"Polyproteins" - Books

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Results: 18 books (72 items)

Select item 16868401.

Retroviruses.

Coffin JM, Hughes SH, Varmus HE, editors.

Cold Spring Harbor (NY): Cold Spring Harbor Laboratory Press; 1997.

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Select item 14003622.

Hepatitis C Viruses: Genomes and Molecular Biology.

Tan SL, editor.

Norfolk (UK): Horizon Bioscience; 2006.

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Select item 14152803.

Madame Curie Bioscience Database [Internet].

Austin (TX): Landes Bioscience; 2000-2013.

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Select item 29002584.

Learning from SARS: Preparing for the Next Disease Outbreak: Workshop Summary.

Institute of Medicine (US) Forum on Microbial Threats; Knobler S, Mahmoud A, Lemon S, et al., editors.

Washington (DC): National Academies Press (US); 2004.

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Select item 19111645.

Genomes. 2nd edition.

Brown TA.

Oxford: Wiley-Liss; 2002.

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Select item 31642466.

Confronting AIDS: Directions for Public Health, Health Care, and Research.

Institute of Medicine (US) Committee on a National Strategy for AIDS.

Washington (DC): National Academies Press (US); 1986.

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Select item 16541067.

Immunobiology: The Immune System in Health and Disease. 5th edition.

Janeway CA Jr, Travers P, Walport M, et al.

New York: Garland Science; 2001.

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Select item 51971328.

Tumour Site Concordance and Mechanisms of Carcinogenesis.

Baan RA, Stewart BW, Straif K, editors.

Lyon (FR): International Agency for Research on Cancer; 2019. (IARC Scientific Publications, No. 165.)

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Select item 44036689.

StatPearls [Internet].

Treasure Island (FL): StatPearls Publishing; 2026 Jan-.

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Select item 437626410.

Human Immunodeficiency Viruses and Human T-Cell Lymphotropic Viruses.

IARC Working Group on the Evaluation of Carcinogenic Risks to Humans.

Lyon (FR): International Agency for Research on Cancer; 1996. (IARC Monographs on the Evaluation of Carcinogenic Risks to Humans, No. 67.)

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Select item 408515611.

Biological Agents.

IARC Working Group on the Evaluation of Carcinogenic Risks to Humans.

Lyon (FR): International Agency for Research on Cancer; 2012. (IARC Monographs on the Evaluation of Carcinogenic Risks to Humans, No. 100B.)

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Select item 306009612.

The NCBI Handbook [Internet]. 2nd edition.

Bethesda (MD): National Center for Biotechnology Information (US); 2013-.

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Select item 189578813.

Molecular Biology of the Cell. 4th edition.

Alberts B, Johnson A, Lewis J, et al.

New York: Garland Science; 2002.

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Select item 186695414.

C. elegans II. 2nd edition.

Riddle DL, Blumenthal T, Meyer BJ, et al., editors.

Cold Spring Harbor (NY): Cold Spring Harbor Laboratory Press; 1997.

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Select item 520324815.

SARS-CoV-2 Assays [Internet].

Bethesda (MD): National Center for Advancing Translational Sciences (NCATS); 2020-.

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Select item 315091216.

Opportunities in Biology.

National Research Council (US) Committee on Research Opportunities in Biology.

Washington (DC): National Academies Press (US); 1989.

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Select item 166869017.

Holland-Frei Cancer Medicine. 6th edition.

Kufe DW, Pollock RE, Weichselbaum RR, et al., editors.

Hamilton (ON): BC Decker; 2003.

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Select item 158168618.

Medical Microbiology. 4th edition.

Baron S, editor.

Galveston (TX): University of Texas Medical Branch at Galveston; 1996.

