-
1
-
-
26944466459
-
Mechanism of membrane fusion by viral envelope proteins
-
Harrison SC. 2005. Mechanism of membrane fusion by viral envelope proteins. Adv Virus Res 64:231-259. https://doi.org/10.1016/S0065-3527(05)64007-9.
-
(2005)
Adv Virus Res
, vol.64
, pp. 231-259
-
-
Harrison, S.C.1
-
2
-
-
0030970693
-
Core structure of gp41 from the HIV envelope glycoprotein
-
Chan DC, Fass D, Berger JM, Kim PS. 1997. Core structure of gp41 from the HIV envelope glycoprotein. Cell 89:263-273. https://doi.org/10.1016/ S0092-8674(00)80205-6.
-
(1997)
Cell
, vol.89
, pp. 263-273
-
-
Chan, D.C.1
Fass, D.2
Berger, J.M.3
Kim, P.S.4
-
3
-
-
0030962291
-
Atomic structure of the ectodomain from HIV-1 gp41
-
Weissenhorn W, Dessen A, Harrison SC, Skehel JJ, Wiley DC. 1997. Atomic structure of the ectodomain from HIV-1 gp41. Nature 387:426-430. https://doi.org/10.1038/387426a0.
-
(1997)
Nature
, vol.387
, pp. 426-430
-
-
Weissenhorn, W.1
Dessen, A.2
Harrison, S.C.3
Skehel, J.J.4
Wiley, D.C.5
-
4
-
-
84864365540
-
HIV-1 envelope trimer elicits more potent neutralizing antibody responses than monomeric gp120
-
Kovacs JM, Nkolola JP, Peng H, Cheung A, Perry J, Miller CA, Seaman MS, Barouch DH, Chen B. 2012. HIV-1 envelope trimer elicits more potent neutralizing antibody responses than monomeric gp120. Proc Natl Acad Sci U S A 109:12111-12116. https://doi.org/10.1073/pnas.1204533109.
-
(2012)
Proc Natl Acad Sci U S A
, vol.109
, pp. 12111-12116
-
-
Kovacs, J.M.1
Nkolola, J.P.2
Peng, H.3
Cheung, A.4
Perry, J.5
Miller, C.A.6
Seaman, M.S.7
Barouch, D.H.8
Chen, B.9
-
5
-
-
84937544544
-
HIV-1 envelope. Effect of the cytoplasmic domain on antigenic characteristics of HIV-1 envelope glycoprotein
-
Chen J, Kovacs JM, Peng H, Rits-Volloch S, Lu J, Park D, Zablowsky E, Seaman MS, Chen B. 2015. HIV-1 envelope. Effect of the cytoplasmic domain on antigenic characteristics of HIV-1 envelope glycoprotein. Science 349:191-195. https://doi.org/10.1126/science.aaa9804.
-
(2015)
Science
, vol.349
, pp. 191-195
-
-
Chen, J.1
Kovacs, J.M.2
Peng, H.3
Rits-Volloch, S.4
Lu, J.5
Park, D.6
Zablowsky, E.7
Seaman, M.S.8
Chen, B.9
-
6
-
-
84884678235
-
A next-generation cleaved, soluble HIV-1 Env trimer, BG505 SOSIP.664 gp140, expresses multiple epitopes for broadly neutralizing but not non-neutralizing antibodies
-
Sanders RW, Derking R, Cupo A, Julien JP, Yasmeen A, de Val N, Kim HJ, Blattner C, de la Pena AT, Korzun J, Golabek M, de Los Reyes K, Ketas TJ, van Gils MJ, King CR, Wilson IA, Ward AB, Klasse PJ, Moore JP. 2013. A next-generation cleaved, soluble HIV-1 Env trimer, BG505 SOSIP.664 gp140, expresses multiple epitopes for broadly neutralizing but not non-neutralizing antibodies. PLoS Pathog 9:e1003618. https://doi.org/10 .1371/journal.ppat.1003618.
