-
2
-
-
0020472010
-
A Large Particle Associated with the Perimeter of the Nuclear Pore Complex
-
(1982)
J Cell Biol
, vol.93
, pp. 63-75
-
-
Unwin1
Milligan2
-
3
-
-
0024417594
-
Interactions and Structure of the Nuclear Pore Complex Revealed by Cryo-Electron Microscopy
-
(1989)
J Cell Biol
, vol.109
, pp. 955-970
-
-
Akey1
-
4
-
-
0026323478
-
Towards a More Complete 3-D Structure of the Nuclear Pore Complex
-
(1991)
J Struct Biol
, vol.107
, pp. 291-308
-
-
Jarnik1
Aebi2
-
5
-
-
0026776959
-
Architecture and Design of the Nuclear Pore Complex
-
of outstanding interest, A 3D reconstruction of negatively stained NPCs released from the nuclear envelope by detergent treatment has been computed by the random conical tilt method. The map shows the following: first, a highly symmetric (822 symmetry) NPC framework built from eight multi-domain spokes; and second the existence of eight peripheral channels that are proposed to be sites for passive diffusion.
-
(1992)
Cell
, vol.69
, pp. 1133-1141
-
-
Hinshaw1
Carragher2
Milligan3
-
6
-
-
0027287349
-
Architecture of the Xenopusnuclear Pore Complex Revealed by Three-Dimensional Cryo-Electron Microscopy
-
••], but it includes the central channel complex, and the diffusional channels are located more centrally.
-
(1993)
J Cell Biol
, vol.122
, pp. 1-19
-
-
Akey1
Radermacher2
-
7
-
-
0026042170
-
Cytosolic Proteins that Specifically Bind Nuclear Localization Signals are Receptors for Nuclear Innport
-
(1991)
Cell
, vol.66
, pp. 837-847
-
-
Adam1
Gerace2
-
8
-
-
0026723508
-
The Two Steps of Nuclear Import, Targeting to the Nuclear Envelope and Translocadon Through the Nuclear Pore, Require Different Cytosolic Factors
-
(1992)
Cell
, vol.68
, pp. 939-950
-
-
Moon1
Blobel2
-
9
-
-
0027376308
-
The GTP Binding Protein Ran/TC4 is Required for Protein Import into the Nucleus
-
of outstanding interest, A component required for the activity of a cytosolic fraction which is involved In the ATP-dependent nuclear protein translocation step was isolated. Biochemical characterization of this component has identified it as the GTP-binding protein Ran/TC4. Import assays with non-hydrolyzable GTP analogues revealed that GTP hydrolysis is required for protein import.
-
(1993)
Nature
, vol.365
, pp. 661-663
-
-
Moon1
Blobel2
-
10
-
-
84914757448
-
Inhibition of Nuclear Protein Import by Nonhydrolyrlple Analogues of GTP and Identification of the Small GTPase Ran/rC4 as an Essential Transport Factor
-
of outstanding interest, in press, GTP-g-S and other non-hydrolyzable GTP analogues were found to inhibit nuclear protein Import in digitonin permeabiliaed cells. The cytosolic factor responsible for this inhibition was found to be the small GTPase Ran/TC4.
-
(1994)
J Cell Biol
-
-
Melchor1
Paschal2
Evans3
Gerace4
-
11
-
-
0025119137
-
Monomethylated Cap Structures Facilitate RNA Export from the Nucleus
-
(1990)
Cell
, vol.63
, pp. 109-118
-
-
Hamm1
Mattaj2
-
12
-
-
84901973748
-
Nuclear Export of Different Classes of RNA is Mediated by Specific Factors
-
of outstanding interest, The factors involved in nuclear export of different classes of RNAs were Investigated by coinjection and competition studies in Xenopus oocyte nuclei. Distinct specific factors were essential for export of the various RNAs from the nucleus. This study supported the idea that a monomethylated rap structure is required for export of UsnRNAs. Using synthetic homopolymenc RNAs as competitors, common steps in the export process are suggested.
