Display Settings:

Items per page
We are sorry, but NCBI web applications do not support your browser and may not function properly. More information

Results: 9

1.
Figure 5

Figure 5. From: The hrp23 Protein in the Balbiani Ring Pre-mRNP Particles Is Released Just before or at the Binding of the Particles to the Nuclear Pore Complex .

Primary structure comparison of hrp23 with Drosophila Rox21 protein. The two complete amino acid sequences are aligned and presented by the PILEUP and PRETTYPLOT programs. Regions with sequence similarity are boxed. Gaps in the alignment are shown by dashes.

Xin Sun, et al. J Cell Biol. 1998 September 7;142(5):1181-1193.
2.
Figure 2

Figure 2. From: The hrp23 Protein in the Balbiani Ring Pre-mRNP Particles Is Released Just before or at the Binding of the Particles to the Nuclear Pore Complex .

Immunolocalization of hrp23 on isolated C. tentans polytene chromosomes. The chromosomes were isolated from prefixed salivary glands and incubated with monoclonal antibody 1D3 (a and c) or with an anti–factor VIII antibody as negative control (b and d). The antibody-binding sites were visualized by a gold-conjugated secondary antibody and silver enhancement. Examples of chromosome IVs (a and b) and chromosomes IIIs (c and d) are shown. The positions of BR1, BR2, and nucleolus (Nu) have been indicated. Bar, 10 μm.

Xin Sun, et al. J Cell Biol. 1998 September 7;142(5):1181-1193.
3.
Figure 3

Figure 3. From: The hrp23 Protein in the Balbiani Ring Pre-mRNP Particles Is Released Just before or at the Binding of the Particles to the Nuclear Pore Complex .

Western blot comparison of hrp23 from C. tentans tissue culture cells with hrp23 expressed in E. coli. The extracted proteins were separated by SDS-PAGE, blotted onto transfer membranes, and probed with mAb 1D3. Lane 1, RNP extract from tissue culture cells. Lane 2, alkaline phosphatase–treated RNP extract from tissue culture cells. Lane 3, extract from E. coli, containing the hrp23 cDNA clone, before IPTG induction. Lane 4, extract from E. coli, containing the hrp23 cDNA clone, after IPTG induction. The positions of two molecular mass standards are indicated to the left.

Xin Sun, et al. J Cell Biol. 1998 September 7;142(5):1181-1193.
4.
Figure 6

Figure 6. From: The hrp23 Protein in the Balbiani Ring Pre-mRNP Particles Is Released Just before or at the Binding of the Particles to the Nuclear Pore Complex .

Immunocytological localization of hrp23 in C. tentans salivary gland cells. Semithin cryosections of salivary glands were treated with mAb 1D3 (or with a negative control antibody), a gold-conjugated secondary antibody was added, and the antibody binding was visualized by silver enhancement. The 1D3-treated specimens are shown in bright field (a and b), and the negative controls are shown in bright field (c) and phase contrast (c′). The nuclei (NUC), cytoplasm (CYT), and gland lumen (LUM) are indicated. Bars, 40 μm.

Xin Sun, et al. J Cell Biol. 1998 September 7;142(5):1181-1193.
5.
Figure 4

Figure 4. From: The hrp23 Protein in the Balbiani Ring Pre-mRNP Particles Is Released Just before or at the Binding of the Particles to the Nuclear Pore Complex .

Nucleotide sequence and deduced amino acid sequence of the hrp23 cDNA clone pHRP23.2. This HRP clone was the longest one recorded and sequenced. The RBD is boxed. Within RBD, the two most highly conserved sequence elements, RNP-1 (solid line) and RNP-2 (dashed line) are underlined. The end of the coding region is indicated by an asterisk. These sequence data are available from the EMBL DNA data base under accession number AJ003820.

Xin Sun, et al. J Cell Biol. 1998 September 7;142(5):1181-1193.
6.
Figure 9

Figure 9. From: The hrp23 Protein in the Balbiani Ring Pre-mRNP Particles Is Released Just before or at the Binding of the Particles to the Nuclear Pore Complex .

