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For: Schuller AP, Wojtynek M, Mankus D, Tatli M, Kronenberg-Tenga R, Regmi SG, Dip PV, Lytton-Jean AKR, Brignole EJ, Dasso M, Weis K, Medalia O, Schwartz TU. The cellular environment shapes the nuclear pore complex architecture. Nature 2021;598:667-71. [PMID: 34646014 DOI: 10.1038/s41586-021-03985-3] [Cited by in Crossref: 54] [Cited by in F6Publishing: 62] [Article Influence: 54.0] [Reference Citation Analysis]
Number Citing Articles
1 Guaita M, Watters SC, Loerch S. Recent advances and current trends in cryo-electron microscopy. Current Opinion in Structural Biology 2022;77:102484. [DOI: 10.1016/j.sbi.2022.102484] [Reference Citation Analysis]
2 Pesce M, Duda GN, Forte G, Girao H, Raya A, Roca-cusachs P, Sluijter JPG, Tschöpe C, Van Linthout S. Cardiac fibroblasts and mechanosensation in heart development, health and disease. Nat Rev Cardiol 2022. [DOI: 10.1038/s41569-022-00799-2] [Reference Citation Analysis]
3 Weber M, von der Emde H, Leutenegger M, Gunkel P, Sambandan S, Khan TA, Keller-findeisen J, Cordes VC, Hell SW. MINSTED nanoscopy enters the Ångström localization range. Nat Biotechnol 2022. [DOI: 10.1038/s41587-022-01519-4] [Cited by in Crossref: 1] [Cited by in F6Publishing: 1] [Article Influence: 1.0] [Reference Citation Analysis]
4 Andronov L, Genthial R, Hentsch D, Klaholz BP. splitSMLM, a spectral demixing method for high-precision multi-color localization microscopy applied to nuclear pore complexes. Commun Biol 2022;5:1100. [PMID: 36253454 DOI: 10.1038/s42003-022-04040-1] [Reference Citation Analysis]
5 Ng SC, Biswas A, Huyton T, Schünemann J, Reber S, Görlich D. Barrier-properties of Nup98 FG phases ruled by FG motif identity and inter-FG spacer length.. [DOI: 10.1101/2022.10.14.512266] [Reference Citation Analysis]
6 Bryant P, Pozzati G, Zhu W, Shenoy A, Kundrotas P, Elofsson A. Predicting the structure of large protein complexes using AlphaFold and Monte Carlo tree search. Nat Commun 2022;13:6028. [PMID: 36224222 DOI: 10.1038/s41467-022-33729-4] [Reference Citation Analysis]
7 Ashkenazy-Titelman A, Atrash MK, Boocholez A, Kinor N, Shav-Tal Y. RNA export through the nuclear pore complex is directional. Nat Commun 2022;13:5881. [PMID: 36202822 DOI: 10.1038/s41467-022-33572-7] [Reference Citation Analysis]
8 Wang C, Wojtynek M, Medalia O. Structural investigation of eukaryotic cells: From the periphery to the interior by cryo-electron tomography. Advances in Biological Regulation 2022. [DOI: 10.1016/j.jbior.2022.100923] [Reference Citation Analysis]
9 Mannino PJ, Lusk CP. Quality control mechanisms that protect nuclear envelope identity and function. J Cell Biol 2022;221:e202205123. [PMID: 36036741 DOI: 10.1083/jcb.202205123] [Reference Citation Analysis]
10 Winogradoff D, Chou HY, Maffeo C, Aksimentiev A. Percolation transition prescribes protein size-specific barrier to passive transport through the nuclear pore complex. Nat Commun 2022;13:5138. [PMID: 36050301 DOI: 10.1038/s41467-022-32857-1] [Cited by in Crossref: 1] [Cited by in F6Publishing: 1] [Article Influence: 1.0] [Reference Citation Analysis]
