-
1
-
-
84909949812
-
Meta-analysis of Ubiquilin1 gene polymorphism and Alzheimer's disease risk
-
pmid: 25387430
-
T. Zhang, Y. Jia, Meta-analysis of Ubiquilin1 gene polymorphism and Alzheimer's disease risk. Med. Sci. Monit. 20, 2250-2255 (2014). doi: 10.12659/MSM.891030; pmid: 25387430
-
(2014)
Med. Sci. Monit.
, vol.20
, pp. 2250-2255
-
-
Zhang, T.1
Jia, Y.2
-
2
-
-
80052580969
-
Mutations in UBQLN2 cause dominant X-linked juvenile and adult-onset ALS and ALS/dementia
-
pmid: 21857683
-
H.-X. Deng et al., Mutations in UBQLN2 cause dominant X-linked juvenile and adult-onset ALS and ALS/dementia. Nature 477, 211-215 (2011). doi: 10.1038/nature10353; pmid: 21857683
-
(2011)
Nature
, vol.477
, pp. 211-215
-
-
Deng, H.-X.1
-
3
-
-
0028235965
-
A 26 S protease subunit that binds ubiquitin conjugates
-
pmid: 8125911
-
Q. Deveraux, V. Ustrell, C. Pickart, M. Rechsteiner, A 26 S protease subunit that binds ubiquitin conjugates. J. Biol. Chem. 269, 7059-7061 (1994). pmid: 8125911
-
(1994)
J. Biol. Chem.
, vol.269
, pp. 7059-7061
-
-
Deveraux, Q.1
Ustrell, V.2
Pickart, C.3
Rechsteiner, M.4
-
4
-
-
0029806477
-
The multiubiquitin-chain-binding protein Mcb1 is a component of the 26S proteasome in Saccharomyces cerevisiae and plays a nonessential, substrate-specific role in protein turnover
-
pmid: 8887631
-
S. Van Nocker et al., The multiubiquitin-chain-binding protein Mcb1 is a component of the 26S proteasome in Saccharomyces cerevisiae and plays a nonessential, substrate-specific role in protein turnover. Mol. Cell. Biol. 16, 6020-6028 (1996). doi: 10.1128/MCB.16.11.6020; pmid: 8887631
-
(1996)
Mol. Cell. Biol.
, vol.16
, pp. 6020-6028
-
-
Van Nocker, S.1
-
5
-
-
0031890210
-
Multiubiquitin chain binding and protein degradation are mediated by distinct domains within the 26 S proteasome subunit Mcb1
-
pmid: 9442033
-
H. Fu et al., Multiubiquitin chain binding and protein degradation are mediated by distinct domains within the 26 S proteasome subunit Mcb1. J. Biol. Chem. 273, 1970-1981 (1998). doi: 10.1074/jbc.273.4.1970; pmid: 9442033
-
(1998)
J. Biol. Chem.
, vol.273
, pp. 1970-1981
-
-
Fu, H.1
-
6
-
-
44349116590
-
Proteasome subunit Rpn13 is a novel ubiquitin receptor
-
pmid: 18497817
-
K. Husnjak et al., Proteasome subunit Rpn13 is a novel ubiquitin receptor. Nature 453, 481-488 (2008). doi: 10.1038/nature06926; pmid: 18497817
-
(2008)
Nature
, vol.453
, pp. 481-488
-
-
Husnjak, K.1
-
7
-
-
44349094727
-
Ubiquitin docking at the proteasome through a novel pleckstrin-homology domain interaction
-
pmid: 18497827
-
P. Schreiner et al., Ubiquitin docking at the proteasome through a novel pleckstrin-homology domain interaction. Nature 453, 548-552 (2008). doi: 10.1038/nature06924; pmid: 18497827
-
(2008)
Nature
, vol.453
, pp. 548-552
-
-
Schreiner, P.1
-
8
-
-
3042677641
-
Rad23 and Rpn10 serve as alternative ubiquitin receptors for the proteasome
-
pmid: 15117949
-
S. Elsasser, D. Chandler-Militello, B. Müller, J. Hanna, D. Finley, Rad23 and Rpn10 serve as alternative ubiquitin receptors for the proteasome. J. Biol. Chem. 279, 26817-26822 (2004). doi: 10.1074/jbc.M404020200; pmid: 15117949
-
(2004)