-
(1993)
The Journal of Cell Biology
, vol.123
, pp. 1649-1659
-
-
Jarmolowski1
Boelens2
Izaurralde3
Mattaj4
-
17
-
-
0027619054
-
The Nuclear Pore Complex and Nucleocy toplasmic Transport
-
of special interest, A comprehensive review on the nuclear pore complex and nucleocytoplasmic transport. Recent findings on the NPC protein NUP153, identification of cytosolic factors, and the role of the 70 kDa heat shock protein (hsc70/hsp70) in nuclear import are discussed in detail.
-
(1993)
Curr Opin Cell Biol
, vol.5
, pp. 395-407
-
-
Newmeyer1
-
18
-
-
0027199147
-
The Nuclear Pore Complex
-
of outstanding interest, A comprehensive, authoritative review on nuclear pore complex structure, molecular composition and function with emphasis on questions and ambiguities centered around these areas. Emerging structural and functional models are critically evaluated.
-
(1993)
The Journal of Cell Biology
, vol.122
, pp. 977-984
-
-
Panté1
Aebi2
-
19
-
-
0025180782
-
Visualization of Transport-Related Configurations of the Nuclear Pore Transporter
-
(1990)
Biophys J
, vol.58
, pp. 341-355
-
-
Akey1
-
20
-
-
0027500249
-
The Amino-Terminal Domain of the Lamin B Receptor is a Nuclear Envelope Targeting Signal
-
of special interest, Fusion proteins containing different domains of the lamin B receptor were localized by immunofluorescence microscopy. Proteins carrying the amino terminal domain were targeted to the inner nuclear membrane, whereas proteins currying only the transmembrane domain remained in the ER.
-
(1993)
The Journal of Cell Biology
, vol.120
, pp. 1093-1100
-
-
Soullan1
Worman2
-
21
-
-
0027613912
-
Nuclear Membrane Dynamics
-
of special interest, An Informative review on the latest findings of nuclear envelope assembly with particular emphasis on vesicle binding to chromatin, vesicle fusion, and protein targeting to the inner nuclear membrane.
-
(1993)
Curr Opin Cell Biol
, vol.5
, pp. 387-394
-
-
Wiese1
Wilson2
-
22
-
-
0002272634
-
The 3-D Structure of the Nuclear Pore Complex as Seen by High Voltage Electron Microscopy and High Resolution Low Voltage Scanning Electron Microscopy
-
(1991)
EMSA Bull
, vol.21
, pp. 54-56
-
-
Ris1
-
23
-
-
0027104231
-
High Resolution Scanning Electron Microscopy of the Nuclear Envelope: Demonstration of a new, Regular, Fibrous Lattice Attached to the Baskets of the Nucleoplasmic Face of the Nuclear Pores
-
of special interest, The cytoplasmic filaments and nuclear baskets are visualized by high-resolution scanning EM of nuclear envelopes from Triturus cristatus oocytes. This study describes a new fibrous lattice (‘NE lattice’ or NEL) that is different from the nuclear lamina, and is attached to the NPCs via their nuclear baskets.
-
(1992)
J Cell Biol
, vol.119
, pp. 1429-1440
-
-
Goldberg1
Allen2
-
24
-
-
0027366167
-
Isolation of the Yeast Nuclear Pore Complex
-
of outstanding interest, A procedure to isolate milligram quantities of NPCs from yeast was developed. The isolated NPCs, visualized by negative staining, while revealing the same overal morphology are smaller (∼97 rain in diameter) than vertebrate NPCs. The molecular mass of yeast NPCs determined by analytical ultracentrifugation (∼66 MDa) was also smaller than the mass of vertebrate NPCs.
-
(1993)
J Cell Biol
, vol.123
, pp. 771-783
-
-
Rout1
Blobel2
-
25
-
-
0027525230
-
The Nuclear Pore Complex: Three-Dimensional Surface Structure Revealed by Field Emission, In-Lens Scanning Electron Microscopy, with Underlaying Structure Uncovered by Proteolysis
-
•]). Tryptic digestion of the NPCs removed first their cytoplasmic filaments and nuclear basket, then their cytoplasmic and nuclear rings. Digestion of the rings involved sequential removal of subunits, rather than their fragmentation. In these digestions, the nuclear rings were more sensitive to proteolysis than the cytoplasmic rings.