11 Xue H, Zhang M, Liu J, Wang J, Ren G. Cryo-electron tomography related radiation-damage parameters for individual-molecule 3D structure determination. Front Chem 2022;10:889203. [DOI: 10.3389/fchem.2022.889203] [Reference Citation Analysis]
12 Kralt A, Wojtynek M, Fischer JS, Agote-Aran A, Mancini R, Dultz E, Noor E, Uliana F, Tatarek-Nossol M, Antonin W, Onischenko E, Medalia O, Weis K. An amphipathic helix in Brl1 is required for nuclear pore complex biogenesis in S. cerevisiae. Elife 2022;11:e78385. [PMID: 36000978 DOI: 10.7554/eLife.78385] [Cited by in Crossref: 1] [Cited by in F6Publishing: 1] [Article Influence: 1.0] [Reference Citation Analysis]
13 Hu D, Dong Z, Li B, Lu F, Li Y. Mechanical Force Directs Proliferation and Differentiation of Stem Cells. Tissue Engineering Part B: Reviews 2022. [DOI: 10.1089/ten.teb.2022.0052] [Reference Citation Analysis]
14 Dai S, Liu S, Zhou C, Yu F, Zhu G, Zhang W, Deng H, Burlingame A, Yu W, Wang T, Li N. Capturing the Hierarchically Assorted Modules of Protein Interaction in the Organized Nucleome.. [DOI: 10.1101/2022.08.14.503837] [Reference Citation Analysis]
15 Gallusser B, Maltese G, Di Caprio G, Vadakkan TJ, Sanyal A, Somerville E, Sahasrabudhe M, O’connor J, Weigert M, Kirchhausen T. Deep neural network automated segmentation of cellular structures in volume electron microscopy.. [DOI: 10.1101/2022.08.02.502534] [Reference Citation Analysis]
16 Francis AC, Cereseto A, Singh PK, Shi J, Poeschla E, Engelman AN, Aiken C, Melikyan GB. Localization and functions of native and eGFP-tagged capsid proteins in HIV-1 particles. PLoS Pathog 2022;18:e1010754. [PMID: 35951676 DOI: 10.1371/journal.ppat.1010754] [Cited by in Crossref: 1] [Cited by in F6Publishing: 1] [Article Influence: 1.0] [Reference Citation Analysis]
17 Mauro MS, Celma G, Zimyanin V, Magaj MM, Gibson KH, Redemann S, Bahmanyar S. Ndc1 drives nuclear pore complex assembly independent of membrane biogenesis to promote nuclear formation and growth. Elife 2022;11:e75513. [PMID: 35852146 DOI: 10.7554/eLife.75513] [Cited by in Crossref: 2] [Cited by in F6Publishing: 2] [Article Influence: 2.0] [Reference Citation Analysis]
18 Yu M, Heidari M, Mikhaleva S, Tan P, Mingu S, Ruan H, Reinkermeier C, Obarska-kosinska A, Siggel M, Beck M, Hummer G, Lemke E. Deciphering the conformations and dynamics of FG-nucleoporins in situ.. [DOI: 10.1101/2022.07.07.499201] [Reference Citation Analysis]
19 Fragasso A, de Vries HW, Andersson J, van der Sluis EO, van der Giessen E, Onck PR, Dekker C. Transport receptor occupancy in nuclear pore complex mimics. Nano Res . [DOI: 10.1007/s12274-022-4647-1] [Cited by in Crossref: 3] [Article Influence: 3.0] [Reference Citation Analysis]
20 Schwartz TU. Solving the nuclear pore puzzle. Science 2022;376:1158-9. [PMID: 35679398 DOI: 10.1126/science.abq4792] [Cited by in Crossref: 4] [Cited by in F6Publishing: 2] [Article Influence: 4.0] [Reference Citation Analysis]
