2o6v › Citations

Crystal structure and solution NMR studies of Lys48-linked tetraubiquitin at neutral pH.

Eddins MJ, Varadan R, Fushman D, Pickart CM, Wolberger C
J Mol Biol 367 204-11 (2007)
Cited: 118 times
EuropePMC logo PMID: 17240395

Abstract

Ubiquitin modification of proteins is used as a signal in many cellular processes. Lysine side-chains can be modified by a single ubiquitin or by a polyubiquitin chain, which is defined by an isopeptide bond between the C terminus of one ubiquitin and a specific lysine in a neighboring ubiquitin. Polyubiquitin conformations that result from different lysine linkages presumably differentiate their roles and ability to bind specific targets and enzymes. However, conflicting results have been obtained regarding the precise conformation of Lys48-linked tetraubiquitin. We report the crystal structure of Lys48-linked tetraubiquitin at near-neutral pH. The two tetraubiquitin complexes in the asymmetric unit show the complete connectivity of the chain and the molecular details of the interactions. This tetraubiquitin conformation is consistent with our NMR data as well as with previous studies of diubiquitin and tetraubiquitin in solution at neutral pH. The structure provides a basis for understanding Lys48-linked polyubiquitin recognition under physiological conditions.

Reviews - 2o6v mentioned but not cited (4)

  1. Unraveling the complexity of ubiquitin signaling. Strieter ER, Korasick DA. ACS Chem Biol 7 52-63 (2012)
  2. The WD40-repeat protein-containing deubiquitinase complex: catalysis, regulation, and potential for therapeutic intervention. Villamil MA, Liang Q, Zhuang Z. Cell Biochem Biophys 67 111-126 (2013)
  3. Ubiquitination in the ERAD Process. Lopata A, Kniss A, Löhr F, Rogov VV, Dötsch V. Int J Mol Sci 21 E5369 (2020)
  4. The Role of Cullin-RING Ligases in Striated Muscle Development, Function, and Disease. Blondelle J, Biju A, Lange S. Int J Mol Sci 21 E7936 (2020)

Articles - 2o6v mentioned but not cited (20)