-
(2013)
PLoS Pathog
, vol.9
-
-
Sanders, R.W.1
Derking, R.2
Cupo, A.3
Julien, J.P.4
Yasmeen, A.5
de Val, N.6
Kim, H.J.7
Blattner, C.8
de la Pena, A.T.9
Korzun, J.10
Golabek, M.11
de Los Reyes, K.12
Ketas, T.J.13
van Gils, M.J.14
King, C.R.15
Wilson, I.A.16
Ward, A.B.17
Klasse, P.J.18
Moore, J.P.19
-
7
-
-
84923172318
-
A native-like SOSIP.664 trimer based on an HIV-1 subtype B env gene
-
Pugach P, Ozorowski G, Cupo A, Ringe R, Yasmeen A, de Val N, Derking R, Kim HJ, Korzun J, Golabek M, de Los Reyes K, Ketas TJ, Julien JP, Burton DR, Wilson IA, Sanders RW, Klasse PJ, Ward AB, Moore JP. 2015. A native-like SOSIP.664 trimer based on an HIV-1 subtype B env gene. J Virol 89:3380-3395. https://doi.org/10.1128/JVI.03473-14.
-
(2015)
J Virol
, vol.89
, pp. 3380-3395
-
-
Pugach, P.1
Ozorowski, G.2
Cupo, A.3
Ringe, R.4
Yasmeen, A.5
de Val, N.6
Derking, R.7
Kim, H.J.8
Korzun, J.9
Golabek, M.10
de Los Reyes, K.11
Ketas, T.J.12
Julien, J.P.13
Burton, D.R.14
Wilson, I.A.15
Sanders, R.W.16
Klasse, P.J.17
Ward, A.B.18
Moore, J.P.19
-
8
-
-
84890858459
-
Crystal structure of a soluble cleaved HIV-1 envelope trimer
-
Julien JP, Cupo A, Sok D, Stanfield RL, Lyumkis D, Deller MC, Klasse PJ, Burton DR, Sanders RW, Moore JP, Ward AB, Wilson IA. 2013. Crystal structure of a soluble cleaved HIV-1 envelope trimer. Science 342: 1477-1483. https://doi.org/10.1126/science.1245625.
-
(2013)
Science
, vol.342
, pp. 1477-1483
-
-
Julien, J.P.1
Cupo, A.2
Sok, D.3
Stanfield, R.L.4
Lyumkis, D.5
Deller, M.C.6
Klasse, P.J.7
Burton, D.R.8
Sanders, R.W.9
Moore, J.P.10
Ward, A.B.11
Wilson, I.A.12
-
9
-
-
84890859441
-
Cryo-EM structure of a fully glycosylated soluble cleaved HIV-1 envelope trimer
-
Lyumkis D, Julien JP, de Val N, Cupo A, Potter CS, Klasse PJ, Burton DR, Sanders RW, Moore JP, Carragher B, Wilson IA, Ward AB. 2013. Cryo-EM structure of a fully glycosylated soluble cleaved HIV-1 envelope trimer. Science 342:1484-1490. https://doi.org/10.1126/science.1245627.
-
(2013)
Science
, vol.342
, pp. 1484-1490
-
-
Lyumkis, D.1
Julien, J.P.2
de Val, N.3
Cupo, A.4
Potter, C.S.5
Klasse, P.J.6
Burton, D.R.7
Sanders, R.W.8
Moore, J.P.9
Carragher, B.10
Wilson, I.A.11
Ward, A.B.12
-
10
-
-
84909640954
-
Structure and immune recognition of trimeric pre-fusion HIV-1 Env
-
Pancera M, Zhou T, Druz A, Georgiev IS, Soto C, Gorman J, Huang J, Acharya P, Chuang GY, Ofek G, Stewart-Jones GB, Stuckey J, Bailer RT, Joyce MG, Louder MK, Tumba N, Yang Y, Zhang B, Cohen MS, Haynes BF, Mascola JR, Morris L, Munro JB, Blanchard SC, Mothes W, Connors M, Kwong PD. 2014. Structure and immune recognition of trimeric pre-fusion HIV-1 Env. Nature 514:455-461. https://doi.org/10.1038/ nature13808.
-
(2014)
Nature
, vol.514
, pp. 455-461
-
-
Pancera, M.1
Zhou, T.2
Druz, A.3
Georgiev, I.S.4
Soto, C.5
Gorman, J.6
Huang, J.7
Acharya, P.8
Chuang, G.Y.9
Ofek, G.10
Stewart-Jones, G.B.11
Stuckey, J.12
Bailer, R.T.13
Joyce, M.G.14
Louder, M.K.15
Tumba, N.16
Yang, Y.17
Zhang, B.18
Cohen, M.S.19
Haynes, B.F.20
Mascola, J.R.21
Morris, L.22
Munro, J.B.23
Blanchard, S.C.24
Mothes, W.25
Connors, M.26
Kwong, P.D.27
more..