J. Biol. Chem.
, vol.279
, pp. 26817-26822
-
-
Elsasser, S.1
Chandler-Militello, D.2
Müller, B.3
Hanna, J.4
Finley, D.5
-
9
-
-
3142566639
-
Multiubiquitin chain receptors define a layer of substrate selectivity in the ubiquitin-proteasome system
-
pmid: 15242647
-
R. Verma, R. Oania, J. Graumann, R. J. Deshaies, Multiubiquitin chain receptors define a layer of substrate selectivity in the ubiquitin-proteasome system. Cell 118, 99-110 (2004). doi: 10.1016/j.cell.2004.06.014; pmid: 15242647
-
(2004)
Cell
, vol.118
, pp. 99-110
-
-
Verma, R.1
Oania, R.2
Graumann, J.3
Deshaies, R.J.4
-
10
-
-
0037154160
-
Budding yeast Dsk2p is a polyubiquitin-binding protein that can interact with the proteasome
-
pmid: 11805328
-
M. Funakoshi, T. Sasaki, T. Nishimoto, H. Kobayashi, Budding yeast Dsk2p is a polyubiquitin-binding protein that can interact with the proteasome. Proc. Natl. Acad. Sci. U.S.A. 99, 745-750 (2002). doi: 10.1073/pnas.012585199; pmid: 11805328
-
(2002)
Proc. Natl. Acad. Sci. U.S.A.
, vol.99
, pp. 745-750
-
-
Funakoshi, M.1
Sasaki, T.2
Nishimoto, T.3
Kobayashi, H.4
-
11
-
-
20444417275
-
The DNA damage-inducible UbL-UbA protein Ddi1 participates in Mec1-mediated degradation of Ho endonuclease
-
pmid: 15964793
-
L. Kaplun et al., The DNA damage-inducible UbL-UbA protein Ddi1 participates in Mec1-mediated degradation of Ho endonuclease. Mol. Cell. Biol. 25, 5355-5362 (2005). doi: 10.1128/MCB.25.13.5355-5362.2005; pmid: 15964793
-
(2005)
Mol. Cell. Biol.
, vol.25
, pp. 5355-5362
-
-
Kaplun, L.1
-
12
-
-
84864003919
-
Transfer of Ho endonuclease and Ufo1 to the proteasome by the UbL-UbA shuttle protein, Ddi1, analysed by complex formation in vitro
-
pmid: 22815701
-
O. Voloshin, A. Bakhrat, S. Herrmann, D. Raveh, Transfer of Ho endonuclease and Ufo1 to the proteasome by the UbL-UbA shuttle protein, Ddi1, analysed by complex formation in vitro. PLOS ONE 7, e39210 (2012). doi: 10.1371/journal. pone.0039210; pmid: 22815701
-
(2012)
PLOS ONE
, vol.7
, pp. e39210
-
-
Voloshin, O.1
Bakhrat, A.2
Herrmann, S.3
Raveh, D.4
-
13
-
-
11844263929
-
A series of ubiquitin binding factors connects CDC48/p97 to substrate multiubiquitylation and proteasomal targeting
-
pmid: 15652483
-
H. Richly et al., A series of ubiquitin binding factors connects CDC48/p97 to substrate multiubiquitylation and proteasomal targeting. Cell 120, 73-84 (2005). doi: 10.1016/j.cell.2004.11.013; pmid: 15652483
-
(2005)
Cell
, vol.120
, pp. 73-84
-
-
Richly, H.1
-
14
-
-
84922539969
-
Dss1 is a 26S proteasome ubiquitin receptor
-
pmid: 25306921
-
K. Paraskevopoulos et al., Dss1 is a 26S proteasome ubiquitin receptor. Mol. Cell 56, 453-461 (2014). doi: 10.1016/j.molcel.2014.09.008; pmid: 25306921
-
(2014)
Mol. Cell
, vol.56
, pp. 453-461
-
-
Paraskevopoulos, K.1
-
15
-
-
28844484999
-
Preparation of ubiquitinated substrates by the PY motif-insertion method for monitoring 26S proteasome activity
-
pmid: 16338358
-
Y. Saeki, E. Isono, A. Toh-E, Preparation of ubiquitinated substrates by the PY motif-insertion method for monitoring 26S proteasome activity. Methods Enzymol. 399, 215-227 (2005). doi: 10.1016/S0076-6879(05)99014-9; pmid: 16338358
-
(2005)
Methods Enzymol.