  1. Analyses of the effects of all ubiquitin point mutants on yeast growth rate. Roscoe BP, Thayer KM, Zeldovich KB, Fushman D, Bolon DN. J Mol Biol 425 1363-1377 (2013)
  2. Recovering a representative conformational ensemble from underdetermined macromolecular structural data. Berlin K, Castañeda CA, Schneidman-Duhovny D, Sali A, Nava-Tudela A, Fushman D. J Am Chem Soc 135 16595-16609 (2013)
  3. Understanding the role of the Josephin domain in the PolyUb binding and cleavage properties of ataxin-3. Nicastro G, Todi SV, Karaca E, Bonvin AM, Paulson HL, Pastore A. PLoS One 5 e12430 (2010)
  4. De novo macrocyclic peptides that specifically modulate Lys48-linked ubiquitin chains. Nawatha M, Rogers JM, Bonn SM, Livneh I, Lemma B, Mali SM, Vamisetti GB, Sun H, Bercovich B, Huang Y, Ciechanover A, Fushman D, Suga H, Brik A. Nat Chem 11 644-652 (2019)
  5. The ubiquitin ligase Ubr4 controls stability of podocin/MEC-2 supercomplexes. Rinschen MM, Bharill P, Wu X, Kohli P, Reinert MJ, Kretz O, Saez I, Schermer B, Höhne M, Bartram MP, Aravamudhan S, Brooks BR, Vilchez D, Huber TB, Müller RU, Krüger M, Benzing T. Hum Mol Genet 25 1328-1344 (2016)
  6. A single MIU motif of MINDY-1 recognizes K48-linked polyubiquitin chains. Kristariyanto YA, Abdul Rehman SA, Weidlich S, Knebel A, Kulathu Y. EMBO Rep 18 392-402 (2017)
  7. Structural and biochemical studies of the open state of Lys48-linked diubiquitin. Lai MY, Zhang D, Laronde-Leblanc N, Fushman D. Biochim Biophys Acta 1823 2046-2056 (2012)
  8. Mechanistic insights into enhancement or inhibition of phase separation by different polyubiquitin chains. Dao TP, Yang Y, Presti MF, Cosgrove MS, Hopkins JB, Ma W, Loh SN, Castañeda CA. EMBO Rep 23 e55056 (2022)
  9. Assessing the potential of atomistic molecular dynamics simulations to probe reversible protein-protein recognition and binding. Abriata LA, Dal Peraro M. Sci Rep 5 10549 (2015)
  10. An Extended Conformation for K48 Ubiquitin Chains Revealed by the hRpn2:Rpn13:K48-Diubiquitin Structure. Lu X, Ebelle DL, Matsuo H, Walters KJ. Structure 28 495-506.e3 (2020)
  11. In vivo modulation of ubiquitin chains by N-methylated non-proteinogenic cyclic peptides. Rogers JM, Nawatha M, Lemma B, Vamisetti GB, Livneh I, Barash U, Vlodavsky I, Ciechanover A, Fushman D, Suga H, Brik A. RSC Chem Biol 2 513-522 (2021)
  12. Structural Basis for the Inhibitory Effects of Ubistatins in the Ubiquitin-Proteasome Pathway. Nakasone MA, Lewis TA, Walker O, Thakur A, Mansour W, Castañeda CA, Goeckeler-Fried JL, Parlati F, Chou TF, Hayat O, Zhang D, Camara CM, Bonn SM, Nowicka UK, Krueger S, Glickman MH, Brodsky JL, Deshaies RJ, Fushman D. Structure 25 1839-1855.e11 (2017)
  13. Crystal structure of a complex of NOD1 CARD and ubiquitin. Ver Heul AM, Gakhar L, Piper RC, Subramanian R. PLoS One 9 e104017 (2014)
  14. Nonspecific yet decisive: Ubiquitination can affect the native-state dynamics of the modified protein. Gavrilov Y, Hagai T, Levy Y. Protein Sci 24 1580-1592 (2015)
  15. Comparison of native and non-native ubiquitin oligomers reveals analogous structures and reactivities. Pham GH, Rana AS, Korkmaz EN, Trang VH, Cui Q, Strieter ER. Protein Sci 25 456-471 (2016)
  16. Dynamics of an Active-Site Flap Contributes to Catalysis in a JAMM Family Metallo Deubiquitinase. Bueno AN, Shrestha RK, Ronau JA, Babar A, Sheedlo MJ, Fuchs JE, Paul LN, Das C. Biochemistry 54 6038-6051 (2015)
  17. Recognition of Poly-Ubiquitins by the Proteasome through Protein Refolding Guided by Electrostatic and Hydrophobic Interactions. Zhang Y, Vuković L, Rudack T, Han W, Schulten K. J Phys Chem B 120 8137-8146 (2016)
  18. Crystallographic structure of ubiquitin in complex with cadmium ions. Qureshi IA, Ferron F, Seh CC, Cheung P, Lescar J. BMC Res Notes 2 251 (2009)
  19. Enhancing ubiquitin crystallization through surface-entropy reduction. Loll PJ, Xu P, Schmidt JT, Melideo SL. Acta Crystallogr F Struct Biol Commun 70 1434-1442 (2014)
  20. Mechanism of selective recognition of Lys48-linked polyubiquitin by macrocyclic peptide inhibitors of proteasomal degradation. Lemma B, Zhang D, Vamisetti GB, Wentz BG, Suga H, Brik A, Lubkowski J, Fushman D. Nat Commun 14 7212 (2023)


Reviews citing this publication (31)

