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Volumn 14, Issue 1, 2014, Pages

Dimeric structure of p300/CBP associated factor

Author keywords

ATAC; Dimerization; Histone acetyltransferase; PCAF

Indexed keywords

HISTONE ACETYLTRANSFERASE PCAF; MALTOSE BINDING PROTEIN;

EID: 84892407850     PISSN: None     EISSN: 14726807     Source Type: Journal    
DOI: 10.1186/1472-6807-14-2     Document Type: Article
Times cited : (14)

References (45)
  • 1
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • 10.1038/47412 10638745
    • The language of covalent histone modifications. Strahl BD, Allis CD, Nature 2000 403 6765 41 45 10.1038/47412 10638745
    • (2000) Nature , vol.403 , Issue.6765 , pp. 41-45
    • Strahl, B.D.1    Allis, C.D.2
  • 2
    • 33847076849 scopus 로고    scopus 로고
    • Chromatin modifications and their function
    • 10.1016/j.cell.2007.02.005 17320507
    • Chromatin modifications and their function. Kouzarides T, Cell 2007 128 4 693 705 10.1016/j.cell.2007.02.005 17320507
    • (2007) Cell , vol.128 , Issue.4 , pp. 693-705
    • Kouzarides, T.1
  • 3
    • 2342599619 scopus 로고    scopus 로고
    • The diverse superfamily of lysine acetyltransferases and their roles in leukemia and other diseases
    • 10.1093/nar/gkh252 14960713
    • The diverse superfamily of lysine acetyltransferases and their roles in leukemia and other diseases. Yang XJ, Nucleic Acids Res 2004 32 3 959 976 10.1093/nar/gkh252 14960713
    • (2004) Nucleic Acids Res , vol.32 , Issue.3 , pp. 959-976
    • Yang, X.J.1
  • 4
    • 28044471827 scopus 로고    scopus 로고
    • Acetylation and deacetylation of non-histone proteins
    • 16289629
    • Acetylation and deacetylation of non-histone proteins. Glozak MA, Sengupta N, Zhang X, Seto E, Gene 2005 363 15 23 16289629
    • (2005) Gene , vol.363 , pp. 15-23
    • Glozak, M.A.1    Sengupta, N.2    Zhang, X.3    Seto, E.4
  • 5
    • 34547890019 scopus 로고    scopus 로고
    • Functions of site-specific histone acetylation and deacetylation
    • 10.1146/annurev.biochem.76.052705.162114 17362198
    • Functions of site-specific histone acetylation and deacetylation. Shahbazian MD, Grunstein M, Annu Rev Biochem 2007 76 75 100 10.1146/annurev. biochem.76.052705.162114 17362198
    • (2007) Annu Rev Biochem , vol.76 , pp. 75-100
    • Shahbazian, M.D.1    Grunstein, M.2
  • 6
    • 0033623238 scopus 로고    scopus 로고
    • Loss of Gcn5l2 leads to increased apoptosis and mesodermal defects during mouse development
    • 10.1038/79973 11017084
    • Loss of Gcn5l2 leads to increased apoptosis and mesodermal defects during mouse development. Xu W, Edmondson DG, Evrard YA, Wakamiya M, Behringer RR, Roth SY, Nat Genet 2000 26 2 229 232 10.1038/79973 11017084
    • (2000) Nat Genet , vol.26 , Issue.2 , pp. 229-232
    • Xu, W.1    Edmondson, D.G.2    Evrard, Y.A.3    Wakamiya, M.4    Behringer, R.R.5    Roth, S.Y.6
  • 7
    • 0034633644 scopus 로고    scopus 로고
    • Distinct but overlapping roles of histone acetylase PCAF and of the closely related PCAF-B/GCN5 in mouse embryogenesis
    • 10.1073/pnas.97.21.11303 11027331
    • Distinct but overlapping roles of histone acetylase PCAF and of the closely related PCAF-B/GCN5 in mouse embryogenesis. Yamauchi T, Yamauchi J, Kuwata T, Tamura T, Yamashita T, Bae N, Westphal H, Ozato K, Nakatani Y, Proc Natl Acad Sci U S A 2000 97 21 11303 11306 10.1073/pnas.97.21.11303 11027331
    • (2000) Proc Natl Acad Sci U S A , vol.97 , Issue.21 , pp. 11303-11306
    • Yamauchi, T.1    Yamauchi, J.2    Kuwata, T.3    Tamura, T.4    Yamashita, T.5    Bae, N.6    Westphal, H.7    Ozato, K.8    Nakatani, Y.9
  • 8