-
(1993)
J Cell Sci
, vol.106
, pp. 261-274
-
-
Goldberg1
Allen2
-
26
-
-
0025144559
-
Selective Digestion of Nuclear Envelopes from Xenopus Oocyte Germinal Vesicles: Possible Structural Role for the Nuclear Lamine
-
(1990)
J Cell Sci
, vol.97
, pp. 571-580
-
-
Whytock1
Moir2
Stewart3
-
27
-
-
84901970853
-
Exploring Native Nuclear Pore Complex Structure and Conformation by Scanning Force Microscopy in Physiological Buffers
-
of special interest, in press, The cytoplasmic and nuclear surface topographies of membrane-bound NPCs kept in their physiological buffers have been imaged with the scanning force microscope and compared with corresponding EM images of dehydrated metal-coated NPCs. The scanning force microscope images confirm the highly asymmetric appearance of the cytoplasmec and nuclear faces of the NPC.
-
(1994)
J High Vacc Tech
-
-
Goldie1
Panté2
Engel3
Aebi4
-
28
-
-
1842357147
-
The Structure and Interactions of Components of Nuclear Envelopes from Xenopus Oocyte Germinal Vesicles Observed by Heavy Metal Shadowing
-
(1988)
J Cell Sci
, vol.90
, pp. 409-423
-
-
Stewart1
Whytock2
-
30
-
-
0027491276
-
Localization of Vault Particles to the Nuclear Pore Complex
-
of special interest, A polyclonal rabbit antiserum raised against vaults, cytoplasmic ribonucleoprotein particles, bound to isolated nuclei as shown by by immunobloting, immunofluorescence and immuno-EM. This anti-serum also labeled the nuclear envelope and the NPCs in tissue sections or sections of isolated NEs. From these results it is concluded that vaults are associated with NPCs. On the basis of the similarity in the dimensions and geometry of the vault and those of the central plug from the 3D reconstruction of Akey and Radermacher [6], the authors suggest that vaults may form the central plug of the NPC.
-
(1993)
J Cell Sci
, vol.106
, pp. 23-29
-
-
Chugani1
Rome2
Kedersha3
-
31
-
-
0023257987
-
Monoclonal Antibodies Identify a Group of Nuclear Pore Complex Glycoproteins
-
(1987)
J Cell Biol
, vol.104
, pp. 1143-1156
-
-
Snow1
Senior2
Gerace3
-
33
-
-
0023449881
-
The Nuclear Pore Complex Contains a Family of Glycoproteins that Includes p62: Glycosylation Through a Previously Unidentified Cellular Pathway
-
(1987)
Proc Natl Acad Sci USA
, vol.84
, pp. 7552-7556
-
-
Davis1
Blobel2
-
34
-
-
0027395040
-
Nup155 is a Novel Nuclear Pore Complex Protein that Contains Neither Repetitive Sequence Motifs nor Reacts with WGA
-
of special interest, A procedure was developed to isolate ∼30 proteins from rat liver nuclear envelopes that do not bind the lectin WGA. The gene encoding one of these polypeptides, termed NUP155, was cloned, sequenced, and immunolocalized to the NPC. The amino acid sequence of NUP155 did not reveal any repetitive sequence motif.
-
(1993)
J Cell Biol
, vol.121
, pp. 1-9
-
-
Radu1
Blobel2
Wozniak3
-
35
-
-
0027458374
-
A Nuclear Pore Complex Protein that Contains Zinc Finger Motifs, Binds DNA, and Faces the Nucleopiasm
-
of outstanding interest, A rat liver nuclear pore complex protein of 153 kDa was cloned and sequenced. It contains a repetitive pentapeptide motif (XFXFG) common to p62 and yeast NSP1 and NUP1, and four zinc finger motifs. It was localized exclusively to the nucleoplasmic side of the NE by immuno-EM.
-
(1993)
Cell
, vol.72
, pp. 29-38
-
-
Sukegawa1
Blobel2
-
37
-
-
0027744056
-
Nup180, a Novel Nuclear Pore Complex Protein Localizing to the Cytoplasmic Ring and Associated Fibrils
-
of outstanding interest, A nuclear pore complex protein of 180kDa, termed NUP180, was identified using an autoimmune serum from a patient with an overlap connective tissue disease. NUP180 did not bind WGA and was located to the cytoplasmic ring and cytoplasmic filaments. Anti-NUP180 antibodies did not inhibit nuclear protein import.