-
11
-
-
84961231130
-
Cryo-EM structure of a native, fully glycosylated, cleaved HIV-1 envelope trimer
-
Lee JH, Ozorowski G, Ward AB. 2016. Cryo-EM structure of a native, fully glycosylated, cleaved HIV-1 envelope trimer. Science 351:1043-1048. https://doi.org/10.1126/science.aad2450.
-
(2016)
Science
, vol.351
, pp. 1043-1048
-
-
Lee, J.H.1
Ozorowski, G.2
Ward, A.B.3
-
12
-
-
84901499773
-
Stable 293 T and CHO cell lines expressing cleaved, stable HIV-1 envelope glycoprotein trimers for structural and vaccine studies
-
Chung NP, Matthews K, Kim HJ, Ketas TJ, Golabek M, de Los Reyes K, Korzun J, Yasmeen A, Sanders RW, Klasse PJ, Wilson IA, Ward AB, Marozsan AJ, Moore JP, Cupo A. 2014. Stable 293 T and CHO cell lines expressing cleaved, stable HIV-1 envelope glycoprotein trimers for structural and vaccine studies. Retrovirology 11:33. https://doi.org/10.1186/ 1742-4690-11-33.
-
(2014)
Retrovirology
, vol.11
, pp. 33
-
-
Chung, N.P.1
Matthews, K.2
Kim, H.J.3
Ketas, T.J.4
Golabek, M.5
de Los Reyes, K.6
Korzun, J.7
Yasmeen, A.8
Sanders, R.W.9
Klasse, P.J.10
Wilson, I.A.11
Ward, A.B.12
Marozsan, A.J.13
Moore, J.P.14
Cupo, A.15
-
13
-
-
84976633087
-
Uncleaved prefusionoptimized gp140 trimers derived from analysis of HIV-1 envelope metastability
-
Kong L, He L, de Val N, Vora N, Morris CD, Azadnia P, Sok D, Zhou B, Burton DR, Ward AB, Wilson IA, Zhu J. 2016. Uncleaved prefusionoptimized gp140 trimers derived from analysis of HIV-1 envelope metastability. Nat Commun 7:12040. https://doi.org/10.1038/ncomms12040.
-
(2016)
Nat Commun
, vol.7
, pp. 12040
-
-
Kong, L.1
He, L.2
de Val, N.3
Vora, N.4
Morris, C.D.5
Azadnia, P.6
Sok, D.7
Zhou, B.8
Burton, D.R.9
Ward, A.B.10
Wilson, I.A.11
Zhu, J.12
-
14
-
-
1242338175
-
Expression and characterisation of recombinant oligomeric envelope glycoproteins derived from primary isolates of HIV-1
-
Jeffs SA, Goriup S, Kebble B, Crane D, Bolgiano B, Sattentau Q, Jones S, Holmes H. 2004. Expression and characterisation of recombinant oligomeric envelope glycoproteins derived from primary isolates of HIV-1. Vaccine 22:1032-1046. https://doi.org/10.1016/j.vaccine.2003.08.042.
-
(2004)
Vaccine
, vol.22
, pp. 1032-1046
-
-
Jeffs, S.A.1
Goriup, S.2
Kebble, B.3
Crane, D.4
Bolgiano, B.5
Sattentau, Q.6
Jones, S.7
Holmes, H.8
-
15
-
-
84887307095
-
Cleavage strongly influences whether soluble HIV-1 envelope glycoprotein trimers adopt a native-like conformation
-
Ringe RP, Sanders RW, Yasmeen A, Kim HJ, Lee JH, Cupo A, Korzun J, Derking R, van Montfort T, Julien JP, Wilson IA, Klasse PJ, Ward AB, Moore JP. 2013. Cleavage strongly influences whether soluble HIV-1 envelope glycoprotein trimers adopt a native-like conformation. Proc Natl Acad Sci U S A 110:18256-18261. https://doi.org/10.1073/pnas.1314351110.