    • 43649104766 scopus 로고    scopus 로고
    • Altered memory capacities and response to stress in p300/CBP-associated factor (PCAF) histone acetylase knockout mice
    • 10.1038/sj.npp.1301551 17805310
    • Altered memory capacities and response to stress in p300/CBP-associated factor (PCAF) histone acetylase knockout mice. Maurice T, Duclot F, Meunier J, Naert G, Givalois L, Meffre J, Celerier A, Jacquet C, Copois V, Mechti N, et al. Neuropsychopharmacology 2008 33 7 1584 1602 10.1038/sj.npp.1301551 17805310
    • (2008) Neuropsychopharmacology , vol.33 , Issue.7 , pp. 1584-1602
    • Maurice, T.1    Duclot, F.2    Meunier, J.3    Naert, G.4    Givalois, L.5    Meffre, J.6    Celerier, A.7    Jacquet, C.8    Copois, V.9    Mechti, N.10
  • 9
    • 77952553303 scopus 로고    scopus 로고
    • Alteration of working memory but not in anxiety or stress response in p300/CBP associated factor (PCAF) histone acetylase knockout mice bred on a C57BL/6 background
    • 10.1016/j.neulet.2010.03.077 20371377
    • Alteration of working memory but not in anxiety or stress response in p300/CBP associated factor (PCAF) histone acetylase knockout mice bred on a C57BL/6 background. Duclot F, Jacquet C, Gongora C, Maurice T, Neurosci Lett 2010 475 3 179 183 10.1016/j.neulet.2010.03.077 20371377
    • (2010) Neurosci Lett , vol.475 , Issue.3 , pp. 179-183
    • Duclot, F.1    Jacquet, C.2    Gongora, C.3    Maurice, T.4
  • 10
    • 78651250895 scopus 로고    scopus 로고
    • Genetic variation in PCAF, a key mediator in epigenetics, is associated with reduced vascular morbidity and mortality: Evidence for a new concept from three independent prospective studies
    • 10.1136/hrt.2010.199927 21062767
    • Genetic variation in PCAF, a key mediator in epigenetics, is associated with reduced vascular morbidity and mortality: evidence for a new concept from three independent prospective studies. Pons D, Trompet S, De Craen AJ, Thijssen PE, Quax PH, De Vries MR, Wierda RJ, van den Elsen PJ, Monraats PS, Ewing MM, et al. Heart 2011 97 2 143 150 10.1136/hrt.2010.199927 21062767
    • (2011) Heart , vol.97 , Issue.2 , pp. 143-150
    • Pons, D.1    Trompet, S.2    De Craen, A.J.3    Thijssen, P.E.4    Quax, P.H.5    De Vries, M.R.6    Wierda, R.J.7    Van Den Elsen, P.J.8    Monraats, P.S.9    Ewing, M.M.10
  • 11
    • 34547864553 scopus 로고    scopus 로고
    • Distinct GCN5/PCAF-containing complexes function as co-activators and are involved in transcription factor and global histone acetylation
    • 10.1038/sj.onc.1210604 17694077
    • Distinct GCN5/PCAF-containing complexes function as co-activators and are involved in transcription factor and global histone acetylation. Nagy Z, Tora L, Oncogene 2007 26 37 5341 5357 10.1038/sj.onc.1210604 17694077
    • (2007) Oncogene , vol.26 , Issue.37 , pp. 5341-5357
    • Nagy, Z.1    Tora, L.2
  • 12
    • 0029984469 scopus 로고    scopus 로고
    • Tetrahymena histone acetyltransferase A: A homolog to yeast Gcn5p linking histone acetylation to gene activation
    • 10.1016/S0092-8674(00)81063-6 8601308
    • Tetrahymena histone acetyltransferase A: a homolog to yeast Gcn5p linking histone acetylation to gene activation. Brownell JE, Zhou J, Ranalli T, Kobayashi R, Edmondson DG, Roth SY, Allis CD, Cell 1996 84 6 843 851 10.1016/S0092-8674(00)81063-6 8601308
    • (1996) Cell , vol.84 , Issue.6 , pp. 843-851
    • Brownell, J.E.1    Zhou, J.2    Ranalli, T.3    Kobayashi, R.4    Edmondson, D.G.5    Roth, S.Y.6    Allis, C.D.7
  • 13
    • 0029665857 scopus 로고    scopus 로고
    • A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A
    • 10.1038/382319a0 8684459
