From: W. Trevor King Date: Sun, 24 Jun 2012 06:51:45 +0000 (-0400) Subject: Add labeit95 and sandal09 to root.bib. X-Git-Tag: v1.0~335 X-Git-Url: http://git.tremily.us/?a=commitdiff_plain;h=478bc8e575e25d1c891b14c1fe058265fc2a74ac;p=thesis.git Add labeit95 and sandal09 to root.bib. --- diff --git a/src/root.bib b/src/root.bib index b7192ba..6f389eb 100644 --- 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", +}