  1. The ubiquitin code. Komander D, Rape M. Annu Rev Biochem 81 203-229 (2012)
  2. Regulation and cellular roles of ubiquitin-specific deubiquitinating enzymes. Reyes-Turcu FE, Ventii KH, Wilkinson KD. Annu Rev Biochem 78 363-397 (2009)
  3. Atypical ubiquitylation - the unexplored world of polyubiquitin beyond Lys48 and Lys63 linkages. Kulathu Y, Komander D. Nat Rev Mol Cell Biol 13 508-523 (2012)
  4. Polyubiquitin chains: functions, structures, and mechanisms. Li W, Ye Y. Cell Mol Life Sci 65 2397-2406 (2008)
  5. Constructing and decoding unconventional ubiquitin chains. Behrends C, Harper JW. Nat Struct Mol Biol 18 520-528 (2011)
  6. Balancing act: deubiquitinating enzymes in the nervous system. Todi SV, Paulson HL. Trends Neurosci 34 370-382 (2011)
  7. Polyubiquitin binding and disassembly by deubiquitinating enzymes. Reyes-Turcu FE, Wilkinson KD. Chem Rev 109 1495-1508 (2009)
  8. The diversity of ubiquitin recognition: hot spots and varied specificity. Winget JM, Mayor T. Mol Cell 38 627-635 (2010)
  9. The ubiquitin landscape at DNA double-strand breaks. Messick TE, Greenberg RA. J Cell Biol 187 319-326 (2009)
  10. The complexity of recognition of ubiquitinated substrates by the 26S proteasome. Ciechanover A, Stanhill A. Biochim Biophys Acta 1843 86-96 (2014)
  11. Substrate specificity of the ubiquitin and Ubl proteases. Ronau JA, Beckmann JF, Hochstrasser M. Cell Res 26 441-456 (2016)
  12. The role of Ubiquitination in Apoptosis and Necroptosis. Roberts JZ, Crawford N, Longley DB. Cell Death Differ 29 272-284 (2022)
  13. Chemistry and biology of the ubiquitin signal. Spasser L, Brik A. Angew Chem Int Ed Engl 51 6840-6862 (2012)
  14. The multiple layers of ubiquitin-dependent cell cycle control. Wickliffe K, Williamson A, Jin L, Rape M. Chem Rev 109 1537-1548 (2009)
  15. Breakdown of endocytosis in the oncogenic activation of receptor tyrosine kinases. Abella JV, Park M. Am J Physiol Endocrinol Metab 296 E973-84 (2009)
  16. Structure characterization of the 26S proteasome. Kim HM, Yu Y, Cheng Y. Biochim Biophys Acta 1809 67-79 (2011)
  17. Met1-linked ubiquitination in immune signalling. Fiil BK, Gyrd-Hansen M. FEBS J 281 4337-4350 (2014)
  18. Structure, Dynamics and Function of the 26S Proteasome. Mao Y. Subcell Biochem 96 1-151 (2021)
  19. Development of inhibitors in the ubiquitination cascade. Zhang W, Sidhu SS. FEBS Lett 588 356-367 (2014)
  20. Multitasking with ubiquitin through multivalent interactions. Liu F, Walters KJ. Trends Biochem Sci 35 352-360 (2010)
  21. Design principles of a universal protein degradation machine. Matyskiela ME, Martin A. J Mol Biol 425 199-213 (2013)
  22. Proteasome in action: substrate degradation by the 26S proteasome. Sahu I, Glickman MH. Biochem Soc Trans 49 629-644 (2021)
  23. Specificity and disease in the ubiquitin system. Chaugule VK, Walden H. Biochem Soc Trans 44 212-227 (2016)
  24. Ubiquitin and its binding domains. Randles L, Walters KJ. Front Biosci (Landmark Ed) 17 2140-2157 (2012)
  25. Protein Engineering in the Ubiquitin System: Tools for Discovery and Beyond. Zhao B, Tsai YC, Jin B, Wang B, Wang Y, Zhou H, Carpenter T, Weissman AM, Yin J. Pharmacol Rev 72 380-413 (2020)
  26. Post translational modification of Parkin. Chakraborty J, Basso V, Ziviani E. Biol Direct 12 6 (2017)
  27. Deubiquitinating Enzymes Related to Autophagy: New Therapeutic Opportunities? Jacomin AC, Taillebourg E, Fauvarque MO. Cells 7 E112 (2018)
  28. RAP80, ubiquitin and SUMO in the DNA damage response. Lombardi PM, Matunis MJ, Wolberger C. J Mol Med (Berl) 95 799-807 (2017)
  29. Non-enzymatic synthesis of ubiquitin chains: where chemistry makes a difference. Hemantha HP, Brik A. Bioorg Med Chem 21 3411-3420 (2013)
  30. The ubiquitin codes in cellular stress responses. Sheng X, Xia Z, Yang H, Hu R. Protein Cell 15 157-190 (2024)
  31. Using protein motion to read, write, and erase ubiquitin signals. Phillips AH, Corn JE. J Biol Chem 290 26437-26444 (2015)