    • A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A. Yang XJ, Ogryzko VV, Nishikawa J, Howard BH, Nakatani Y, Nature 1996 382 6589 319 324 10.1038/382319a0 8684459
    • (1996) Nature , vol.382 , Issue.6589 , pp. 319-324
    • Yang, X.J.1    Ogryzko, V.V.2    Nishikawa, J.3    Howard, B.H.4    Nakatani, Y.5
  • 14
    • 0035902781 scopus 로고    scopus 로고
    • Structure of histone acetyltransferases
    • 10.1006/jmbi.2001.4859 11492997
    • Structure of histone acetyltransferases. Marmorstein R, J Mol Biol 2001 311 3 433 444 10.1006/jmbi.2001.4859 11492997
    • (2001) J Mol Biol , vol.311 , Issue.3 , pp. 433-444
    • Marmorstein, R.1
  • 15
    • 59449087016 scopus 로고    scopus 로고
    • Histone modifying enzymes: Structures, mechanisms, and specificities
    • 10.1016/j.bbagrm.2008.07.009 18722564
    • Histone modifying enzymes: structures, mechanisms, and specificities. Marmorstein R, Trievel RC, Biochim Biophys Acta 2009 1789 1 58 68 10.1016/j.bbagrm.2008.07.009 18722564
    • (2009) Biochim Biophys Acta , vol.1789 , Issue.1 , pp. 58-68
    • Marmorstein, R.1    Trievel, R.C.2
  • 16
    • 0033517354 scopus 로고    scopus 로고
    • Structure of Tetrahymena GCN5 bound to coenzyme A and a histone H3 peptide
    • 10.1038/43487 10485713
    • Structure of Tetrahymena GCN5 bound to coenzyme A and a histone H3 peptide. Rojas JR, Trievel RC, Zhou J, Mo Y, Li X, Berger SL, Allis CD, Marmorstein R, Nature 1999 401 6748 93 98 10.1038/43487 10485713
    • (1999) Nature , vol.401 , Issue.6748 , pp. 93-98
    • Rojas, J.R.1    Trievel, R.C.2    Zhou, J.3    Mo, Y.4    Li, X.5    Berger, S.L.6    Allis, C.D.7    Marmorstein, R.8
  • 17
    • 0033168714 scopus 로고    scopus 로고
    • Crystal structure of the histone acetyltransferase domain of the human PCAF transcriptional regulator bound to coenzyme A
    • 10.1093/emboj/18.13.3521 10393169
    • Crystal structure of the histone acetyltransferase domain of the human PCAF transcriptional regulator bound to coenzyme A. Clements A, Rojas JR, Trievel RC, Wang L, Berger SL, Marmorstein R, EMBO J 1999 18 13 3521 3532 10.1093/emboj/18.13.3521 10393169
    • (1999) EMBO J , vol.18 , Issue.13 , pp. 3521-3532
    • Clements, A.1    Rojas, J.R.2    Trievel, R.C.3    Wang, L.4    Berger, S.L.5    Marmorstein, R.6
  • 18
    • 0347481147 scopus 로고    scopus 로고
    • Molecular basis for Gcn5/PCAF histone acetyltransferase selectivity for histone and nonhistone substrates
    • 10.1021/bi035632n 14661947
    • Molecular basis for Gcn5/PCAF histone acetyltransferase selectivity for histone and nonhistone substrates. Poux AN, Marmorstein R, Biochemistry 2003 42 49 14366 14374 10.1021/bi035632n 14661947
    • (2003) Biochemistry , vol.42 , Issue.49 , pp. 14366-14374
    • Poux, A.N.1    Marmorstein, R.2
  • 19
    • 0029835806 scopus 로고    scopus 로고
    • Transcription-linked acetylation by Gcn5p of histones H3 and H4 at specific lysines
    • 10.1038/383269a0 8805705
    • Transcription-linked acetylation by Gcn5p of histones H3 and H4 at specific lysines. Kuo MH, Brownell JE, Sobel RE, Ranalli TA, Cook RG, Edmondson DG, Roth SY, Allis CD, Nature 1996 383 6597 269 272 10.1038/383269a0 8805705
    • (1996) Nature , vol.383 , Issue.6597 , pp. 269-272
    • Kuo, M.H.1    Brownell, J.E.2    Sobel, R.E.3    Ranalli, T.A.4    Cook, R.G.5    Edmondson, D.G.6    Roth, S.Y.7    Allis, C.D.8
  • 20
    • 0033556404 scopus 로고    scopus 로고
    • Overlapping but distinct patterns of histone acetylation by the human coactivators p300 and PCAF within nucleosomal substrates
    • 10.1074/jbc.274.3.1189 9880483
