Add labeit95 and sandal09 to root.bib.

diff --git a/src/root.bib b/src/root.bib
index b7192ba4d71e171223b81004ad4bedac7e1b1bd0..6f389eb95db136662641a9fc413fd9fc0abfa9a4 100644 (file)
--- a/src/root.bib
+++ b/src/root.bib
@@ -58,6 +58,7 @@
 @string{GSBeddard = "Beddard, Godfrey S."}
 @string{KBeeson = "Beeson, K."}
 @string{GIBell = "Bell, G. I."}
+@string{FBenedetti = "Benedetti, Fabrizio"}
 @string{VBenes = "Benes, Vladimir"}
 @string{ABensimon = "Bensimon, A."}
 @string{DBensimon = "Bensimon, David"}
@@ -75,6 +76,7 @@
 @string{BCBPRC = "Biochemical and Biophysical Research Communications"}
 @string{Biochem = "Biochemistry"}
 @string{BBABE = "Biochimica et Biophysica Acta (BBA) - Bioenergetics"}
+@string{BIOINFO = "Bioinformatics (Oxford, England)",}
 @string{BPJ = "Biophys. J."}
 @string{BIOSENSE = "Biosensors and Bioelectronics"}
 @string{BIOTECH = "Biotechnology and Bioengineering"}
@@ -96,6 +98,7 @@
 @string{SBroedel = "Broedel, Sheldon E."}
 @string{BrooksCole = "Brooks/Cole"}
 @string{BDBrowerToland = "Brower-Toland, Brent D."}
+@string{MBrucale = "Brucale, Marco"}
 @string{TBruls = "Bruls, T."}
 @string{VBrumfeld = "Brumfeld, Vlad"}
 @string{JDBryngelson = "Bryngelson, J. D."}
@@ -277,6 +280,7 @@
 @string{GGloeckner = "Gloeckner, G."}
 @string{AGluecksmann = "Gluecksmann, A."}
 @string{JDGocayne = "Gocayne, J. D."}
+@string{AGomezCasado = "Gomez-Casado, Alberto"}
 @string{BGompertz = "Gompertz, Benjamin"}
 @string{FGong = "Gong, F."}
 @string{MGorokhov = "Gorokhov, M."}
@@ -704,7 +708,8 @@
 @string{JPRyckaert = "Ryckaert, Jean-Paul"}
 @string{YSakaki = "Sakaki, Y."}
 @string{SSalzberg = "Salzberg, S."}
-@string{BSamori = "Samori, Bruno"}
+@string{BSamori = "Samor{\`i}, Bruno"}
+@string{MSandal = "Sandal, Massimo"}
 @string{RSanders = "Sanders, R."}
 @string{ASarkar = "Sarkar, Atom"}
 @string{TSasaki = "Sasaki, T."}
@@ -3995,6 +4000,58 @@
         spring that adapts to the physiological state of the cell."
 }
 
+@article{ labeit95,
+  author = SLabeit #" and "# BKolmerer,
+  title = "Titins: giant proteins in charge of muscle ultrastructure
+    and elasticity.",
+  journal = SCI,
+  year = 1995,
+  month = oct,
+  day = 13,
+  address = "European Molecular Biology Laboratory, Heidelberg, Germany.",
+  volume = 270,
+  number = 5234,
+  pages = "293--296",
+  keywords = "Actin Cytoskeleton",
+  keywords = "Amino Acid Sequence",
+  keywords = "Animals",
+  keywords = "DNA, Complementary",
+  keywords = "Elasticity",
+  keywords = "Fibronectins",
+  keywords = "Humans",
+  keywords = "Immunoglobulins",
+  keywords = "Molecular Sequence Data",
+  keywords = "Muscle Contraction",
+  keywords = "Muscle Proteins",
+  keywords = "Muscle, Skeletal",
+  keywords = "Myocardium",
+  keywords = "Protein Kinases",
+  keywords = "Rabbits",
+  keywords = "Repetitive Sequences, Nucleic Acid",
+  keywords = "Sarcomeres",
+  abstract = "In addition to thick and thin filaments, vertebrate
+    striated muscle contains a third filament system formed by the
+    giant protein titin. Single titin molecules extend from Z discs to
+    M lines and are longer than 1 micrometer. The titin filament
+    contributes to muscle assembly and resting tension, but more
+    details are not known because of the large size of the
+    protein. The complete complementary DNA sequence of human cardiac
+    titin was determined. The 82-kilobase complementary DNA predicts a
+    3-megadalton protein composed of 244 copies of immunoglobulin and
+    fibronectin type III (FN3) domains. The architecture of sequences
+    in the A band region of titin suggests why thick filament
+    structure is conserved among vertebrates. In the I band region,
+    comparison of titin sequences from muscles of different passive
+    tension identifies two elements that correlate with tissue
+    stiffness. This suggests that titin may act as two springs in
+    series. The differential expression of the springs provides a
+    molecular explanation for the diversity of sarcomere length and
+    resting tension in vertebrate striated muscles.",
+  ISSN = "0036-8075",
+  URL = "http://www.ncbi.nlm.nih.gov/pubmed/7569978",
+  language = "eng",
+}
+
 @article { law03,
     author = RLaw #" and "# GLiao #" and "# SHarper #" and "# GYang #" and "#
         DSpeicher #" and "# DDischer,
@@ -7705,3 +7762,42 @@
   URL =          "http://www.ncbi.nlm.nih.gov/pubmed/16683841",
   language =     "eng",
 }
+
+@article{ sandal09,
+  author = MSandal #" and "# FBenedetti #" and "# MBrucale #" and "#
+    AGomezCasado #" and "# BSamori,
+  title = "Hooke: an open software platform for force spectroscopy.",
+  journal = BIOINFO,
+  year = 2009,
+  month = jun,
+  day = 01,
+  address = "Department of Biochemistry, University of Bologna,
+             Bologna, Italy. massimo.sandal@unibo.it",
+  volume = 25,
+  number = 11,
+  pages = "1428--1430",
+  keywords = "Algorithms",
+  keywords = "Computational Biology",
+  keywords = "Internet",
+  keywords = "Microscopy, Atomic Force",
+  keywords = "Proteome",
+  keywords = "Proteomics",
+  keywords = "Software",
+  abstract = "SUMMARY: Hooke is an open source, extensible software
+    intended for analysis of atomic force microscope (AFM)-based
+    single molecule force spectroscopy (SMFS) data. We propose it as a
+    platform on which published and new algorithms for SMFS analysis
+    can be integrated in a standard, open fashion, as a general
+    solution to the current lack of a standard software for SMFS data
+    analysis. Specific features and support for file formats are coded
+    as independent plugins. Any user can code new plugins, extending
+    the software capabilities.  Basic automated dataset filtering and
+    semi-automatic analysis facilities are included. AVAILABILITY:
+    Software and documentation are available at
+    (http://code.google.com/p/hooke). Hooke is a free software under
+    the GNU Lesser General Public License.",
+  ISSN = "1367-4811",
+  doi = "10.1093/bioinformatics/btp180",
+  URL = "http://www.ncbi.nlm.nih.gov/pubmed/19336443",
+  language = "eng",
+}