21 Petrovic S, Samanta D, Perriches T, Bley CJ, Thierbach K, Brown B, Nie S, Mobbs GW, Stevens TA, Liu X, Tomaleri GP, Schaus L, Hoelz A. Architecture of the linker-scaffold in the nuclear pore. Science 2022;376:eabm9798. [PMID: 35679425 DOI: 10.1126/science.abm9798] [Cited by in Crossref: 3] [Cited by in F6Publishing: 5] [Article Influence: 3.0] [Reference Citation Analysis]
22 Bley CJ, Nie S, Mobbs GW, Petrovic S, Gres AT, Liu X, Mukherjee S, Harvey S, Huber FM, Lin DH, Brown B, Tang AW, Rundlet EJ, Correia AR, Chen S, Regmi SG, Stevens TA, Jette CA, Dasso M, Patke A, Palazzo AF, Kossiakoff AA, Hoelz A. Architecture of the cytoplasmic face of the nuclear pore. Science 2022;376:eabm9129. [PMID: 35679405 DOI: 10.1126/science.abm9129] [Cited by in Crossref: 3] [Cited by in F6Publishing: 4] [Article Influence: 3.0] [Reference Citation Analysis]
23 Mosalaganti S, Obarska-Kosinska A, Siggel M, Taniguchi R, Turoňová B, Zimmerli CE, Buczak K, Schmidt FH, Margiotta E, Mackmull MT, Hagen WJH, Hummer G, Kosinski J, Beck M. AI-based structure prediction empowers integrative structural analysis of human nuclear pores. Science 2022;376:eabm9506. [PMID: 35679397 DOI: 10.1126/science.abm9506] [Cited by in Crossref: 10] [Cited by in F6Publishing: 10] [Article Influence: 10.0] [Reference Citation Analysis]
24 Pennacchio FA, Poli A, Pramotton FM, Lavore S, Rancati I, Cinquanta M, Vorselen D, Prina E, Romano OM, Ferrari A, Piel M, Lagomarsino MC, Maiuri P. Force-biased nuclear import sets nuclear-cytoplasmic volumetric coupling by osmosis.. [DOI: 10.1101/2022.06.07.494975] [Cited by in Crossref: 1] [Cited by in F6Publishing: 1] [Article Influence: 1.0] [Reference Citation Analysis]
25 Andreu I, Granero-Moya I, Chahare NR, Clein K, Molina-Jordán M, Beedle AEM, Elosegui-Artola A, Abenza JF, Rossetti L, Trepat X, Raveh B, Roca-Cusachs P. Mechanical force application to the nucleus regulates nucleocytoplasmic transport. Nat Cell Biol 2022;24:896-905. [PMID: 35681009 DOI: 10.1038/s41556-022-00927-7] [Cited by in Crossref: 4] [Cited by in F6Publishing: 5] [Article Influence: 4.0] [Reference Citation Analysis]
26 Andreu I, Granero-Moya I, Garcia-Manyes S, Roca-Cusachs P. Understanding the role of mechanics in nucleocytoplasmic transport. APL Bioeng 2022;6:020901. [PMID: 35783457 DOI: 10.1063/5.0076034] [Cited by in F6Publishing: 1] [Reference Citation Analysis]
27 Tingey M, Li Y, Yu W, Young A, Yang W. Spelling out the roles of individual nucleoporins in nuclear export of mRNA. Nucleus 2022;13:170-93. [PMID: 35593254 DOI: 10.1080/19491034.2022.2076965] [Reference Citation Analysis]
28 Heckmann M, Pauli M. Visualizing Presynaptic Active Zones and Synaptic Vesicles. Front Synaptic Neurosci 2022;14:901341. [DOI: 10.3389/fnsyn.2022.901341] [Reference Citation Analysis]
29 Theiss M, Hériché J, Russell C, Helekal D, Soppitt A, Ries J, Ellenberg J, Brazma A, Uhlmann V. Simulating structurally variable Nuclear Pore Complexes for Microscopy.. [DOI: 10.1101/2022.05.17.492295] [Cited by in Crossref: 1] [Cited by in F6Publishing: 1] [Article Influence: 1.0] [Reference Citation Analysis]
