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For: Fukuda Y, Beck F, Plitzko JM, Baumeister W. In situ structural studies of tripeptidyl peptidase II (TPPII) reveal spatial association with proteasomes. Proc Natl Acad Sci U S A 2017;114:4412-7. [PMID: 28396430 DOI: 10.1073/pnas.1701367114] [Cited by in Crossref: 19] [Cited by in F6Publishing: 18] [Article Influence: 3.8] [Reference Citation Analysis]
Number Citing Articles
1 Jiang W, Wagner J, Du W, Plitzko J, Baumeister W, Beck F, Guo Q. A transformation clustering algorithm and its application in polyribosomes structural profiling. Nucleic Acids Research 2022. [DOI: 10.1093/nar/gkac547] [Cited by in Crossref: 1] [Article Influence: 1.0] [Reference Citation Analysis]
2 Foster HE, Ventura Santos C, Carter AP. A cryo-ET survey of microtubules and intracellular compartments in mammalian axons. J Cell Biol 2022;221:e202103154. [PMID: 34878519 DOI: 10.1083/jcb.202103154] [Cited by in F6Publishing: 5] [Reference Citation Analysis]
3 Croxford M, Elbaum M, Arigovindan M, Kam Z, Agard D, Villa E, Sedat J. Entropy-regularized deconvolution of cellular cryotransmission electron tomograms. Proc Natl Acad Sci U S A 2021;118:e2108738118. [PMID: 34876518 DOI: 10.1073/pnas.2108738118] [Cited by in F6Publishing: 2] [Reference Citation Analysis]
4 Narayan V, McMahon M, O'Brien JJ, McAllister F, Buffenstein R. Insights into the Molecular Basis of Genome Stability and Pristine Proteostasis in Naked Mole-Rats. Adv Exp Med Biol 2021;1319:287-314. [PMID: 34424521 DOI: 10.1007/978-3-030-65943-1_11] [Reference Citation Analysis]
5 Reboud-Ravaux M. [The proteasome - structural aspects and inhibitors: a second life for a validated drug target]. Biol Aujourdhui 2021;215:1-23. [PMID: 34397372 DOI: 10.1051/jbio/2021005] [Cited by in Crossref: 1] [Cited by in F6Publishing: 1] [Article Influence: 1.0] [Reference Citation Analysis]
6 Floyd BM, Drew K, Marcotte EM. Systematic Identification of Protein Phosphorylation-Mediated Interactions. J Proteome Res 2021;20:1359-70. [PMID: 33476154 DOI: 10.1021/acs.jproteome.0c00750] [Cited by in F6Publishing: 5] [Reference Citation Analysis]
7 Turk M, Baumeister W. The promise and the challenges of cryo-electron tomography. FEBS Lett 2020;594:3243-61. [PMID: 33020915 DOI: 10.1002/1873-3468.13948] [Cited by in Crossref: 29] [Cited by in F6Publishing: 62] [Article Influence: 14.5] [Reference Citation Analysis]
8 Greene ER, Dong KC, Martin A. Understanding the 26S proteasome molecular machine from a structural and conformational dynamics perspective. Curr Opin Struct Biol 2020;61:33-41. [PMID: 31783300 DOI: 10.1016/j.sbi.2019.10.004] [Cited by in Crossref: 15] [Cited by in F6Publishing: 22] [Article Influence: 5.0] [Reference Citation Analysis]
9 Tomkinson B. Tripeptidyl-peptidase II: Update on an oldie that still counts. Biochimie 2019;166:27-37. [DOI: 10.1016/j.biochi.2019.05.012] [Cited by in Crossref: 3] [Cited by in F6Publishing: 3] [Article Influence: 1.0] [Reference Citation Analysis]
10 Wang HW, Fan X. Challenges and opportunities in cryo-EM with phase plate. Curr Opin Struct Biol 2019;58:175-82. [PMID: 31374473 DOI: 10.1016/j.sbi.2019.06.013] [Cited by in Crossref: 10] [Cited by in F6Publishing: 10] [Article Influence: 3.3] [Reference Citation Analysis]
11 Zhang P. Advances in cryo-electron tomography and subtomogram averaging and classification. Curr Opin Struct Biol 2019;58:249-58. [PMID: 31280905 DOI: 10.1016/j.sbi.2019.05.021] [Cited by in Crossref: 35] [Cited by in F6Publishing: 35] [Article Influence: 11.7] [Reference Citation Analysis]
12 Pfeffer S, Mahamid J. Unravelling molecular complexity in structural cell biology. Curr Opin Struct Biol 2018;52:111-8. [PMID: 30339965 DOI: 10.1016/j.sbi.2018.08.009] [Cited by in Crossref: 36] [Cited by in F6Publishing: 27] [Article Influence: 9.0] [Reference Citation Analysis]
13 Englmeier R, Förster F. Cryo-electron tomography for the structural study of mitochondrial translation. Tissue Cell 2019;57:129-38. [PMID: 30197222 DOI: 10.1016/j.tice.2018.08.009] [Cited by in F6Publishing: 4] [Reference Citation Analysis]
14 Elbaum M. Expanding horizons of cryo-tomography to larger volumes. Current Opinion in Microbiology 2018;43:155-61. [DOI: 10.1016/j.mib.2018.01.001] [Cited by in Crossref: 6] [Cited by in F6Publishing: 5] [Article Influence: 1.5] [Reference Citation Analysis]
15 Mishra R, Upadhyay A, Prajapati VK, Mishra A. Proteasome-mediated proteostasis: Novel medicinal and pharmacological strategies for diseases. Med Res Rev 2018;38:1916-73. [DOI: 10.1002/med.21502] [Cited by in Crossref: 14] [Cited by in F6Publishing: 16] [Article Influence: 3.5] [Reference Citation Analysis]
16 Anderson KL, Page C, Swift MF, Hanein D, Volkmann N. Marker-free method for accurate alignment between correlated light, cryo-light, and electron cryo-microscopy data using sample support features. J Struct Biol 2018;201:46-51. [PMID: 29113849 DOI: 10.1016/j.jsb.2017.11.001] [Cited by in Crossref: 11] [Cited by in F6Publishing: 10] [Article Influence: 2.2] [Reference Citation Analysis]
17 Wagner J, Schaffer M, Fernández-Busnadiego R. Cryo-electron tomography-the cell biology that came in from the cold. FEBS Lett 2017;591:2520-33. [PMID: 28726246 DOI: 10.1002/1873-3468.12757] [Cited by in Crossref: 35] [Cited by in F6Publishing: 31] [Article Influence: 7.0] [Reference Citation Analysis]
18 Chung JM, Jung HS. Cryo-electron tomography: A tool for in situ structural analysis of macromolecular complexes. Applied Spectroscopy Reviews 2017;53:195-202. [DOI: 10.1080/05704928.2017.1328426] [Cited by in Crossref: 3] [Cited by in F6Publishing: 1] [Article Influence: 0.6] [Reference Citation Analysis]
19 [DOI: 10.1101/2021.04.26.441469] [Cited by in Crossref: 1] [Cited by in F6Publishing: 2] [Reference Citation Analysis]