Author: bugman
Date: Tue Aug 28 19:33:25 2012
New Revision: 17367
URL: http://svn.gna.org/viewcvs/relax?rev=17367&view=rev
Log:
Added and fixed DOI numbers for many bibliographic entries.
Modified:
trunk/docs/latex/bibliography.bib
Modified: trunk/docs/latex/bibliography.bib
URL:
http://svn.gna.org/viewcvs/relax/trunk/docs/latex/bibliography.bib?rev=17367&r1=17366&r2=17367&view=diff
==============================================================================
--- trunk/docs/latex/bibliography.bib (original)
+++ trunk/docs/latex/bibliography.bib Tue Aug 28 19:33:25 2012
@@ -163,6 +163,7 @@
Support, Non-U.S. Gov't ; Research Support, U.S. Gov't,
P.H.S. ; Rotation},
language = {eng},
+ doi = {10.1006/jmre.2000.2113},
medline-aid = {10.1006/jmre.2000.2113 [doi] ; S109078070092113X [pii]},
medline-ci = {Copyright 2000 Academic Press.},
medline-da = {20001025},
@@ -235,6 +236,7 @@
Support, Non-U.S. Gov't ; Research Support, U.S. Gov't,
P.H.S.},
language = {eng},
+ doi = {10.1006/jmre.1999.1839},
medline-aid = {10.1006/jmre.1999.1839 [doi] ; S1090780799918396 [pii]},
medline-ci = {Copyright 1999 Academic Press.},
medline-da = {20000316},
@@ -315,6 +317,7 @@
Sequence Alignment ; *Signal Transduction ;
Thermodynamics ; Titrimetry},
language = {eng},
+ doi = {10.1016/S0022-2836(02)00282-6},
medline-aid = {10.1016/S0022-2836(02)00282-6 [doi] ;
S0022-2836(02)00282-6 [pii]},
medline-ci = {(c) 2002 Elsevier Science Ltd.},
@@ -435,7 +438,7 @@
volume = {50},
issue = {2},
url = {http://dx.doi.org/10.1007/s10858-011-9509-1},
- note = {10.1007/s10858-011-9509-1},
+ doi = {10.1007/s10858-011-9509-1},
abstract = {Investigation of protein dynamics on the ps-ns and μs-ms
timeframes provides detailed insight into the mechanisms of enzymes and the
binding properties of proteins. Nuclear magnetic resonance (NMR) is an
excellent tool for studying protein dynamics at atomic resolution. Analysis
of relaxation data using model-free analysis can be a tedious and time
consuming process, which requires good knowledge of scripting procedures. The
software relaxGUI was developed for fast and simple model-free analysis and
is fully integrated into the software package relax. It is written in Python
and uses wxPython to build the graphical user interface (GUI) for maximum
performance and multi-platform use. This software allows the analysis of NMR
relaxation data with ease and the generation of publication quality graphs as
well as color coded images of molecular structures. The interface is designed
for simple data analysis and management. The software was tested and
validated against the command line version of relax.},
year = {2011}
}
@@ -615,6 +618,7 @@
P.H.S. ; *Saccharomyces cerevisiae Proteins ;
Temperature},
language = {eng},
+ doi = {S0022-2836(98)92429-9},
medline-aid = {S0022-2836(98)92429-9 [pii] ; 10.1006/jmbi.1998.2429
[doi]},
medline-ci = {Copyright 1999 Academic Press Limited.},
@@ -876,6 +880,7 @@
Thymus/chemistry/*metabolism ; Sequence Homology, Amino
Acid ; Thermus thermophilus/enzymology},
language = {eng},
+ doi = {10.1016/j.jmb.2004.03.055},
medline-aid = {10.1016/j.jmb.2004.03.055 [doi] ; S0022283604003572
[pii]},
medline-da = {20040528},
@@ -964,6 +969,7 @@
; Research Support, U.S. Gov't, P.H.S. ; Software ;
Tetrahydrofolate Dehydrogenase/chemistry ; Time Factors},
language = {eng},
+ doi = {10.1023/b:jnmr.0000032504.70912.58},
medline-aid = {10.1023/B:JNMR.0000032504.70912.58 [doi] ; 5266056
[pii]},
medline-da = {20040623},
@@ -1122,7 +1128,8 @@
publisher = {Amer Chemical Soc},
size = {3 p.},
sourceid = {ISI:A1990DH27700070},
- year = 1990
+ year = 1990,
+ doi = {10.1021/ja00168a070}
}
@Article{Cordier98,
@@ -1221,7 +1228,8 @@
School = {Biochemistry and Molecular Biology, University of
Melbourne.