, vol.399
, pp. 215-227
-
-
Saeki, Y.1
Isono, E.2
Toh-E, A.3
-
16
-
-
0036713383
-
Proteasome subunit Rpn1 binds ubiquitin-like protein domains
-
pmid: 12198498
-
S. Elsasser et al., Proteasome subunit Rpn1 binds ubiquitin-like protein domains. Nat. Cell Biol. 4, 725-730 (2002). doi: 10.1038/ncb845; pmid: 12198498
-
(2002)
Nat. Cell Biol.
, vol.4
, pp. 725-730
-
-
Elsasser, S.1
-
17
-
-
79957637389
-
Identification of a functional docking site in the Rpn1 LRR domain for the UBA-UBL domain protein Ddi1
-
pmid: 21627799
-
T. A. Gomez, N. Kolawa, M. Gee, M. J. Sweredoski, R. J. Deshaies, Identification of a functional docking site in the Rpn1 LRR domain for the UBA-UBL domain protein Ddi1. BMC Biol. 9, 33 (2011). doi: 10.1186/1741-7007-9-33; pmid: 21627799
-
(2011)
BMC Biol.
, vol.9
, pp. 33
-
-
Gomez, T.A.1
Kolawa, N.2
Gee, M.3
Sweredoski, M.J.4
Deshaies, R.J.5
-
18
-
-
84860376787
-
Rpn1 and Rpn2 coordinate ubiquitin processing factors at proteasome
-
pmid: 22318722
-
R. Rosenzweig, V. Bronner, D. Zhang, D. Fushman, M. H. Glickman, Rpn1 and Rpn2 coordinate ubiquitin processing factors at proteasome. J. Biol. Chem. 287, 14659-14671 (2012). doi: 10.1074/jbc.M111.316323; pmid: 22318722
-
(2012)
J. Biol. Chem.
, vol.287
, pp. 14659-14671
-
-
Rosenzweig, R.1
Bronner, V.2
Zhang, D.3
Fushman, D.4
Glickman, M.H.5
-
19
-
-
84857935771
-
The structure of the 26S proteasome subunit Rpn2 reveals its PC repeat domain as a closed toroid of two concentric a-helical rings
-
pmid: 22405010
-
J. He et al., The structure of the 26S proteasome subunit Rpn2 reveals its PC repeat domain as a closed toroid of two concentric a-helical rings. Structure 20, 513-521 (2012). doi: 10.1016/j.str.2011.12.015; pmid: 22405010
-
(2012)
Structure
, vol.20
, pp. 513-521
-
-
He, J.1
-
20
-
-
0037147328
-
What curves alpha-solenoids? Evidence for an alpha-helical toroid structure of Rpn1 and Rpn2 proteins of the 26 S proteasome
-
pmid: 12270919
-
A. V. Kajava, What curves alpha-solenoids? Evidence for an alpha-helical toroid structure of Rpn1 and Rpn2 proteins of the 26 S proteasome. J. Biol. Chem. 277, 49791-49798 (2002). doi: 10.1074/jbc.M204982200; pmid: 12270919
-
(2002)