    • Overlapping but distinct patterns of histone acetylation by the human coactivators p300 and PCAF within nucleosomal substrates. Schiltz RL, Mizzen CA, Vassilev A, Cook RG, Allis CD, Nakatani Y, J Biol Chem 1999 274 3 1189 1192 10.1074/jbc.274.3.1189 9880483
    • (1999) J Biol Chem , vol.274 , Issue.3 , pp. 1189-1192
    • Schiltz, R.L.1    Mizzen, C.A.2    Vassilev, A.3    Cook, R.G.4    Allis, C.D.5    Nakatani, Y.6
  • 23
    • 84858329099 scopus 로고    scopus 로고
    • ATAC-king the complexity of SAGA during evolution
    • 10.1101/gad.184705.111 22426530
    • ATAC-king the complexity of SAGA during evolution. Spedale G, Timmers HT, Pijnappel WW, Genes Dev 2012 26 6 527 541 10.1101/gad.184705.111 22426530
    • (2012) Genes Dev , vol.26 , Issue.6 , pp. 527-541
    • Spedale, G.1    Timmers, H.T.2    Pijnappel, W.W.3
  • 24
    • 0037041022 scopus 로고    scopus 로고
    • Role of the Ada2 and Ada3 transcriptional coactivators in histone acetylation
    • 10.1074/jbc.M110849200 11773077
    • Role of the Ada2 and Ada3 transcriptional coactivators in histone acetylation. Balasubramanian R, Pray-Grant MG, Selleck W, Grant PA, Tan S, J Biol Chem 2002 277 10 7989 7995 10.1074/jbc.M110849200 11773077
    • (2002) J Biol Chem , vol.277 , Issue.10 , pp. 7989-7995
    • Balasubramanian, R.1    Pray-Grant, M.G.2    Selleck, W.3    Grant, P.A.4    Tan, S.5
  • 25
    • 58149476940 scopus 로고    scopus 로고
    • The STAGA subunit ADA2b is an important regulator of human GCN5 catalysis
    • 10.1128/MCB.00315-08 18936164
    • The STAGA subunit ADA2b is an important regulator of human GCN5 catalysis. Gamper AM, Kim J, Roeder RG, Mol Cell Biol 2009 29 1 266 280 10.1128/MCB.00315-08 18936164
    • (2009) Mol Cell Biol , vol.29 , Issue.1 , pp. 266-280
    • Gamper, A.M.1    Kim, J.2    Roeder, R.G.3
  • 26
    • 33144483781 scopus 로고    scopus 로고
    • Structure and function of the SWIRM domain, a conserved protein module found in chromatin regulatory complexes
    • 10.1073/pnas.0510949103 16461455
    • Structure and function of the SWIRM domain, a conserved protein module found in chromatin regulatory complexes. Da G, Lenkart J, Zhao K, Shiekhattar R, Cairns BR, Marmorstein R, Proc Natl Acad Sci U S A 2006 103 7 2057 2062 10.1073/pnas.0510949103 16461455
    • (2006) Proc Natl Acad Sci U S A , vol.103 , Issue.7 , pp. 2057-2062
    • Da, G.1    Lenkart, J.2    Zhao, K.3    Shiekhattar, R.4    Cairns, B.R.5    Marmorstein, R.6
  • 27
    • 0037040978 scopus 로고    scopus 로고
    • The SANT domain of Ada2 is required for normal acetylation of histones by the yeast SAGA complex
    • 10.1074/jbc.M108601200 11777910
    • The SANT domain of Ada2 is required for normal acetylation of histones by the yeast SAGA complex. Sterner DE, Wang X, Bloom MH, Simon GM, Berger SL, J Biol Chem 2002 277 10 8178 8186 10.1074/jbc.M108601200 11777910
    • (2002) J Biol Chem , vol.277 , Issue.10 , pp. 8178-8186
    • Sterner, D.E.1    Wang, X.2    Bloom, M.H.3    Simon, G.M.4    Berger, S.L.5
  • 28
    • 0036809731 scopus 로고    scopus 로고
    • Essential role for the SANT domain in the functioning of multiple chromatin remodeling enzymes
    • 10.1016/S1097-2765(02)00634-2 12419236
    • Essential role for the SANT domain in the functioning of multiple chromatin remodeling enzymes. Boyer LA, Langer MR, Crowley KA, Tan S, Denu JM, Peterson CL, Mol Cell 2002 10 4 935 942 10.1016/S1097-2765(02)00634-2 12419236
    • (2002) Mol Cell , vol.10 , Issue.4 , pp. 935-942
    • Boyer, L.A.1    Langer, M.R.2    Crowley, K.A.3    Tan, S.4    Denu, J.M.5    Peterson, C.L.6
  • 29
    • 0742305878 scopus 로고    scopus 로고
    • The SANT domain: A unique histone-tail-binding module?