http://eprints.infodiv.unimelb.edu.au/archive/00002799/},
url = {http://eprints.infodiv.unimelb.edu.au/archive/00002799/},
- year = 2006
+ year = 2006,
+ doi = {10187/2281}
}
@Article{dAuvergneGooley03,
@@ -1295,7 +1303,8 @@
medline-so = {J Biomol NMR 2003 Jan;25(1):25-39.},
medline-stat = {MEDLINE},
url =
{http://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?cmd=prlinks\&dbfrom=pubmed\&retmode=ref\&id=12566997},
- year = 2003
+ year = 2003,
+ doi = {10.1023/a:1021902006114}
}
@Article{dAuvergneGooley06,
@@ -1350,6 +1359,7 @@
University of Melbourne, Parkville, Victoria, 3010,
Australia, edward@xxxxxxxxxxxxxx},
language = {eng},
+ doi = {10.1007/s10858-006-9007-z},
medline-aid = {10.1007/s10858-006-9007-z [doi]},
medline-da = {20060704},
medline-dep = {20060622},
@@ -1417,6 +1427,7 @@
keywords = {Magnetic Resonance Spectroscopy/*methods ; *Models,
Theoretical ; Proteins/chemistry ; Thermodynamics},
language = {eng},
+ doi = {10.1039/b702202f},
medline-aid = {10.1039/b702202f [doi]},
medline-da = {20070620},
medline-dcom = {20070823},
@@ -1504,6 +1515,7 @@
Biomolecular/*methods ; Rhodobacter
capsulatus/chemistry ; *Rotation},
language = {eng},
+ doi = {10.1007/s10858-007-9214-2},
medline-aid = {10.1007/s10858-007-9214-2 [doi]},
medline-crdt = {2007/12/19 09:00},
medline-da = {20080109},
@@ -1587,6 +1599,7 @@
Protein/chemistry ; Peptide Fragments/chemistry ;
Protein Structure, Secondary ; *Rotation},
language = {eng},
+ doi = {10.1007/s10858-007-9213-3},
medline-aid = {10.1007/s10858-007-9213-3 [doi]},
medline-crdt = {2007/12/19 09:00},
medline-da = {20080109},
@@ -1840,7 +1853,7 @@
Erdelyi, Mate, Gothenburg Univ, Dept Chem, S-41124 Gothenburg, Sweden.
Erdelyi, Mate, Gothenburg Univ, Swedish NMR Ctr, S-41124 Gothenburg,
Sweden.