30 Gwosch KC, Balzarotti F, Pape JK, Hoess P, Ellenberg J, Ries J, Matti U, Schmidt R, Sahl SJ, Hell SW. Assessment of 3D MINFLUX data for quantitative structural biology in cells revisited.. [DOI: 10.1101/2022.05.13.491065] [Reference Citation Analysis]
31 Kalukula Y, Stephens AD, Lammerding J, Gabriele S. Mechanics and functional consequences of nuclear deformations. Nat Rev Mol Cell Biol 2022. [PMID: 35513718 DOI: 10.1038/s41580-022-00480-z] [Cited by in Crossref: 7] [Cited by in F6Publishing: 7] [Article Influence: 7.0] [Reference Citation Analysis]
32 Tati S, Alisaraie L. Recruitment of dynein and kinesin to viral particles. The FASEB Journal 2022;36. [DOI: 10.1096/fj.202101900rr] [Reference Citation Analysis]
33 Dultz E, Wojtynek M, Medalia O, Onischenko E. The Nuclear Pore Complex: Birth, Life, and Death of a Cellular Behemoth. Cells 2022;11:1456. [DOI: 10.3390/cells11091456] [Cited by in Crossref: 3] [Cited by in F6Publishing: 3] [Article Influence: 3.0] [Reference Citation Analysis]
34 King GA, Wettstein R, Varberg JM, Chetlapalli K, Walsh ME, Gillet L, Hernández-armenta C, Beltrao P, Aebersold R, Jaspersen SL, Matos J, Ünal E. Meiotic Nuclear Pore Complex Remodeling Provides Key Insights into Nuclear Basket Organization.. [DOI: 10.1101/2022.04.14.488376] [Reference Citation Analysis]
35 Varberg JM, Unruh JR, Bestul AJ, Khan AA, Jaspersen SL. Quantitative analysis of nuclear pore complex organization in Schizosaccharomyces pombe. Life Sci Alliance 2022;5:e202201423. [PMID: 35354597 DOI: 10.26508/lsa.202201423] [Cited by in Crossref: 3] [Cited by in F6Publishing: 3] [Article Influence: 3.0] [Reference Citation Analysis]
36 Huang G, Zhan X, Zeng C, Liang K, Zhu X, Zhao Y, Wang P, Wang Q, Zhou Q, Tao Q, Liu M, Lei J, Yan C, Shi Y. Cryo-EM structure of the inner ring from the Xenopus laevis nuclear pore complex. Cell Res 2022. [PMID: 35301439 DOI: 10.1038/s41422-022-00633-x] [Cited by in Crossref: 4] [Cited by in F6Publishing: 3] [Article Influence: 4.0] [Reference Citation Analysis]
37 Bryant P, Pozzati G, Zhu W, Shenoy A, Kundrotas P, Elofsson A. Predicting the structure of large protein complexes using AlphaFold and Monte Carlo tree search.. [DOI: 10.1101/2022.03.12.484089] [Cited by in Crossref: 6] [Cited by in F6Publishing: 6] [Article Influence: 6.0] [Reference Citation Analysis]
38 Kralt A, Wojtynek M, Fischer JS, Agote-aran A, Mancini R, Dultz E, Noor E, Uliana F, Tatarek-nossol M, Antonin W, Onischenko E, Medalia O, Weis K. An amphipathic helix in Brl1 is required for membrane fusion during nuclear pore complex biogenesis in S. cerevisiae.. [DOI: 10.1101/2022.03.04.483005] [Cited by in Crossref: 1] [Cited by in F6Publishing: 1] [Article Influence: 1.0] [Reference Citation Analysis]
39 Hampoelz B, Baumbach J. Nuclear envelope assembly and dynamics during development. Semin Cell Dev Biol 2022:S1084-9521(22)00067-2. [PMID: 35249812 DOI: 10.1016/j.semcdb.2022.02.028] [Cited by in Crossref: 1] [Cited by in F6Publishing: 2] [Article Influence: 1.0] [Reference Citation Analysis]
