Sandbox Reserved 896: Difference between revisions

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== References ==

[1] Taniguchi Y. The Bromodomain and Extra-Terminal Domain (BET) Family: Functional Anatomy of BET Paralogous Proteins. International Journal of Molecular Sciences. 2016Jul;17(11):1849.

[2] Nakamura Y, Umehara T, Nakano K, Jang MK, Shirouzu M, Morita S, et al. Crystal Structure of the Human BRD2 Bromodomain: INSIGHTS INTO DIMERIZATION AND RECOGNITION OF ACETYLATED HISTONE H4. Journal of Biological Chemistry. 2006;282(6):4193–201.

[3] Umehara T, Nakamura Y, Jang MK, Nakano K, Tanaka A, Ozato K, et al. Structural Basis for Acetylated Histone H4 Recognition by the Human BRD2 Bromodomain. Journal of Biological Chemistry. 2010Apr;285(10):7610–8.

[4] Wang Q, Li Y, Xu J, Wang Y, Leung EL-H, Liu L, et al. Selective inhibition mechanism of RVX-208 to the second bromodomain of bromo and extraterminal proteins: insight from microsecond molecular dynamics simulations. Scientific Reports. 2017;7(1).

[5] Viejo-Borbolla A, Ottinger M, Bruning E, Burger A, Konig R, Kati E, et al. Brd2/RING3 interacts with a chromatin-binding domain in the Kaposi's Sarcoma-associated herpesvirus latency-associated nuclear antigen 1 (LANA-1) that is required for multiple functions of LANA-1. Journal of Virology. 2005Nov;

[6] Gilan O, Rioja I, Knezevic K, Bell M, Yeung M. Selective targeting of BD1 and BD2 of the BET proteins in cancer and immunoinflammation. Science. 2020Apr24;368(6489):387–94.

[7] Pal DK, Evgrafov OV, Tabares P, Zhang F, Durner M, Greenberg DA. BRD2 (RING3) Is a Probable Major Susceptibility Gene for Common Juvenile Myoclonic Epilepsy. The American Journal of Human Genetics. 2003;73(2):261–70.

[8] UniProt ConsortiumEuropean Bioinformatics InstituteProtein Information ResourceSIB Swiss Institute of Bioinformatics. Bromodomain-containing protein 2 [Internet]. UniProt ConsortiumEuropean Bioinformatics InstituteProtein Information ResourceSIB Swiss Institute of Bioinformatics. State Secretariat for Education, Research, and Innovation; 2020 [cited 2020Apr28]. Available from: https://www.uniprot.org/uniprot/P25440#expression

[9] UniProt ConsortiumEuropean Bioinformatics InstituteProtein Information ResourceSIB Swiss Institute of Bioinformatics. Bromodomain-containing protein 3 [Internet]. UniProt ConsortiumEuropean Bioinformatics InstituteProtein Information ResourceSIB Swiss Institute of Bioinformatics. State Secretariat for Education, Research, and Innovation; 2020 [cited 2020Apr28]. Available from: https://www.uniprot.org/uniprot/Q15059

[10] UniProt ConsortiumEuropean Bioinformatics InstituteProtein Information ResourceSIB Swiss Institute of Bioinformatics. Bromodomain-containing protein 4 [Internet]. UniProt ConsortiumEuropean Bioinformatics InstituteProtein Information ResourceSIB Swiss Institute of Bioinformatics. State Secretariat for Education, Research, and Innovation; 2020 [cited 2020Apr28]. Available from: https://www.uniprot.org/uniprot/O60885

[11] UniProt ConsortiumEuropean Bioinformatics InstituteProtein Information ResourceSIB Swiss Institute of Bioinformatics. Bromodomain testis-specific protein [Internet]. UniProt ConsortiumEuropean Bioinformatics InstituteProtein Information ResourceSIB Swiss Institute of Bioinformatics. State Secretariat for Education, Research, and Innovation; 2020 [cited 2020Apr28]. Available from: https://www.uniprot.org/uniprot/Q58F21

[12] RCSB Protein Data Bank. 2DVQ: Crystal structure analysis of the N-terminal bromodomain of human BRD2 complexed with acetylated histone H4 peptide [Internet]. RCSB PDB. [cited 2020Apr28]. Available from: https://www.rcsb.org/structure/2DVQ

[13] Tommaso PD, Moretti S, Xenarios I, Orobitg M, Montanyola A, Chang J-M, et al. T-Coffee: a web server for the multiple sequence alignment of protein and RNA sequences using structural information and homology extension. Nucleic Acids Research. 2011Sep;39(suppl).

[14] Armougom F, Moretti S, Poirot O, Audic S, Dumas P, Schaeli B, et al. Expresso: automatic incorporation of structural information in multiple sequence alignments using 3D-Coffee. Nucleic Acids Research. 2006Jan;34(Web Server).

[15] Osullivan O. 3DCoffee: Combining Protein Sequences and Structures within Multiple Sequence Alignments. Journal of Molecular Biology. 2004;

[16] Notredame C, Higgins DG, Heringa J. T-coffee: a novel method for fast and accurate multiple sequence alignment. Thornton J, editor. Journal of Molecular Biology. 2000;302(1):205–17.