-
(1993)
J Cell Biol
, vol.123
, pp. 1345-1354
-
-
Wilken1
Kossner2
Senécal3
Scheer4
Dabauvalle5
-
38
-
-
0026554284
-
Nucleotidc Sequence Analysis of Human tpr cDNA clones
-
(1992)
Oncogene
, vol.7
, pp. 383-388
-
-
Mitchell1
Cooper2
-
39
-
-
84901970855
-
Role of Different Domains in the Self-Association of Rat Nucleoporin p62
-
of special interest, in press, Rat p62 was expressed in E. coil. The molecular structure of recombinant p62, deduced by EM and circular dichroism, was similar to that predicted by primary sequence analysis: a rod-shaped molecule with an α-helical coiled-coil conformation domain at the carboxy-terminal domain and a cross-β structure at the amino-terminal domain. Further characterization of a series of proteolytic fragments of p62 revealed a small region near the carboxy-terminal end important for its association into higher-order structures.
-
(1993)
J Cell Sci
-
-
Buss1
Kent2
Stewart3
Bailer4
Hanover5
-
41
-
-
0025886328
-
Human Nuclcoporin p62 and the Essential Yeast Nuclear Pore Protein NSP1 Show Sequence Homology and a Similar Domain Organization
-
(1991)
Eur J Cell Biol
, vol.55
, pp. 17-30
-
-
Carmo-Fonseca1
Kern2
Hurt3
-
42
-
-
0025771404
-
Nuclear Pore Complex Glycoprotein p62 of Xenopus laevis and Mouse: cDNA Cloning and Identification of its Glycosylation Region
-
(1991)
Eur J Cell Biol
, vol.55
, pp. 31-47
-
-
Cordes1
Waizenegger2
Krohne3
-
43
-
-
0027236761
-
An Integral Membrane Protein of the Pore Membrane Domain of the Nuclear Envelope Contains a Nucleoporin-Like Region
-
of special interest, The gene encoding a new integral membrane protein, MOP121, was cloned and sequenced. Very much like the O-linked NPC glycoproteins, MOP121 contains N-acetylglucosamine residues and harbours the repetitive peptapeptide motif common to p62 and NUP153. MOP121 has a transmembrane domain localized in the pore membrane domain around the NPCs.
-
(1993)
The Journal of Cell Biology
, vol.122
, pp. 513-521
-
-
Halliierg1
Wozniak2
Blobel3
-
45
-
-
0026567673
-
O-Linked Glycoproteins of the Nuclear Pore Complex Interact with a Cytosolic Factor Required for Nuclear Protein Import
-
(1992)
J Cell Biol
, vol.116
, pp. 271-280
-
-
Sterne-Marr1
Blevitt2
Gerace3
-
46
-
-
0025274481
-
An N-Ethylmaleimide-Sensitive Cytosolic Factor Necessary for Nuclear Protein Import: Requirement in Signal-Mediated Binding to the Nuclear Pore
-
(1990)
J Cell Biol
, vol.110
, pp. 547-557
-
-
Newmeyer1
Forbes2
-
48
-
-
0027751329
-
Intranuclear Filaments Containing a Nuclear Pore Complex Protein
-
of special interest, NUP153 was localized to intranuclear filaments attached to the NPC by immuno-EN. Using immunofluorescence microscopy these authors have shown that NUP153 is disperse over the cytoplasm when the NE disassembles, and speculate that — as is the case with lamins — the disassembly and reassembly during mitosis (and meiosis) of the NUP153-containing filament is affected by protein modification.
-
(1993)
J Cell Biol
, vol.123
, pp. 1333-1344
-
-
Cordes1
Reidenbach2
Köhler3
Stuurman4
van Driel5
Franke6
-
49
-
-
0027771070
-
High-Resolution Field Emission Scanning Electron Microscope Imaging of Internal Cell Structures after Epon Extraction from Sections: A New Approach to Coorelative Ultrastructural and Immunocytochemical Studies
-
of special interest, Xenopus oocyte nuclear envelopes and insect striated muscle are examined by high-resolution, low voltage scanning EM after using a new less-destructive method for removing the Epon resin from section. This method allows to image the sample from any desired angle, and in the case of the NPC new ‘cable-like’ structures attached to the terminal ring of the nuclear baskets were observed.