-
(2013)
Proc Natl Acad Sci U S A
, vol.110
, pp. 18256-18261
-
-
Ringe, R.P.1
Sanders, R.W.2
Yasmeen, A.3
Kim, H.J.4
Lee, J.H.5
Cupo, A.6
Korzun, J.7
Derking, R.8
van Montfort, T.9
Julien, J.P.10
Wilson, I.A.11
Klasse, P.J.12
Ward, A.B.13
Moore, J.P.14
-
16
-
-
84941363719
-
Broadly neutralizing antibody 8ANC195 recognizes closed and open states of HIV-1 Env
-
Scharf L, Wang H, Gao H, Chen S, McDowall AW, Bjorkman PJ. 2015. Broadly neutralizing antibody 8ANC195 recognizes closed and open states of HIV-1 Env. Cell 162:1379-1390. https://doi.org/10.1016/j.cell .2015.08.035.
-
(2015)
Cell
, vol.162
, pp. 1379-1390
-
-
Scharf, L.1
Wang, H.2
Gao, H.3
Chen, S.4
McDowall, A.W.5
Bjorkman, P.J.6
-
17
-
-
84923154103
-
Stable, uncleaved HIV-1 envelope glycoprotein gp140 forms a tightly folded trimer with a native-like structure
-
Kovacs JM, Noeldeke E, Ha HJ, Peng H, Rits-Volloch S, Harrison SC, Chen B. 2014. Stable, uncleaved HIV-1 envelope glycoprotein gp140 forms a tightly folded trimer with a native-like structure. Proc Natl Acad Sci U S A 111:18542-18547. https://doi.org/10.1073/pnas.1422269112.
-
(2014)
Proc Natl Acad Sci U S A
, vol.111
, pp. 18542-18547
-
-
Kovacs, J.M.1
Noeldeke, E.2
Ha, H.J.3
Peng, H.4
Rits-Volloch, S.5
Harrison, S.C.6
Chen, B.7
-
18
-
-
84928379119
-
A primer to singleparticle cryo-electron microscopy
-
Cheng Y, Grigorieff N, Penczek PA, Walz T. 2015. A primer to singleparticle cryo-electron microscopy. Cell 161:438-449. https://doi.org/10 .1016/j.cell.2015.03.050.
-
(2015)
Cell
, vol.161
, pp. 438-449
-
-
Cheng, Y.1
Grigorieff, N.2
Penczek, P.A.3
Walz, T.4
-
19
-
-
84868444740
-
RELION: implementation of a Bayesian approach to cryo-EM structure determination
-
Scheres SH. 2012. RELION: implementation of a Bayesian approach to cryo-EM structure determination. J Struct Biol 180:519-530. https://doi .org/10.1016/j.jsb.2012.09.006.
-
(2012)
J Struct Biol
, vol.180
, pp. 519-530
-
-
Scheres, S.H.1
-
20
-
-
0027756896
-
A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants
-
Harbury PB, Zhang T, Kim PS, Alber T. 1993. A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants. Science 262:1401-1407. https://doi.org/10.1126/science.8248779.
-
(1993)
Science
, vol.262
, pp. 1401-1407
-
-
Harbury, P.B.1
Zhang, T.2
Kim, P.S.3
Alber, T.4
-
21
-
-
0036178009
-
Domain organization, folding and stability of bacteriophage T4 fibritin, a segmented coiled-coil protein
-
Boudko SP, Londer YY, Letarov AV, Sernova NV, Engel J, Mesyanzhinov VV. 2002. Domain organization, folding and stability of bacteriophage T4 fibritin, a segmented coiled-coil protein. Eur J Biochem 269:833-841. https://doi.org/10.1046/j.1432-1033.2002.02734.x.
-
(2002)
Eur J Biochem
, vol.269
, pp. 833-841
-
-
Boudko, S.P.1
Londer, Y.Y.2
Letarov, A.V.3
Sernova, N.V.4
Engel, J.5
Mesyanzhinov, V.V.6
-
22
-
-
84974849211
-
Frealign: an exploratory tool for single-particle cryo-EM
-
Grigorieff N. 2016. Frealign: an exploratory tool for single-particle cryo-EM. Methods Enzymol 579:191-226. https://doi.org/10.1016/bs.mie.2016 .04.013.