Articles citing this publication (63)

  1. Complete subunit architecture of the proteasome regulatory particle. Lander GC, Estrin E, Matyskiela ME, Bashore C, Nogales E, Martin A. Nature 482 186-191 (2012)
  2. Molecular discrimination of structurally equivalent Lys 63-linked and linear polyubiquitin chains. Komander D, Reyes-Turcu F, Licchesi JD, Odenwaelder P, Wilkinson KD, Barford D. EMBO Rep 10 466-473 (2009)
  3. K11-linked polyubiquitination in cell cycle control revealed by a K11 linkage-specific antibody. Matsumoto ML, Wickliffe KE, Dong KC, Yu C, Bosanac I, Bustos D, Phu L, Kirkpatrick DS, Hymowitz SG, Rape M, Kelley RF, Dixit VM. Mol Cell 39 477-484 (2010)
  4. Engineered diubiquitin synthesis reveals Lys29-isopeptide specificity of an OTU deubiquitinase. Virdee S, Ye Y, Nguyen DP, Komander D, Chin JW. Nat Chem Biol 6 750-757 (2010)
  5. The deubiquitinating enzyme ataxin-3, a polyglutamine disease protein, edits Lys63 linkages in mixed linkage ubiquitin chains. Winborn BJ, Travis SM, Todi SV, Scaglione KM, Xu P, Williams AJ, Cohen RE, Peng J, Paulson HL. J Biol Chem 283 26436-26443 (2008)
  6. Structural Basis for the Ubiquitin-Linkage Specificity and deISGylating activity of SARS-CoV papain-like protease. Ratia K, Kilianski A, Baez-Santos YM, Baker SC, Mesecar A. PLoS Pathog 10 e1004113 (2014)
  7. The E3 ligase RNF8 regulates KU80 removal and NHEJ repair. Feng L, Chen J. Nat Struct Mol Biol 19 201-206 (2012)
  8. Affinity makes the difference: nonselective interaction of the UBA domain of Ubiquilin-1 with monomeric ubiquitin and polyubiquitin chains. Zhang D, Raasi S, Fushman D. J Mol Biol 377 162-180 (2008)
  9. Ubiquitin chain conformation regulates recognition and activity of interacting proteins. Ye Y, Blaser G, Horrocks MH, Ruedas-Rama MJ, Ibrahim S, Zhukov AA, Orte A, Klenerman D, Jackson SE, Komander D. Nature 492 266-270 (2012)
  10. Total chemical synthesis of di-ubiquitin chains. Kumar KS, Spasser L, Erlich LA, Bavikar SN, Brik A. Angew Chem Int Ed Engl 49 9126-9131 (2010)
  11. Engineering and structural characterization of a linear polyubiquitin-specific antibody. Matsumoto ML, Dong KC, Yu C, Phu L, Gao X, Hannoush RN, Hymowitz SG, Kirkpatrick DS, Dixit VM, Kelley RF. J Mol Biol 418 134-144 (2012)
  12. Recognition of polyubiquitin isoforms by the multiple ubiquitin binding modules of isopeptidase T. Reyes-Turcu FE, Shanks JR, Komander D, Wilkinson KD. J Biol Chem 283 19581-19592 (2008)
  13. Structure of proteasome ubiquitin receptor hRpn13 and its activation by the scaffolding protein hRpn2. Chen X, Lee BH, Finley D, Walters KJ. Mol Cell 38 404-415 (2010)
  14. The structure and conformation of Lys63-linked tetraubiquitin. Datta AB, Hura GL, Wolberger C. J Mol Biol 392 1117-1124 (2009)
  15. Total chemical synthesis of a 304 amino acid K48-linked tetraubiquitin protein. Kumar KS, Bavikar SN, Spasser L, Moyal T, Ohayon S, Brik A. Angew Chem Int Ed Engl 50 6137-6141 (2011)
  16. The ubiquitination code: a signalling problem. Woelk T, Sigismund S, Penengo L, Polo S. Cell Div 2 11 (2007)