-
(1993)
J Struct Biol
, vol.111
, pp. 148-157
-
-
Ris1
Maecki2
-
50
-
-
0027979480
-
The Human CAN Protein, a Putative Oncogenc Product Associated with Myeloid Leukemogenesis, is a Nuclear Pore Complex Protein that Faces the Cytoplasm
-
of special interest, The previously described 1311 210 kDa O4inked NPC glycoprotein was found to be the homolog of the human CAN protein [51]. Partial amino acid sequence of this O-linked NPC glycoprotein revealed a high degree of similarity with CAN, and an antibody directed against a segment of CAN labeled with the cytoplasmic side of the NPC by immuno-EM.
-
(1994)
Proc Natl Acad Sci USA
, vol.91
, pp. 1519-1523
-
-
Kraemer1
Wozniak2
Blobel3
Radu4
-
54
-
-
0025253486
-
A Major Glycoprotein of the Nuclear Pore Complex is a Membrane-Spanning Polypeptide with a Large Lumenal Domain and a Small Cytoplasmic Tail
-
(1990)
EMBO J
, vol.9
, pp. 1495-1502
-
-
Greber1
Senior2
Gerace3
-
55
-
-
0027043255
-
The Single Tmnsmembrane Seg- ment of gp210 is Sufficient for Sorting to the Pore Membrane Domain of the Nuclear Envelope
-
of special interest, Various cDNAs coding for different segments of gp210 were expressed in mouse Balb/c 3T3 cells and the recombinant proteins localized by immunofluorescence microscopy. It was found that the transmembrane domain of gp210 is sufficient for sorting of the protein to the pore membrane. The short cytoplasmic tail of gp210 contains an additional, but weaker, sorting determinant.
-
(1992)
J Cell Blol
, vol.119
, pp. 1441-1449
-
-
Wozniak1
Blobel2
-
57
-
-
0024293481
-
A Novel Nucleoskeletal-Like Protein Located at the Nuclear Periphery is Required for jhe Life Cycle of Saccbaromyces cerevisiae
-
(1988)
EMBO J
, vol.7
, pp. 4323-4334
-
-
Hurt1
-
58
-
-
0025367662
-
The NUP1 Gene Encodes an Essential Component of the Yeast Nuclear Pore Complex
-
(1990)
Cell
, vol.61
, pp. 965-978
-
-
Davis1
Fink2
-
59
-
-
0027405398
-
NUP2, a Novel Yeast Nucleoporin, has Functional Overlap with Other Proteins of the Nuclear Pore Complex
-
of special interest, A new NPC protein, NUP2, was cloned and sequenced in yeast. NUP2 contains several copies of the pentapeptide motif XFXFG similar to the yeast prottins NSP1 and NUP1. At difference with these two yeast proteins, NUP2 is not essential for growth.
-
(1993)
Mol Biol Cell
, vol.4
, pp. 209-222
-
-
Loeb1
Davis2
Fink3
-
60
-
-
0026463881
-
A New Family of Yeast Nuclear Pore Complex Proteins
-
of special interest, Three new NPC proteins, NUP116, NUP100 and NUP49 were cloned and sequenced in yeast and shown to represent a new class of nucleoporins that share an amino-terminal domain with a repetitive tetrapeptide motif (GLFG).
-
(1992)
J Cell Biol
, vol.119
, pp. 705-723
-
-
Wente1
Rout2
Blobei3
-
62
-
-
0027428431
-
A Temperature-Sensitive NUP116 Null Mutant Forms a Nuclear Envelope Seal Over the Yeast Nuclear Pore Complex Thereby Blocking Nucleocytoplasmic Traffic
-
•] was characterized by EM. At 23°C, the mutation slowed down cell growth, and the inner nuclear membrane exhibited some invaginations. At 37°C, the mutation was lethal, and a membrane seal was formed over the cytoplasmic side of the NUP116 deficient NPCs. It was shown that such a membrane fusion across the cytoplasmic face does not block nuclear export, instead the mutatnt cells accumulated export substrate within these membrane herniations.
-
(1993)
J Cell Biol
, vol.123
, pp. 275-284
-
-
Wente1
Blobel2
|