-
(2016)
Methods Enzymol
, vol.579
, pp. 191-226
-
-
Grigorieff, N.1
-
23
-
-
51349162563
-
Molecular architecture of native HIV-1 gp120 trimers
-
Liu J, Bartesaghi A, Borgnia MJ, Sapiro G, Subramaniam S. 2008. Molecular architecture of native HIV-1 gp120 trimers. Nature 455:109-113. https://doi.org/10.1038/nature07159.
-
(2008)
Nature
, vol.455
, pp. 109-113
-
-
Liu, J.1
Bartesaghi, A.2
Borgnia, M.J.3
Sapiro, G.4
Subramaniam, S.5
-
24
-
-
0019890491
-
Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 A resolution
-
Wilson IA, Skehel JJ, Wiley DC. 1981. Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 A resolution. Nature 289:366-373. https://doi.org/10.1038/289366a0.
-
(1981)
Nature
, vol.289
, pp. 366-373
-
-
Wilson, I.A.1
Skehel, J.J.2
Wiley, D.C.3
-
25
-
-
18844470928
-
Structure of the hemagglutinin precursor cleavage site, a determinant of influenza pathogenicity and the origin of the labile conformation
-
Chen J, Lee KH, Steinhauer DA, Stevens DJ, Skehel JJ, Wiley DC. 1998. Structure of the hemagglutinin precursor cleavage site, a determinant of influenza pathogenicity and the origin of the labile conformation. Cell 95:409-417. https://doi.org/10.1016/S0092-8674(00)81771-7.
-
(1998)
Cell
, vol.95
, pp. 409-417
-
-
Chen, J.1
Lee, K.H.2
Steinhauer, D.A.3
Stevens, D.J.4
Skehel, J.J.5
Wiley, D.C.6
-
26
-
-
84976908417
-
Structural basis for membrane anchoring of HIV-1 envelope spike
-
Dev J, Park D, Fu Q, Chen J, Ha HJ, Ghantous F, Herrmann T, Chang W, Liu Z, Frey G, Seaman MS, Chen B, Chou JJ. 2016. Structural basis for membrane anchoring of HIV-1 envelope spike. Science 353:172-175. https://doi.org/10.1126/science.aaf7066.
-
(2016)
Science
, vol.353
, pp. 172-175
-
-
Dev, J.1
Park, D.2
Fu, Q.3
Chen, J.4
Ha, H.J.5
Ghantous, F.6
Herrmann, T.7
Chang, W.8
Liu, Z.9
Frey, G.10
Seaman, M.S.11
Chen, B.12
Chou, J.J.13
-
27
-
-
84937469192
-
HIV-1 vaccines. HIV-1 neutralizing antibodies induced by native-like envelope trimers
-
Sanders RW, van Gils MJ, Derking R, Sok D, Ketas TJ, Burger JA, Ozorowski G, Cupo A, Simonich C, Goo L, Arendt H, Kim HJ, Lee JH, Pugach P, Williams M, Debnath G, Moldt B, van Breemen MJ, Isik G, Medina-Ramirez M, Back JW, Koff WC, Julien JP, Rakasz EG, Seaman MS, Guttman M, Lee KK, Klasse PJ, LaBranche C, Schief WR, Wilson IA, Overbaugh J, Burton DR, Ward AB, Montefiori DC, Dean H, Moore JP. 2015. HIV-1 vaccines. HIV-1 neutralizing antibodies induced by native-like envelope trimers. Science 349:aac4223. https://doi.org/10.1126/science.aac4223.
-
(2015)
Science
, vol.349
-
-
Sanders, R.W.1
van Gils, M.J.2
Derking, R.3
Sok, D.4
Ketas, T.J.5
Burger, J.A.6
Ozorowski, G.7
Cupo, A.8
Simonich, C.9
Goo, L.10
Arendt, H.11
Kim, H.J.12
Lee, J.H.13
Pugach, P.14
Williams, M.15
Debnath, G.16
Moldt, B.17
van Breemen, M.J.18
Isik, G.19
Medina-Ramirez, M.20
Back, J.W.21
Koff, W.C.22
Julien, J.P.23
Rakasz, E.G.24
Seaman, M.S.25
Guttman, M.26
Lee, K.K.27
Klasse, P.J.28
LaBranche, C.29
Schief, W.R.30
Wilson, I.A.31
Overbaugh, J.32
Burton, D.R.33
Ward, A.B.34
Montefiori, D.C.35
Dean, H.36
Moore, J.P.37
more..
