG proteins shed light on the function of its structurally unresolved C-terminus
Source:
Nucleic Acids Research [0305-1048] Upton, A L yr:2014
Basic
Full text
Full text available via
PubMed Central
Year:
Volume:
Issue:
Start Page:
Document delivery
Request document via
Library/Bibliothek
Users interested in this article also expressed an interest in the following:
description
1.
Gandía Herrero, F.
"Escherichia coli protein YgiD produces the structural unit of plant pigments betalains: characterization of a prokaryotic enzyme with DOPA-extradiol-dioxygenase activity."
Applied Microbiology and Biotechnology
98.3 (2014): 1165-74.
description
2.
Boo, H.
"Extraction and characterization of some natural plant pigments.(Report)."
Industrial crops and products
40 (2012): 129-.
description
3.
Gandía Herrero, F.
"Biosynthesis of betalains: yellow and violet plant pigments."
Trends in plant science
18.6 (2013): 334-343.
description
4.
Garrity, Steven R.
"Disentangling the relationships between plant pigments and the photochemical reflectance index reveals a new approach for remote estimation of carotenoid content."
Remote sensing of environment
115.2 (2011): 628-635.
Select All
Clear All
Save Citations
Select Format
ProCite
Reference Manager
EndNote
RefWorks
Submit citation export
Advanced
Author
Other articles by this author? -- in
GeoRef
author:
Upton, A L
last name
initials
Other articles by this author? -- in
Online Contents Geosciences
author:
Upton, A L
last name
initials
Other articles by this author? -- using
Web of Science
author:
Upton, A L
last name
initials
Web Search
Find related information in
a Web Search Engine
Excite
Google
HotBot
Ixquick
ZOO
Ask
Yahoo!
Bing
Naver
Search Terms:
Search for related information in
Google Scholar
Article Title
Author Name
Journal Title
Other Search
Search Terms:
A service provided by the
Library of the Wissenschaftspark Albert Einstein
, Potsdam, Germany.
© 2005 SFX by Ex Libris Inc.