J. Biol. Chem.
, vol.277
, pp. 49791-49798
-
-
Kajava, A.V.1
-
21
-
-
17144417404
-
Structure of S5a bound to monoubiquitin provides a model for polyubiquitin recognition
-
pmid: 15826667
-
Q. Wang, P. Young, K. J. Walters, Structure of S5a bound to monoubiquitin provides a model for polyubiquitin recognition. J. Mol. Biol. 348, 727-739 (2005). doi: 10.1016/j.jmb.2005.03.007; pmid: 15826667
-
(2005)
J. Mol. Biol.
, vol.348
, pp. 727-739
-
-
Wang, Q.1
Young, P.2
Walters, K.J.3
-
22
-
-
84863281982
-
Identifying and studying ubiquitin receptors by NMR
-
pmid: 22350893
-
X. Chen, K. J. Walters, Identifying and studying ubiquitin receptors by NMR. Methods Mol. Biol. 832, 279-303 (2012). doi: 10.1007/978-1-61779-474-2-20; pmid: 22350893
-
(2012)
Methods Mol. Biol.
, vol.832
, pp. 279-303
-
-
Chen, X.1
Walters, K.J.2
-
23
-
-
77954757965
-
Multitasking with ubiquitin through multivalent interactions
-
pmid: 20181483
-
F. Liu, K. J. Walters, Multitasking with ubiquitin through multivalent interactions. Trends Biochem. Sci. 35, 352-360 (2010). pmid: 20181483
-
(2010)
Trends Biochem. Sci.
, vol.35
, pp. 352-360
-
-
Liu, F.1
Walters, K.J.2
-
24
-
-
72149114101
-
Together Rpn10 and Dsk2 can serve as a polyubiquitin chain-length sensor
-
pmid: 20064467
-
D. Zhang et al., Together, Rpn10 and Dsk2 can serve as a polyubiquitin chain-length sensor. Mol. Cell 36, 1018-1033 (2009). pmid: 20064467
-
(2009)
Mol. Cell
, vol.36
, pp. 1018-1033
-
-
Zhang, D.1
-
25
-
-
33745742269
-
Quantitative analysis of in vitro ubiquitinated cyclin B1 reveals complex chain topology
-
pmid: 16799550
-
D. S. Kirkpatrick et al., Quantitative analysis of in vitro ubiquitinated cyclin B1 reveals complex chain topology. Nat. Cell Biol. 8, 700-710 (2006). doi: 10.1038/ncb1436; pmid: 16799550
-
(2006)
Nat. Cell Biol.
, vol.8
, pp. 700-710
-
-
Kirkpatrick, D.S.1
-
26
-
-
33749049581
-
Deubiquitinating enzyme Ubp6 functions noncatalytically to delay proteasomal degradation
-
pmid: 17018280
-
J. Hanna et al., Deubiquitinating enzyme Ubp6 functions noncatalytically to delay proteasomal degradation. Cell 127, 99-111 (2006). doi: 10.1016/j.cell.2006.07.038; pmid: 17018280
-
(2006)
Cell
, vol.127
, pp. 99-111
-
-
Hanna, J.1
-
27
-
-
84862776836
-
APC/C-mediated multiple monoubiquitylation provides an alternative degradation signal for cyclin B1
-
pmid: 22286100
-
N. V. Dimova et al., APC/C-mediated multiple monoubiquitylation provides an alternative degradation signal for cyclin B1. Nat. Cell Biol. 14, 168-176 (2012). doi: 10.1038/ncb2425; pmid: 22286100
-
(2012)
Nat. Cell Biol.