  17. An FTS/Hook/p107(FHIP) complex interacts with and promotes endosomal clustering by the homotypic vacuolar protein sorting complex. Xu L, Sowa ME, Chen J, Li X, Gygi SP, Harper JW. Mol Biol Cell 19 5059-5071 (2008)
  18. Trabid, a new positive regulator of Wnt-induced transcription with preference for binding and cleaving K63-linked ubiquitin chains. Tran H, Hamada F, Schwarz-Romond T, Bienz M. Genes Dev 22 528-542 (2008)
  19. Nonenzymatic assembly of natural polyubiquitin chains of any linkage composition and isotopic labeling scheme. Castañeda C, Liu J, Chaturvedi A, Nowicka U, Cropp TA, Fushman D. J Am Chem Soc 133 17855-17868 (2011)
  20. Chemical synthesis of ubiquitinated peptides with varying lengths and types of ubiquitin chains to explore the activity of deubiquitinases. Bavikar SN, Spasser L, Haj-Yahya M, Karthikeyan SV, Moyal T, Kumar KS, Brik A. Angew Chem Int Ed Engl 51 758-763 (2012)
  21. Protein-linked ubiquitin chain structure restricts activity of deubiquitinating enzymes. Schaefer JB, Morgan DO. J Biol Chem 286 45186-45196 (2011)
  22. Substrate filtering by the active site crossover loop in UCHL3 revealed by sortagging and gain-of-function mutations. Popp MW, Artavanis-Tsakonas K, Ploegh HL. J Biol Chem 284 3593-3602 (2009)
  23. Exploring the linkage dependence of polyubiquitin conformations using molecular modeling. Fushman D, Walker O. J Mol Biol 395 803-814 (2010)
  24. Direct Sensing and Discrimination among Ubiquitin and Ubiquitin Chains Using Solid-State Nanopores. Nir I, Huttner D, Meller A. Biophys J 108 2340-2349 (2015)
  25. Structure and recognition of polyubiquitin chains of different lengths and linkage. Fushman D, Wilkinson KD. F1000 Biol Rep 3 26 (2011)
  26. Targeting the ubiquitin E3 ligase MuRF1 to inhibit muscle atrophy. Eddins MJ, Marblestone JG, Suresh Kumar KG, Leach CA, Sterner DE, Mattern MR, Nicholson B. Cell Biochem Biophys 60 113-118 (2011)
  27. Linkage-specific conformational ensembles of non-canonical polyubiquitin chains. Castañeda CA, Chaturvedi A, Camara CM, Curtis JE, Krueger S, Fushman D. Phys Chem Chem Phys 18 5771-5788 (2016)
  28. Recognition and cleavage of related to ubiquitin 1 (Rub1) and Rub1-ubiquitin chains by components of the ubiquitin-proteasome system. Singh RK, Zerath S, Kleifeld O, Scheffner M, Glickman MH, Fushman D. Mol Cell Proteomics 11 1595-1611 (2012)
  29. Both K63 and K48 ubiquitin linkages signal lysosomal degradation of the LDL receptor. Zhang L, Xu M, Scotti E, Chen ZJ, Tontonoz P. J Lipid Res 54 1410-1420 (2013)
  30. Crystal structures of Lys-63-linked tri- and di-ubiquitin reveal a highly extended chain architecture. Weeks SD, Grasty KC, Hernandez-Cuebas L, Loll PJ. Proteins 77 753-759 (2009)
  31. Branching via K11 and K48 Bestows Ubiquitin Chains with a Unique Interdomain Interface and Enhanced Affinity for Proteasomal Subunit Rpn1. Boughton AJ, Krueger S, Fushman D. Structure 28 29-43.e6 (2020)
  32. Conformational dynamics of wild-type Lys-48-linked diubiquitin in solution. Hirano T, Serve O, Yagi-Utsumi M, Takemoto E, Hiromoto T, Satoh T, Mizushima T, Kato K. J Biol Chem 286 37496-37502 (2011)