-
28
-
-
41649090223
-
A fusion-intermediate state of HIV-1 gp41 targeted by broadly neutralizing antibodies
-
Frey G, Peng H, Rits-Volloch S, Morelli M, Cheng Y, Chen B. 2008. A fusion-intermediate state of HIV-1 gp41 targeted by broadly neutralizing antibodies. Proc Natl Acad Sci U S A 105:3739-3744. https://doi.org/10 .1073/pnas.0800255105.
-
(2008)
Proc Natl Acad Sci U S A
, vol.105
, pp. 3739-3744
-
-
Frey, G.1
Peng, H.2
Rits-Volloch, S.3
Morelli, M.4
Cheng, Y.5
Chen, B.6
-
29
-
-
25644458666
-
Automated electron microscope tomography using robust prediction of specimen movements
-
Mastronarde DN. 2005. Automated electron microscope tomography using robust prediction of specimen movements. J Struct Biol 152: 36-51. https://doi.org/10.1016/j.jsb.2005.07.007.
-
(2005)
J Struct Biol
, vol.152
, pp. 36-51
-
-
Mastronarde, D.N.1
-
30
-
-
84930634509
-
Measuring the optimal exposure for single particle cryo-EM using a 2.6 A reconstruction of rotavirus VP6
-
Grant T, Grigorieff N. 2015. Measuring the optimal exposure for single particle cryo-EM using a 2.6 A reconstruction of rotavirus VP6. eLife 4:e06980. https://doi.org/10.7554/eLife.06980.
-
(2015)
ELife
, vol.4
-
-
Grant, T.1
Grigorieff, N.2
-
31
-
-
33845332754
-
EMAN2: an extensible image processing suite for electron microscopy
-
Tang G, Peng L, Baldwin PR, Mann DS, Jiang W, Rees I, Ludtke SJ. 2007. EMAN2: an extensible image processing suite for electron microscopy. J Struct Biol 157:38-46. https://doi.org/10.1016/j.jsb.2006.05.009.
-
(2007)
J Struct Biol
, vol.157
, pp. 38-46
-
-
Tang, G.1
Peng, L.2
Baldwin, P.R.3
Mann, D.S.4
Jiang, W.5
Rees, I.6
Ludtke, S.J.7
-
32
-
-
58049204808
-
SPIDER image processing for single-particle reconstruction of biological macromolecules from electron micrographs
-
Shaikh TR, Gao H, Baxter WT, Asturias FJ, Boisset N, Leith A, Frank J. 2008. SPIDER image processing for single-particle reconstruction of biological macromolecules from electron micrographs. Nat Protoc 3:1941-1974. https://doi.org/10.1038/nprot.2008.156.
-
(2008)
Nat Protoc
, vol.3
, pp. 1941-1974
-
-
Shaikh, T.R.1
Gao, H.2
Baxter, W.T.3
Asturias, F.J.4
Boisset, N.5
Leith, A.6
Frank, J.7
-
33
-
-
4444221565
-
UCSF Chimera-a visualization system for exploratory research and analysis
-
Pettersen EF, Goddard TD, Huang CC, Couch GS, Greenblatt DM, Meng EC, Ferrin TE. 2004. UCSF Chimera-a visualization system for exploratory research and analysis. J Comput Chem 25:1605-1612. https://doi .org/10.1002/jcc.20084.
-
(2004)
J Comput Chem
, vol.25
, pp. 1605-1612
-
-
Pettersen, E.F.1
Goddard, T.D.2
Huang, C.C.3
Couch, G.S.4
Greenblatt, D.M.5
Meng, E.C.6
Ferrin, T.E.7
-
34
-
-
0031570687
-
Structure of bacteriophage T4 fibritin: a segmented coiled coil and the role of the C-terminal domain
-
Tao Y, Strelkov SV, Mesyanzhinov VV, Rossmann MG. 1997. Structure of bacteriophage T4 fibritin: a segmented coiled coil and the role of the C-terminal domain. Structure 5:789-798. https://doi.org/10.1016/S0969-2126(97)00233-5.
-
(1997)
Structure
, vol.5
, pp. 789-798
-
-
Tao, Y.1
Strelkov, S.V.2
Mesyanzhinov, V.V.3
Rossmann, M.G.4
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