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@@ Line 122: / Line 122: @@
 == References ==
+[1]	Taniguchi Y. The Bromodomain and Extra-Terminal Domain (BET) Family: Functional Anatomy of BET Paralogous Proteins. International Journal of Molecular Sciences. 2016Jul;17(11):1849.
+[2]	Nakamura Y, Umehara T, Nakano K, Jang MK, Shirouzu M, Morita S, et al. Crystal Structure of the Human BRD2 Bromodomain: INSIGHTS INTO DIMERIZATION AND RECOGNITION OF ACETYLATED HISTONE H4. Journal of Biological Chemistry. 2006;282(6):4193–201.
+[3]	Umehara T, Nakamura Y, Jang MK, Nakano K, Tanaka A, Ozato K, et al. Structural Basis for Acetylated Histone H4 Recognition by the Human BRD2 Bromodomain. Journal of Biological Chemistry. 2010Apr;285(10):7610–8.
+[4]	Wang Q, Li Y, Xu J, Wang Y, Leung EL-H, Liu L, et al. Selective inhibition mechanism of RVX-208 to the second bromodomain of bromo and extraterminal proteins: insight from microsecond molecular dynamics simulations. Scientific Reports. 2017;7(1).
+[5]	Viejo-Borbolla A, Ottinger M, Bruning E, Burger A, Konig R, Kati E, et al. Brd2/RING3 interacts with a chromatin-binding domain in the Kaposi's Sarcoma-associated herpesvirus latency-associated nuclear antigen 1 (LANA-1) that is required for multiple functions of LANA-1. Journal of Virology. 2005Nov;
+[6]	Gilan O, Rioja I, Knezevic K, Bell M, Yeung M. Selective targeting of BD1 and BD2 of the BET proteins in cancer and immunoinflammation. Science. 2020Apr24;368(6489):387–94.
+[7]	Pal DK, Evgrafov OV, Tabares P, Zhang F, Durner M, Greenberg DA. BRD2 (RING3) Is a Probable Major Susceptibility Gene for Common Juvenile Myoclonic Epilepsy. The American Journal of Human Genetics. 2003;73(2):261–70.
+[8]	UniProt ConsortiumEuropean Bioinformatics InstituteProtein Information ResourceSIB Swiss Institute of Bioinformatics. Bromodomain-containing protein 2 [Internet]. UniProt ConsortiumEuropean Bioinformatics InstituteProtein Information ResourceSIB Swiss Institute of Bioinformatics. State Secretariat for Education, Research, and Innovation; 2020 [cited 2020Apr28]. Available from: https://www.uniprot.org/uniprot/P25440#expression
+[9]	UniProt ConsortiumEuropean Bioinformatics InstituteProtein Information ResourceSIB Swiss Institute of Bioinformatics. Bromodomain-containing protein 3 [Internet]. UniProt ConsortiumEuropean Bioinformatics InstituteProtein Information ResourceSIB Swiss Institute of Bioinformatics. State Secretariat for Education, Research, and Innovation; 2020 [cited 2020Apr28]. Available from: https://www.uniprot.org/uniprot/Q15059
+[10]	UniProt ConsortiumEuropean Bioinformatics InstituteProtein Information ResourceSIB Swiss Institute of Bioinformatics. Bromodomain-containing protein 4 [Internet]. UniProt ConsortiumEuropean Bioinformatics InstituteProtein Information ResourceSIB Swiss Institute of Bioinformatics. State Secretariat for Education, Research, and Innovation; 2020 [cited 2020Apr28]. Available from: https://www.uniprot.org/uniprot/O60885
+[11]	UniProt ConsortiumEuropean Bioinformatics InstituteProtein Information ResourceSIB Swiss Institute of Bioinformatics. Bromodomain testis-specific protein [Internet]. UniProt ConsortiumEuropean Bioinformatics InstituteProtein Information ResourceSIB Swiss Institute of Bioinformatics. State Secretariat for Education, Research, and Innovation; 2020 [cited 2020Apr28]. Available from: https://www.uniprot.org/uniprot/Q58F21
+[12]	RCSB Protein Data Bank. 2DVQ: Crystal structure analysis of the N-terminal bromodomain of human BRD2 complexed with acetylated histone H4 peptide [Internet]. RCSB PDB. [cited 2020Apr28]. Available from: https://www.rcsb.org/structure/2DVQ
+[13]	Tommaso PD, Moretti S, Xenarios I, Orobitg M, Montanyola A, Chang J-M, et al. T-Coffee: a web server for the multiple sequence alignment of protein and RNA sequences using structural information and homology extension. Nucleic Acids Research. 2011Sep;39(suppl).
+[14]	Armougom F, Moretti S, Poirot O, Audic S, Dumas P, Schaeli B, et al. Expresso: automatic incorporation of structural information in multiple sequence alignments using 3D-Coffee. Nucleic Acids Research. 2006Jan;34(Web Server).
+[15]	Osullivan O. 3DCoffee: Combining Protein Sequences and Structures within Multiple Sequence Alignments. Journal of Molecular Biology. 2004;
+[16]	Notredame C, Higgins DG, Heringa J. T-coffee: a novel method for fast and accurate multiple sequence alignment. Thornton J, editor. Journal of Molecular Biology. 2000;302(1):205–17.
 <references/>