  33. Disassembly of Lys11 and mixed linkage polyubiquitin conjugates provides insights into function of proteasomal deubiquitinases Rpn11 and Ubp6. Mansour W, Nakasone MA, von Delbrück M, Yu Z, Krutauz D, Reis N, Kleifeld O, Sommer T, Fushman D, Glickman MH. J Biol Chem 290 4688-4704 (2015)
  34. The Colossus of ubiquitylation: decrypting a cellular code. Williamson A, Werner A, Rape M. Mol Cell 49 591-600 (2013)
  35. Site-specific ubiquitination affects protein energetics and proteasomal degradation. Carroll EC, Greene ER, Martin A, Marqusee S. Nat Chem Biol 16 866-875 (2020)
  36. Transcriptomic and epigenetic regulation of disuse atrophy and the return to activity in skeletal muscle. Fisher AG, Seaborne RA, Hughes TM, Gutteridge A, Stewart C, Coulson JM, Sharples AP, Jarvis JC. FASEB J 31 5268-5282 (2017)
  37. Structural insight into SUMO chain recognition and manipulation by the ubiquitin ligase RNF4. Xu Y, Plechanovová A, Simpson P, Marchant J, Leidecker O, Kraatz S, Hay RT, Matthews SJ. Nat Commun 5 4217 (2014)
  38. Non-degradative Ubiquitination of Protein Kinases. Ball KA, Johnson JR, Lewinski MK, Guatelli J, Verschueren E, Krogan NJ, Jacobson MP. PLoS Comput Biol 12 e1004898 (2016)
  39. Lys63-linked ubiquitin chain adopts multiple conformational states for specific target recognition. Liu Z, Gong Z, Jiang WX, Yang J, Zhu WK, Guo DC, Zhang WP, Liu ML, Tang C. Elife 4 (2015)
  40. PolyUbiquitin chain linkage topology selects the functions from the underlying binding landscape. Wang Y, Tang C, Wang E, Wang J. PLoS Comput Biol 10 e1003691 (2014)
  41. Segmental isotopic labeling of ubiquitin chains to unravel monomer-specific molecular behavior. Castañeda CA, Spasser L, Bavikar SN, Brik A, Fushman D. Angew Chem Int Ed Engl 50 11210-11214 (2011)
  42. Stabilization of an unusual salt bridge in ubiquitin by the extra C-terminal domain of the proteasome-associated deubiquitinase UCH37 as a mechanism of its exo specificity. Morrow ME, Kim MI, Ronau JA, Sheedlo MJ, White RR, Chaney J, Paul LN, Lill MA, Artavanis-Tsakonas K, Das C. Biochemistry 52 3564-3578 (2013)
  43. Structural analysis of the UBA domain of X-linked inhibitor of apoptosis protein reveals different surfaces for ubiquitin-binding and self-association. Tse MK, Hui SK, Yang Y, Yin ST, Hu HY, Zou B, Wong BC, Sze KH. PLoS One 6 e28511 (2011)
  44. Modifying the vicinity of the isopeptide bond to reveal differential behavior of ubiquitin chains with interacting proteins: organic chemistry applied to synthetic proteins. Haj-Yahya N, Haj-Yahya M, Castañeda CA, Spasser L, Hemantha HP, Jbara M, Penner M, Ciechanover A, Fushman D, Brik A. Angew Chem Int Ed Engl 52 11149-11153 (2013)
  45. Structure of a compact conformation of linear diubiquitin. Rohaim A, Kawasaki M, Kato R, Dikic I, Wakatsuki S. Acta Crystallogr D Biol Crystallogr 68 102-108 (2012)
  46. Mechanism of activation and regulation of deubiquitinase activity in MINDY1 and MINDY2. Abdul Rehman SA, Armstrong LA, Lange SM, Kristariyanto YA, Gräwert TW, Knebel A, Svergun DI, Kulathu Y. Mol Cell 81 4176-4190.e6 (2021)