Navarro-Vazquez, Armando, Univ Vigo, Dept Organ Chem, Vigo, Spain.}},
-DOI = {{10.1002/chem.201100854}},
+DOI = {10.1002/chem.201100854},
ISSN = {{0947-6539}},
Keywords = {{glycosidic bonds; molecular dynamics; NMR spectroscopy;
oligosaccharides; paramagnetism}},
@@ -1997,7 +2010,8 @@
protein drk.},
month = {Sep},
sourceid = {ISI:A1995RY39200006},
- year = 1995
+ year = 1995,
+ doi = {10.1021/bi00003a021}
}
@Article{Favro60,
@@ -2332,6 +2346,7 @@
Support, U.S. Gov't, P.H.S. ; Signal
Transduction/physiology ; Solutions ; *Thermodynamics},
language = {eng},
+ doi = {10.1021/bi050149t},
medline-aid = {10.1021/bi050149t [doi]},
medline-da = {20050712},
medline-dcom = {20051011},
@@ -2461,6 +2476,7 @@
Research Support, Non-U.S. Gov't ; Research Support,
U.S. Gov't, Non-P.H.S. ; Zinc/metabolism},
language = {eng},
+ doi = {10.1021/bi952524v},
medline-aid = {10.1021/bi952524v [doi] ; bi952524v [pii]},
medline-da = {19960916},
medline-dcom = {19960916},
@@ -2573,6 +2589,7 @@
Protein Disulfide-Isomerase/*chemistry ; Protein
Structure, Secondary ; Vibrio cholerae/*enzymology},
language = {eng},
+ doi = {10.1016/j.jmb.2007.05.067},
medline-aid = {S0022-2836(07)00707-3 [pii] ;
10.1016/j.jmb.2007.05.067 [doi]},
medline-da = {20070730},
@@ -3453,6 +3470,7 @@
Trans-Activators/*chemistry/genetics/metabolism ;
*Transcription Factors},
language = {eng},
+ doi = {10.1021/bi9526802},
medline-aid = {10.1021/bi9526802 [doi] ; bi9526802 [pii]},
medline-da = {19960605},
medline-dcom = {19960605},
@@ -3546,7 +3564,8 @@
publisher = {Amer Chemical Soc},
size = {14 p.},
sourceid = {ISI:A1982PC82900009},
- year = 1982
+ year = 1982,
+ doi = {10.1021/ja00381a009}
}
@Article{LipariSzabo82b,
@@ -3617,7 +3636,8 @@
publisher = {Amer Chemical Soc},
size = {12 p.},
sourceid = {ISI:A1982PC82900010},
- year = 1982
+ year = 1982,
+ doi = {10.1021/ja00381a010}
}
@Article{Luginbuhl97,
@@ -3668,6 +3688,7 @@
Proteins/*chemistry/metabolism ; Research Support,
Non-U.S. Gov't ; Solutions},
language = {eng},
+ doi = {10.1021/bi963161h},
medline-aid = {10.1021/bi963161h [doi] ; bi963161h [pii]},
medline-da = {19970710},
medline-dcom = {19970710},
@@ -3748,6 +3769,7 @@
Proteins/chemistry/genetics ; Research Support,
Non-U.S. Gov't},
language = {eng},
+ doi = {10.1021/bi952761y},
medline-aid = {10.1021/bi952761y [doi] ; bi952761y [pii]},
medline-da = {19960806},
medline-dcom = {19960806},
@@ -3827,6 +3849,7 @@
Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S. ;
Ribonuclease H, Calf Thymus/*chemistry ; Thermodynamics},
language = {eng},
+ doi = {10.1021/bi962089k},
medline-aid = {10.1021/bi962089k [doi] ; bi962089k [pii]},
medline-da = {19970123},
medline-dcom = {19970123},
@@ -3921,7 +3944,8 @@
medline-so = {J Mol Biol 1995 Feb 10;246(1):144-63.},
medline-stat = {MEDLINE},
url =
{http://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?cmd=prlinks\&dbfrom=pubmed\&retmode=ref\&id=7531772},
- year = 1995
+ year = 1995,
+ doi = {10.1006/jmbi.1994.0073}
}
@Article{Marquardt63,
@@ -4175,7 +4199,7 @@
volume = {45},
issue = {4},
url = {http://dx.doi.org/10.1007/s10858-009-9381-4},
- note = {10.1007/s10858-009-9381-4},
+ doi = {10.1007/s10858-009-9381-4},
abstract = {15N spin relaxation data is widely used to extract detailed
dynamic information regarding bond vectors such as the amide N-H bond of the
protein backbone. Analysis is typically carried using the Lipari-Szabo
model-free approach. Even though the original model-free equation can be
determined from single field R1 , R2 and NOE , over-determination of more
complex motional models is dependent on the recording of multiple field
datasets. This is especially important for the characterization of
conformational exchange which affects R2 in a field dependent manner.