, vol.14
, pp. 168-176
-
-
Dimova, N.V.1
-
28
-
-
0032879814
-
Pleiotropic defects caused by loss of the proteasome-interacting factors Rad23 and Rpn10 of Saccharomyces cerevisiae
-
pmid: 10471701
-
D. Lambertson, L. Chen, K. Madura, Pleiotropic defects caused by loss of the proteasome-interacting factors Rad23 and Rpn10 of Saccharomyces cerevisiae. Genetics 153, 69-79 (1999). pmid: 10471701
-
(1999)
Genetics
, vol.153
, pp. 69-79
-
-
Lambertson, D.1
Chen, L.2
Madura, K.3
-
29
-
-
55049090325
-
Extraproteasomal Rpn10 restricts access of the polyubiquitin-binding protein Dsk2 to proteasome
-
pmid: 18995839
-
Y. Matiuhin et al., Extraproteasomal Rpn10 restricts access of the polyubiquitin-binding protein Dsk2 to proteasome. Mol. Cell 32, 415-425 (2008). doi: 10.1016/j.molcel.2008.10.011; pmid: 18995839
-
(2008)
Mol. Cell
, vol.32
, pp. 415-425
-
-
Matiuhin, Y.1
-
30
-
-
0142215475
-
Global analysis of protein expression in yeast
-
pmid: 14562106
-
S. Ghaemmaghami et al., Global analysis of protein expression in yeast. Nature 425, 737-741 (2003). doi: 10.1038/nature02046; pmid: 14562106
-
(2003)
Nature
, vol.425
, pp. 737-741
-
-
Ghaemmaghami, S.1
-
31
-
-
0035876040
-
The 19S complex of the proteasome regulates nucleotide excision repair in yeast
-
pmid: 11410533
-
T. G. Gillette et al., The 19S complex of the proteasome regulates nucleotide excision repair in yeast. Genes Dev. 15, 1528-1539 (2001). doi: 10.1101/gad.869601; pmid: 11410533
-
(2001)
Genes Dev.
, vol.15
, pp. 1528-1539
-
-
Gillette, T.G.1
-
32
-
-
68349135106
-
Structure of the S5a:K48-linked diubiquitin complex and its interactions with Rpn13
-
pmid: 19683493
-
N. Zhang et al., Structure of the S5a:K48-linked diubiquitin complex and its interactions with Rpn13. Mol. Cell 35, 280-290 (2009). doi: 10.1016/j.molcel.2009.06.010; pmid: 19683493
-
(2009)
Mol. Cell
, vol.35
, pp. 280-290
-
-
Zhang, N.1
-
33
-
-
84952639230
-
Gates, channels, and switches: Elements of the proteasome machine
-
pmid: 26643069
-
D. Finley, X. Chen, K. J. Walters, Gates, channels, and switches: Elements of the proteasome machine. Trends Biochem. Sci. 41, 77-93 (2016). doi: 10.1016/j.tibs.2015.10.009; pmid: 26643069
-
(2016)
Trends Biochem. Sci.
, vol.41
, pp. 77-93
-
-
Finley, D.1
Chen, X.2
Walters, K.J.3
-
34
-
-
0036753063
-
Multiple associated proteins regulate proteasome structure and function
-
pmid: 12408819
-
D. S. Leggett et al., Multiple associated proteins regulate proteasome structure and function. Mol. Cell 10, 495-507 (2002). doi: 10.1016/S1097-2765(02)00638-X; pmid: 12408819
-
(2002)
Mol. Cell
, vol.10
, pp. 495-507
-
-
Leggett, D.S.1
-
35
-
-
84937111175
-
Structural characterization of the interaction of Ubp6 with the 26S proteasome
-
pmid: 26130806
-
A. Aufderheide et al., Structural characterization of the interaction of Ubp6 with the 26S proteasome. Proc. Natl. Acad. Sci. U.S.A. 112, 8626-8631 (2015). doi: 10.1073/pnas.1510449112; pmid: 26130806
-
(2015)
Proc. Natl. Acad. Sci. U.S.A.
, vol.112
, pp. 8626-8631
-
-
Aufderheide, A.1
-
36
-
-
84940984237
-
Ubp6 deubiquitinase controls conformational dynamics and substrate degradation of the 26S proteasome
-
pmid: 26301997
-
C. Bashore et al., Ubp6 deubiquitinase controls conformational dynamics and substrate degradation of the 26S proteasome. Nat. Struct. Mol. Biol. 22, 712-719 (2015). doi: 10.1038/nsmb.3075; pmid: 26301997
-
(2015)
Nat. Struct. Mol. Biol.