  47. Structural insights into the activity and regulation of human Josephin-2. Grasty KC, Weeks SD, Loll PJ. J Struct Biol X 3 100011 (2019)
  48. NMR analysis of Lys63-linked polyubiquitin recognition by the tandem ubiquitin-interacting motifs of Rap80. Sekiyama N, Jee J, Isogai S, Akagi K, Huang TH, Ariyoshi M, Tochio H, Shirakawa M. J Biomol NMR 52 339-350 (2012)
  49. Recent advances in polyubiquitin chain recognition. Wu H, Lo YC, Lin SC. F1000 Biol Rep 2 1-5 (2010)
  50. A snapshot of ubiquitin chain elongation: lysine 48-tetra-ubiquitin slows down ubiquitination. Kovacev J, Wu K, Spratt DE, Chong RA, Lee C, Nayak J, Shaw GS, Pan ZQ. J Biol Chem 289 7068-7081 (2014)
  51. Letter Simultaneous detection of distinct ubiquitin chain topologies by 19F NMR. Shekhawat SS, Pham GH, Prabakaran J, Strieter ER. ACS Chem Biol 9 2229-2236 (2014)
  52. Selective macrocyclic peptide modulators of Lys63-linked ubiquitin chains disrupt DNA damage repair. Vamisetti GB, Saha A, Huang YJ, Vanjari R, Mann G, Gutbrod J, Ayoub N, Suga H, Brik A. Nat Commun 13 6174 (2022)
  53. Adaptor linked K63 di-ubiquitin activates Nedd4/Rsp5 E3 ligase. Zhu L, Zhang Q, Cordeiro CD, Banjade S, Sardana R, Mao Y, Emr SD. Elife 11 e77424 (2022)
  54. Solution structure of lysine-free (K0) ubiquitin. Huang T, Li J, Byrd RA. Protein Sci 23 662-667 (2014)
  55. Purification, crystallization and preliminary crystallographic studies of Lys48-linked polyubiquitin chains. Morimoto D, Isogai S, Tenno T, Tochio H, Shirakawa M, Ariyoshi M. Acta Crystallogr Sect F Struct Biol Cryst Commun 66 834-837 (2010)
  56. The pros and cons of ubiquitination on the formation of protein condensates. Hou XN, Tang C. Acta Biochim Biophys Sin (Shanghai) 55 1084-1098 (2023)
  57. The acetylase activity of Cdu1 regulates bacterial exit from infected cells by protecting Chlamydia effectors from degradation. Bastidas RJ, Kędzior M, Davidson RK, Walsh SC, Dolat L, Sixt BS, Pruneda JN, Coers J, Valdivia RH. Elife 12 RP87386 (2024)
  58. Intrinsic site-selectivity of ubiquitin dimer formation. Andersen KA, Martin LJ, Prince JM, Raines RT. Protein Sci 24 182-189 (2015)
  59. K48- and K63-linked ubiquitin chain interactome reveals branch- and length-specific ubiquitin interactors. Waltho A, Popp O, Lenz C, Pluska L, Lambert M, Dötsch V, Mertins P, Sommer T. Life Sci Alliance 7 e202402740 (2024)
  60. NMR Characterization of Conformational Interconversions of Lys48-Linked Ubiquitin Chains. Hiranyakorn M, Yanaka S, Satoh T, Wilasri T, Jityuti B, Yagi-Utsumi M, Kato K. Int J Mol Sci 21 E5351 (2020)
  61. Probing the cell delivery of synthetic diubiquitin chains. Mandal S, Brik A. Chem Commun (Camb) 58 8782-8785 (2022)
  62. Using antiubiquitin antibodies to probe the ubiquitination state within rhTRIM5α cytoplasmic bodies. Danielson CM, Hope TJ. AIDS Res Hum Retroviruses 29 1373-1385 (2013)
  63. Diagnosing and mitigating method-based avidity artifacts that confound polyubiquitin-binding assays. Schoeffler AJ, Helgason E, Popovych N, Dueber EC. Biophys Rep (N Y) 1 100033 (2021)


Quick links