Transcription-independent nuclear localization of hrp23. C. tentans tissue culture cells were treated for 1 h with (act D) or without (normal) actinomycin D in the presence of cycloheximide. To locate hrp23, semithin cryosections were incubated with mAb 1D3 and subsequently with a gold-conjugated secondary antibody. The labeling was visualized by silver enhancement and photographed in bright field. The distribution of the shuttling protein hrp36 was analyzed in parallel with mAb 4F9. Some of the immunopositive nuclei have been indicated by arrows. Bar, 25 μm.

Xin Sun, et al. J Cell Biol. 1998 September 7;142(5):1181-1193.
7.
Figure 1

Figure 1. From: The hrp23 Protein in the Balbiani Ring Pre-mRNP Particles Is Released Just before or at the Binding of the Particles to the Nuclear Pore Complex .

Generation and characterization of monoclonal antibody 1D3. (a) SDS-PAGE of the proteins in the RNP extract from C. tentans tissue culture cells (lane 1), and of the proteins immunoprecipitated from the RNP extract by mAb 4F9 and used for subsequent immunization of BALB/c mice (lane 2). The protein recognized by mAb 4F9, hrp36, is indicated with an asterisk at lane 2. The position of molecular mass standards is shown to the left in kilodaltons. (b) Western blot analysis of the RNP extract probed with serum from an immunized mouse (lane 1), mAb 1D3 (lane 2), and negative control antibody (lane 3). The molecular mass standards are the same as in a.

Xin Sun, et al. J Cell Biol. 1998 September 7;142(5):1181-1193.
8.
Figure 8

Figure 8. From: The hrp23 Protein in the Balbiani Ring Pre-mRNP Particles Is Released Just before or at the Binding of the Particles to the Nuclear Pore Complex .

Immunoelectron microscopic localization of hrp23 in the nucleolus of C. tentans salivary glands. Semithin sections through a nucleolus in a salivary gland cell were treated with mAb 1D3, and the binding was visualized by a gold-conjugated secondary antibody. In parallel, sections were incubated with a negative control antibody. (a) A segment of a nucleolus, with its fibrillar (F) and granular (G) compartments, and the surrounding nucleoplasm (NP). (b) The area demarcated with a rectangle in a, at higher magnification. The arrows denote the position of gold particles. (c) The negative control. Bars: (a) 250 nm; (b and c) 100 nm.

Xin Sun, et al. J Cell Biol. 1998 September 7;142(5):1181-1193.
9.
Figure 7

Figure 7. From: The hrp23 Protein in the Balbiani Ring Pre-mRNP Particles Is Released Just before or at the Binding of the Particles to the Nuclear Pore Complex .

Immunoelectron microscopic localization of hrp23 in C. tentans salivary gland cells. Thin cryosections were incubated with mAb 1D3 (a–e), or with a negative control antibody (f), and a gold-conjugated secondary antibody was used to visualize the labeled sites. (a) Proximal (p), middle (m), and distal (d) segments of transcriptionally active BR genes. (b–d) Nucleoplasmic BR particles close to the nuclear envelope (arrows) and extended BR particles translocating through the nuclear pores. Schematic interpretations of the electron micrographs are shown beneath (b′–d′). The nucleus (N) is located above the nuclear envelope, and cytoplasm (C) is located beneath. The non–BR hnRNP complexes appear in the nucleoplasm as an irregular fibrous network labeled with a few gold particles (c). (e) Cytoplasm containing tubular ER with associated ribosomes. The arrows point at gold particles. (f) The negative control showing nuclear envelope with adjacent nuclear (N) and cytoplasmic (C) regions. In the nucleus, growing BR RNP particles can be discerned (cf., a). Bar, 100 nm.

Xin Sun, et al. J Cell Biol. 1998 September 7;142(5):1181-1193.

Display Settings:

Items per page

Supplemental Content

Recent activity

Your browsing activity is empty.

Activity recording is turned off.

Turn recording back on

See more...
Write to the Help Desk