40 Matsuda A, Mofrad MRK. On the nuclear pore complex and its emerging role in cellular mechanotransduction. APL Bioengineering 2022;6:011504. [DOI: 10.1063/5.0080480] [Cited by in Crossref: 2] [Cited by in F6Publishing: 2] [Article Influence: 2.0] [Reference Citation Analysis]
41 Madheshiya PK, Shukla E, Singh J, Bawaria S, Ansari MY, Chauhan R. Insights into the role of Nup62 and Nup93 in assembling cytoplasmic ring and central transport channel of the nuclear pore complex.. [DOI: 10.1101/2022.02.28.482420] [Reference Citation Analysis]
42 Vahabikashi A, Adam SA, Medalia O, Goldman RD. Nuclear lamins: Structure and function in mechanobiology. APL Bioengineering 2022;6:011503. [DOI: 10.1063/5.0082656] [Cited by in Crossref: 6] [Cited by in F6Publishing: 7] [Article Influence: 6.0] [Reference Citation Analysis]
43 Stewart M. Function of the Nuclear Transport Machinery in Maintaining the Distinctive Compositions of the Nucleus and Cytoplasm. Int J Mol Sci 2022;23:2578. [PMID: 35269721 DOI: 10.3390/ijms23052578] [Cited by in Crossref: 4] [Cited by in F6Publishing: 3] [Article Influence: 4.0] [Reference Citation Analysis]
44 Petrauskas A, Fortunati DL, Singh A, Kandi AR, Pothapragada SS, Agrawal K, Huelsmeier J, Hillebrand J, Brown G, Chaturvedi D, Lee J, Lim C, Auburger G, Vijayraghavan K, Ramaswami M, Bakthavachalu B. Structured and disordered regions of Ataxin-2 contribute differently to the specificity and efficiency of mRNP granule formation.. [DOI: 10.1101/2022.02.15.480566] [Reference Citation Analysis]
45 Huang G, Zhan X, Zeng C, Zhu X, Liang K, Zhao Y, Wang P, Wang Q, Zhou Q, Tao Q, Liu M, Lei J, Yan C, Shi Y. Cryo-EM structure of the nuclear ring from Xenopus laevis nuclear pore complex. Cell Res 2022. [PMID: 35177819 DOI: 10.1038/s41422-021-00610-w] [Cited by in Crossref: 5] [Cited by in F6Publishing: 4] [Article Influence: 5.0] [Reference Citation Analysis]
46 Maysinger D, Sanader Maršić Ž, Gran ER, Shobo A, Macairan JR, Zhang I, Perić Bakulić M, Antoine R, Multhaup G, Bonačić-Kouteckỳ V. Insights into the Impact of Gold Nanoclusters Au10SG10 on Human Microglia. ACS Chem Neurosci 2022;13:464-76. [PMID: 35080850 DOI: 10.1021/acschemneuro.1c00621] [Cited by in Crossref: 2] [Cited by in F6Publishing: 2] [Article Influence: 2.0] [Reference Citation Analysis]
47 Dharan A, Campbell EM. Teaching old dogmas new tricks: recent insights into the nuclear import of HIV-1. Curr Opin Virol 2022;53:101203. [PMID: 35121335 DOI: 10.1016/j.coviro.2022.101203] [Cited by in Crossref: 3] [Cited by in F6Publishing: 3] [Article Influence: 3.0] [Reference Citation Analysis]
48 Chandra S, Lusk CP. Emerging Connections between Nuclear Pore Complex Homeostasis and ALS. IJMS 2022;23:1329. [DOI: 10.3390/ijms23031329] [Cited by in Crossref: 4] [Cited by in F6Publishing: 4] [Article Influence: 4.0] [Reference Citation Analysis]