    • 10.1038/nrm1314 15040448
    • The SANT domain: a unique histone-tail-binding module? Boyer LA, Latek RR, Peterson CL, Nat Rev Mol Cell Biol 2004 5 2 158 163 10.1038/nrm1314 15040448
    • (2004) Nat Rev Mol Cell Biol , vol.5 , Issue.2 , pp. 158-163
    • Boyer, L.A.1    Latek, R.R.2    Peterson, C.L.3
  • 30
    • 0028876860 scopus 로고
    • ADA3, a putative transcriptional adaptor, consists of two separable domains and interacts with ADA2 and GCN5 in a trimeric complex
    • 7862114
    • ADA3, a putative transcriptional adaptor, consists of two separable domains and interacts with ADA2 and GCN5 in a trimeric complex. Horiuchi J, Silverman N, Marcus GA, Guarente L, Mol Cell Biol 1995 15 3 1203 1209 7862114
    • (1995) Mol Cell Biol , vol.15 , Issue.3 , pp. 1203-1209
    • Horiuchi, J.1    Silverman, N.2    Marcus, G.A.3    Guarente, L.4
  • 31
    • 34249869569 scopus 로고    scopus 로고
    • Crystal structure of a binary complex between human GCN5 histone acetyltransferase domain and acetyl coenzyme A
    • 10.1002/prot.21407 17410582
    • Crystal structure of a binary complex between human GCN5 histone acetyltransferase domain and acetyl coenzyme A. Schuetz A, Bernstein G, Dong A, Antoshenko T, Wu H, Loppnau P, Bochkarev A, Plotnikov AN, Proteins 2007 68 1 403 407 10.1002/prot.21407 17410582
    • (2007) Proteins , vol.68 , Issue.1 , pp. 403-407
    • Schuetz, A.1    Bernstein, G.2    Dong, A.3    Antoshenko, T.4    Wu, H.5    Loppnau, P.6    Bochkarev, A.7    Plotnikov, A.N.8
  • 32
    • 79251540554 scopus 로고    scopus 로고
    • The tale of protein lysine acetylation in the cytoplasm
    • 21151618
    • The tale of protein lysine acetylation in the cytoplasm. Sadoul K, Wang J, Diagouraga B, Khochbin S, J Biomed Biotechnol 2011 2011 970382 21151618
    • (2011) J Biomed Biotechnol , vol.2011 , pp. 970382
    • Sadoul, K.1    Wang, J.2    Diagouraga, B.3    Khochbin, S.4
  • 33
    • 70349311616 scopus 로고    scopus 로고
    • Histone acetyl transferases as emerging drug targets
    • 10.1016/j.drudis.2009.06.008 19577000
    • Histone acetyl transferases as emerging drug targets. Dekker FJ, Haisma HJ, Drug Discov Today 2009 14 19-20 942 948 10.1016/j.drudis.2009.06.008 19577000
    • (2009) Drug Discov Today , vol.14 , Issue.19-20 , pp. 942-948
    • Dekker, F.J.1    Haisma, H.J.2
  • 34
    • 0035313803 scopus 로고    scopus 로고
    • Histone acetyltransferases: Function, structure, and catalysis
    • 10.1016/S0959-437X(00)00173-8 11250138
    • Histone acetyltransferases: function, structure, and catalysis. Marmorstein R, Roth SY, Curr Opin Genet Dev 2001 11 2 155 161 10.1016/S0959-437X(00)00173-8 11250138
    • (2001) Curr Opin Genet Dev , vol.11 , Issue.2 , pp. 155-161
    • Marmorstein, R.1    Roth, S.Y.2
  • 36
    • 77951218846 scopus 로고    scopus 로고
    • Structural basis for acetylated histone H4 recognition by the human BRD2 bromodomain
    • 10.1074/jbc.M109.062422 20048151
    • Structural basis for acetylated histone H4 recognition by the human BRD2 bromodomain. Umehara T, Nakamura Y, Jang MK, Nakano K, Tanaka A, Ozato K, Padmanabhan B, Yokoyama S, J Biol Chem 2010 285 10 7610 7618 10.1074/jbc.M109.062422 20048151