, vol.22
, pp. 712-719
-
-
Bashore, C.1
-
37
-
-
79951887389
-
Hydrogen exchange mass spectrometry for studying protein structure and dynamics
-
pmid: 21173980
-
L. Konermann, J. Pan, Y.-H. Liu, Hydrogen exchange mass spectrometry for studying protein structure and dynamics. Chem. Soc. Rev. 40, 1224-1234 (2011). doi: 10.1039/C0CS00113A; pmid: 21173980
-
(2011)
Chem. Soc. Rev.
, vol.40
, pp. 1224-1234
-
-
Konermann, L.1
Pan, J.2
Liu, Y.-H.3
-
38
-
-
84858277365
-
Probing protein interactions with hydrogen/deuterium exchange and mass spectrometry-A review
-
pmid: 22405295
-
A. J. Percy, M. Rey, K. M. Burns, D. C. Schriemer, Probing protein interactions with hydrogen/deuterium exchange and mass spectrometry-a review. Anal. Chim. Acta 721, 7-21 (2012). doi: 10.1016/j.aca.2012.01.037; pmid: 22405295
-
(2012)
Anal. Chim. Acta
, vol.721
, pp. 7-21
-
-
Percy, A.J.1
Rey, M.2
Burns, K.M.3
Schriemer, D.C.4
-
39
-
-
33644761306
-
Hydrogen exchange mass spectrometry for the analysis of protein dynamics
-
pmid: 16208684
-
T. E. Wales, J. R. Engen, Hydrogen exchange mass spectrometry for the analysis of protein dynamics. Mass Spectrom. Rev. 25, 158-170 (2006). doi: 10.1002/mas.20064; pmid: 16208684
-
(2006)
Mass Spectrom. Rev.
, vol.25
, pp. 158-170
-
-
Wales, T.E.1
Engen, J.R.2
-
40
-
-
84862520497
-
Protein hydrogen exchange: Testing current models
-
pmid: 22544567
-
J. J. Skinner, W. K. Lim, S. Bédard, B. E. Black, S. W. Englander, Protein hydrogen exchange: Testing current models. Protein Sci. 21, 987-995 (2012). doi: 10.1002/pro.2082; pmid: 22544567
-
(2012)
Protein Sci.
, vol.21
, pp. 987-995
-
-
Skinner, J.J.1
Lim, W.K.2
Bédard, S.3
Black, B.E.4
Englander, S.W.5
-
41
-
-
49549086897
-
Protein structure and dynamics studied by mass spectrometry: H/D exchange, hydroxyl radical labeling, and related approaches
-
pmid: 18523973
-
L. Konermann, X. Tong, Y. Pan, Protein structure and dynamics studied by mass spectrometry: H/D exchange, hydroxyl radical labeling, and related approaches. J. Mass Spectrom. 43, 1021-1036 (2008). doi: 10.1002/jms.1435; pmid: 18523973
-
(2008)
J. Mass Spectrom.
, vol.43
, pp. 1021-1036
-
-
Konermann, L.1
Tong, X.2
Pan, Y.3
-
42
-
-
33749326831
-
Identification and characterization of EX1 kinetics in H/D exchange mass spectrometry by peak width analysis
-
pmid: 16875839
-
D. D. Weis, T. E. Wales, J. R. Engen, M. Hotchko, L. F. Ten Eyck, Identification and characterization of EX1 kinetics in H/D exchange mass spectrometry by peak width analysis. J. Am. Soc. Mass Spectrom. 17, 1498-1509 (2006). doi: 10.1016/j.jasms.2006.05.014; pmid: 16875839
-
(2006)
J. Am. Soc. Mass Spectrom.
, vol.17
, pp. 1498-1509
-
-
Weis, D.D.1
Wales, T.E.2
Engen, J.R.3
Hotchko, M.4
Ten Eyck, L.F.5
-
43
-
-
13244258262
-
Mapping protein energy landscapes with amide hydrogen exchange and mass spectrometry: I. A generalized model for a two-state protein and comparison with experiment
-
pmid: 15659380
-
H. Xiao et al., Mapping protein energy landscapes with amide hydrogen exchange and mass spectrometry: I. A generalized model for a two-state protein and comparison with experiment. Protein Sci. 14, 543-557 (2005). doi: 10.1110/ps.041001705; pmid: 15659380
-
(2005)
Protein Sci.