49 Akey CW, Singh D, Ouch C, Echeverria I, Nudelman I, Varberg JM, Yu Z, Fang F, Shi Y, Wang J, Salzberg D, Song K, Xu C, Gumbart JC, Suslov S, Unruh J, Jaspersen SL, Chait BT, Sali A, Fernandez-Martinez J, Ludtke SJ, Villa E, Rout MP. Comprehensive structure and functional adaptations of the yeast nuclear pore complex. Cell 2022;185:361-378.e25. [PMID: 34982960 DOI: 10.1016/j.cell.2021.12.015] [Cited by in Crossref: 26] [Cited by in F6Publishing: 29] [Article Influence: 26.0] [Reference Citation Analysis]
50 Aksenova V, Dasso M. Mapping paths through the nuclear pore complex. Nat Cell Biol 2022;24:6-7. [PMID: 35013557 DOI: 10.1038/s41556-021-00823-6] [Reference Citation Analysis]
51 Mccarthy MR, Lusk CP. One ring doesn’t rule them all: Distinct nuclear pore complexes in a single cell. Cell 2022;185:230-231. [DOI: 10.1016/j.cell.2021.12.042] [Reference Citation Analysis]
52 Judernatz JH, Roelofs MC, Zeev-ben-mordehai T. Cellular Cryo-Electron Tomography. Reference Module in Life Sciences 2022. [DOI: 10.1016/b978-0-12-821618-7.00112-7] [Reference Citation Analysis]
53 Andronov L, Genthial R, Hentsch D, Klaholz BP. A spectral demixing method for high-precision multi-color localization microscopy.. [DOI: 10.1101/2021.12.23.473862] [Cited by in Crossref: 1] [Cited by in F6Publishing: 1] [Article Influence: 1.0] [Reference Citation Analysis]
54 Hamed M, Antonin W. Dunking into the Lipid Bilayer: How Direct Membrane Binding of Nucleoporins Can Contribute to Nuclear Pore Complex Structure and Assembly. Cells 2021;10:3601. [PMID: 34944108 DOI: 10.3390/cells10123601] [Cited by in Crossref: 6] [Cited by in F6Publishing: 6] [Article Influence: 6.0] [Reference Citation Analysis]
55 Winogradoff D, Chou H, Maffeo C, Aksimentiev A. Percolation transition determines protein size limit for passive transport through the nuclear pore complex.. [DOI: 10.1101/2021.12.17.473237] [Reference Citation Analysis]
56 Lusk CP, King MC. Nuclear pore complexes feel the strain. Mol Cell 2021;81:4962-3. [PMID: 34919818 DOI: 10.1016/j.molcel.2021.11.029] [Cited by in Crossref: 1] [Cited by in F6Publishing: 1] [Article Influence: 1.0] [Reference Citation Analysis]
57 Zimmerli CE, Allegretti M, Rantos V, Goetz SK, Obarska-Kosinska A, Zagoriy I, Halavatyi A, Hummer G, Mahamid J, Kosinski J, Beck M. Nuclear pores dilate and constrict in cellulo. Science 2021;374:eabd9776. [PMID: 34762489 DOI: 10.1126/science.abd9776] [Cited by in Crossref: 57] [Cited by in F6Publishing: 59] [Article Influence: 57.0] [Reference Citation Analysis]
58 Huang G, Zhan X, Zeng C, Liang K, Zhu X, Zhao Y, Wang P, Wang Q, Zhou Q, Tao Q, Liu M, Lei J, Yan C, Shi Y. Cryo-EM structure of the Inner Ring from Xenopus laevis Nuclear Pore Complex.. [DOI: 10.1101/2021.11.13.468242] [Cited by in Crossref: 4] [Cited by in F6Publishing: 4] [Article Influence: 4.0] [Reference Citation Analysis]
59 Petrovic S, Samanta D, Perriches T, Bley CJ, Thierbach K, Brown B, Nie S, Mobbs GW, Stevens TA, Liu X, Hoelz A. Architecture of the linker-scaffold in the nuclear pore.. [DOI: 10.1101/2021.10.26.465796] [Cited by in Crossref: 8] [Cited by in F6Publishing: 8] [Article Influence: 8.0] [Reference Citation Analysis]