However, severe artifacts can be introduced if inconsistencies arise between
experimental setups with different magnets (or samples). Here, we propose the
use of simple tests as validation tools for the assessment of consistency
between different datasets recorded at multiple magnetic fields. Synthetic
data are used to show the effects of inconsistencies on the proposed tests.
Moreover, an analysis of data currently deposited in the BMRB is performed.
Finally, two cases from our laboratory are presented. These tests are
implemented in the open-source program relax , and we propose their use as a
routine check-up for assessment of multiple field dataset consistency prior
to any analysis such as model-free calculations. We believe this will aid in
the extraction of higher quality dynamics information from 15N spin
relaxation data.},
year = {2009}
}
@@ -4437,7 +4461,8 @@
publisher = {Springer Verlag},
size = {8 p.},
sourceid = {ISI:A1995TR35000012},
- year = 1995
+ year = 1995,
+ doi = {10.1007/bf03162365}
}
@Article{Orekhov95b,
@@ -4786,7 +4811,8 @@
publisher = {Amer Chemical Soc},
size = {10 p.},
sourceid = {ISI:A1991FP84400001},
- year = 1991
+ year = 1991,
+ doi = {10.1021/ja00012a001}
}
@Article{Pawley01,
@@ -5157,6 +5183,7 @@
Research Support, U.S. Gov't, P.H.S. ;
Selenium/metabolism ; Signal Transduction},
language = {eng},
+ doi = {10.1016/S0022-2836(02)00242-5},
medline-aid = {10.1016/S0022-2836(02)00242-5 [doi] ;
S0022-2836(02)00242-5 [pii]},
medline-ci = {(c) 2002 Elsevier Science Ltd.},
@@ -5381,7 +5408,7 @@
Sun, Han; d'Auvergne, Edward J.; Reinscheid, Uwe M.; Griesinger,
Christian, Max Planck Inst Biophys Chem, Dept NMR Based Struct Biol, D-37077
Gottingen, Germany.
Dias, Luiz Carlos, Univ Estadual Campinas, Inst Quim, Lab Sintese Organ,
BR-13084971 Campinas, SP, Brazil.
Andrade, Carlos Kleber Z.; Rocha, Rafael Oliveira, Univ Brasilia, Inst
Quim, Lab Quim Metodol \& Organ Sintet, BR-70904970 Brasilia, DF, Brazil.}},
-DOI = {{10.1002/chem.201002520}},
+DOI = {10.1002/chem.201002520},
ISSN = {{0947-6539}},
Keywords = {{configuration determination; Michael addition; niobium; NMR
spectroscopy; optical rotation dispersion}},
@@ -6029,6 +6056,7 @@
University of Maryland School of Medicine, Baltimore,
Maryland 21201, USA.},
language = {eng},
+ doi = {10.1007/s10858-005-1281-7},
medline-aid = {10.1007/s10858-005-1281-7 [doi]},
medline-da = {20051013},
medline-edat = {2005/10/14 09:00},
@@ -6164,6 +6192,7 @@
aeruginosa/chemistry/*metabolism ; Research Support,
Non-U.S. Gov't ; Temperature ; Thermodynamics},
language = {eng},
+ doi = {10.1016/j.jmb.2004.08.001},
medline-aid = {10.1016/j.jmb.2004.08.001 [doi] ;
S0022-2836(04)00955-6 [pii]},
medline-da = {20040914},
@@ -6221,6 +6250,7 @@
Academic Press.},
authoraddress = {University of Gottingen},
language = {ENG},
+ doi = {10.1006/jmps.1999.1276},
medline-aid = {10.1006/jmps.1999.1276 [doi] ; jmps.1999.1276 [pii]},
medline-da = {20000327},
medline-edat = {2000/03/29},
r17367 - /trunk/docs/latex/bibliography.bib