, vol.14
, pp. 543-557
-
-
Xiao, H.1
-
44
-
-
33645073892
-
Partial unfolding of diverse SH3 domains on a wide timescale
-
pmid: 16487539
-
T. E. Wales, J. R. Engen, Partial unfolding of diverse SH3 domains on a wide timescale. J. Mol. Biol. 357, 1592-1604 (2006). doi: 10.1016/j.jmb.2006.01.075; pmid: 16487539
-
(2006)
J. Mol. Biol.
, vol.357
, pp. 1592-1604
-
-
Wales, T.E.1
Engen, J.R.2
-
45
-
-
84927535922
-
Substrate degradation by the proteasome: A single-molecule kinetic analysis
-
pmid: 25859050
-
Y. Lu, B. H. Lee, R. W. King, D. Finley, M. W. Kirschner, Substrate degradation by the proteasome: A single-molecule kinetic analysis. Science 348, 1250834 (2015). doi: 10.1126/science.1250834; pmid: 25859050
-
(2015)
Science
, vol.348
, pp. 1250834
-
-
Lu, Y.1
Lee, B.H.2
King, R.W.3
Finley, D.4
Kirschner, M.W.5
-
46
-
-
4344559454
-
An unstructured initiation site is required for efficient proteasome-mediated degradation
-
pmid: 15311270
-
S. Prakash, L. Tian, K. S. Ratliff, R. E. Lehotzky, A. Matouschek, An unstructured initiation site is required for efficient proteasome-mediated degradation. Nat. Struct. Mol. Biol. 11, 830-837 (2004). doi: 10.1038/nsmb814; pmid: 15311270
-
(2004)
Nat. Struct. Mol. Biol.
, vol.11
, pp. 830-837
-
-
Prakash, S.1
Tian, L.2
Ratliff, K.S.3
Lehotzky, R.E.4
Matouschek, A.5
-
47
-
-
84898807479
-
Deep classification of a large cryo-EM dataset defines the conformational landscape of the 26S proteasome
-
pmid: 24706844
-
P. Unverdorben et al., Deep classification of a large cryo-EM dataset defines the conformational landscape of the 26S proteasome. Proc. Natl. Acad. Sci. U.S.A. 111, 5544-5549 (2014). doi: 10.1073/pnas.1403409111; pmid: 24706844
-
(2014)
Proc. Natl. Acad. Sci. U.S.A.
, vol.111
, pp. 5544-5549
-
-
Unverdorben, P.1
-
48
-
-
45849131354
-
Recognition dynamics up to microseconds revealed from an RDC-derived ubiquitin ensemble in solution
-
pmid: 18556554
-
O. F. Lange et al., Recognition dynamics up to microseconds revealed from an RDC-derived ubiquitin ensemble in solution. Science 320, 1471-1475 (2008). doi: 10.1126/science.1157092; pmid: 18556554
-
(2008)
Science
, vol.320
, pp. 1471-1475
-
-
Lange, O.F.1
-
49
-
-
84955171039
-
Mycobacterium tuberculosis copperregulated protein SocB is an intrinsically disordered protein that folds upon interaction with a synthetic phospholipid bilayer
-
Pmid: 26650755
-
U. Nowicka et al., Mycobacterium tuberculosis copperregulated protein SocB is an intrinsically disordered protein that folds upon interaction with a synthetic phospholipid bilayer. Proteins 84, 193-200 (2016). doi: 10.1002/prot.24970; pmid: 26650755
-
(2016)
Proteins
, vol.84
, pp. 193-200
-
-
Nowicka, U.1
|