    • (2010) J Biol Chem , vol.285 , Issue.10 , pp. 7610-7618
    • Umehara, T.1    Nakamura, Y.2    Jang, M.K.3    Nakano, K.4    Tanaka, A.5    Ozato, K.6    Padmanabhan, B.7    Yokoyama, S.8
  • 37
    • 0028847955 scopus 로고
    • Conservation of deposition-related acetylation sites in newly synthesized histones H3 and H4
    • 10.1073/pnas.92.4.1237 7862667
    • Conservation of deposition-related acetylation sites in newly synthesized histones H3 and H4. Sobel RE, Cook RG, Perry CA, Annunziato AT, Allis CD, Proc Natl Acad Sci U S A 1995 92 4 1237 1241 10.1073/pnas.92.4.1237 7862667
    • (1995) Proc Natl Acad Sci U S A , vol.92 , Issue.4 , pp. 1237-1241
    • Sobel, R.E.1    Cook, R.G.2    Perry, C.A.3    Annunziato, A.T.4    Allis, C.D.5
  • 38
    • 3242680774 scopus 로고    scopus 로고
    • Molecular architecture of the S cerevisiae SAGA complex
    • 10.1016/j.molcel.2004.06.005 15260971
    • Molecular architecture of the S cerevisiae SAGA complex. Wu PY, Ruhlmann C, Winston F, Schultz P, Mol Cell 2004 15 2 199 208 10.1016/j.molcel.2004.06.005 15260971
    • (2004) Mol Cell , vol.15 , Issue.2 , pp. 199-208
    • Wu, P.Y.1    Ruhlmann, C.2    Winston, F.3    Schultz, P.4
  • 39
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 A resolution
    • 10.1038/38444 9305837
    • Crystal structure of the nucleosome core particle at 2.8 A resolution. Luger K, Mader AW, Richmond RK, Sargent DF, Richmond TJ, Nature 1997 389 6648 251 260 10.1038/38444 9305837
    • (1997) Nature , vol.389 , Issue.6648 , pp. 251-260
    • Luger, K.1    Mader, A.W.2    Richmond, R.K.3    Sargent, D.F.4    Richmond, T.J.5
  • 40
    • 79957708413 scopus 로고    scopus 로고
    • Quikgene: A gene synthesis method integrated with ligation-free cloning
    • 10.1016/j.ab.2011.04.004 21530481
    • Quikgene: a gene synthesis method integrated with ligation-free cloning. Mao Y, Lin J, Zhou A, Ji K, Downey JS, Chen R, Han A, Anal Biochem 2011 415 1 21 26 10.1016/j.ab.2011.04.004 21530481
    • (2011) Anal Biochem , vol.415 , Issue.1 , pp. 21-26
    • Mao, Y.1    Lin, J.2    Zhou, A.3    Ji, K.4    Downey, J.S.5    Chen, R.6    Han, A.7
  • 41
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Processing of X-ray diffraction data collected in oscillation mode. Otwinowski Z, Minor W, Methods Enzymol 1997 276 307 326
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 43
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • 15572765
    • Coot: model-building tools for molecular graphics. Emsley P, Cowtan K, Acta Crystallogr D Biol Crystallogr 2004 60 Pt 12 Pt 1 2126 2132 15572765
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , Issue.PART 12 PT 1 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 45
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • 10.1016/j.jmb.2007.05.022 17681537
    • Inference of macromolecular assemblies from crystalline state. Krissinel E, Henrick K, J Mol Biol 2007 372 3 774 797 10.1016/j.jmb.2007.05.022 17681537
    • (2007) J Mol Biol , vol.372 , Issue.3 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2


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