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Figure 2

Overview of retroviral assembly showing the universal features. The nucleus of the infected cell harbors an integrated provirus. Unspliced viral transcripts are used to synthesize Gag and Gag-Pro-Pol proteins in a cytosolic compartment. These polyproteins are subsequently transported to the cytoplasmic face of the plasma membrane where they mediate budding, and two copies of the viral genome are incorported into the particle. Spliced RNA transcripts are used to make Env proteins on the membrane of the RER. These proteins are transported to the external surface of the cell via the secretory pathway and then move laterally to the sites of budding for packaging. Very late or immediately after budding (dashed arrows), the Gag and Gag-Pro-Pol proteins within the immature virion are cleaved by the viral protease to produce the mature, infectious virion.

Synthesis, Assembly, and Processing of Viral Proteins.

Coffin JM, Hughes SH, Varmus HE, editors. Retroviruses. Cold Spring Harbor (NY): Cold Spring Harbor Laboratory Press; 1997.
FIGURE 3-3A 29-nt deletion in the human SCoV genome

(A) Genetic organization of SCoV-like viruses found in humans and animals. ORFs 1a and 1b, encoding the nonstructural polyproteins, and those encoding the S, E, M, and N structural proteins are indicated (green boxes). (B) Expanded view of the SCoV genomic sequence (27700 nt to 28200 nt, based on AY278554 numbering). ORFs for putative proteins and for N in human isolates are indicated as brown and green boxes, respectively (Marra et al., 2003). An extra 29-nt sequence is present downstream of the nucleotide of 27868 of the animal SCoV (based on AY278554 numbering). The presence of this 29-nt sequence in animals isolates results in fusing the ORFs 10 and 11 (top) into a new ORF (bottom; ORF10’, light blue box). (C) Protein sequence alignment of ORF10 and 11 from human isolates and ORF 10’ from animal isolates.

ISOLATION AND CHARACTERIZATION OF VIRUSES RELATED TO THE SARS CORONAVIRUS FROM ANIMALS IN SOUTHERN CHINA.

Institute of Medicine (US) Forum on Microbial Threats; Knobler S, Mahmoud A, Lemon S, et al., editors. Learning from SARS: Preparing for the Next Disease Outbreak: Workshop Summary. Washington (DC): National Academies Press (US); 2004.
Figure 1

The genomic structure and processing of HCV and HIV. A) The 9.6 kb positive strand RNA genome of HCV is illustrated with secondary structure of the 5′ and 3′ noncoding regions (NCR). The 3′ NCR contains several domains, including a single-stranded poly U/UC region (red box) in which the minimal HCV PAMP resides. HCV proteins are generated via IRES-mediated translation to a single long polyprotein that is processed into the mature structural and nonstructural HCV proteins. B) Schematic of the 9.2 kb HIV RNA genome which is capped and poly-adenylated. After reverse transcription and integration of the proviral DNA molecule into the host genome, HIV RNA transcripts are produced via differential splicing, yielding a number of proteins and polyproteins that are processed to their mature forms.

Innate Immune Evasion Strategies of HCV and HIV: Common Themes for Chronic Viral Infection.

Madame Curie Bioscience Database [Internet]. Austin (TX): Landes Bioscience; 2000-2013.
Figure 8

SCAN C₂H₂ proteins are vertebrate specific. The apparent number of SCAN domains found in databases of the worm, fly, zebrafish, frog, chicken, mouse, and human are indicated in the first column. The apparent number of SCAN-containing retrovirus-like polyproteins, compared to the apparent number of SCAN-containing C₂H₂ zinc finger proteins (ZFP), in the represented species is indicated in the second and third columns, respectively (ND, not determined). Searches were limited by the availability of less complete sequence databases for the chicken and frog. The predicted structure of a representative SCAN-containing protein is illustrated to the right of each number. The following conserved regions are indicated: SCAN domain (orange), CCHC zinc knuckle (red), retrovirus-like sequences (black), and C₂H₂ zinc finger (blue). The representative SCAN proteins are: human polyprotein KIAA1925 (Accession XP_166375), human zinc finger protein MGC4161 (Accession NP_077279), mouse zinc finger protein Zfp29 (Accession NP_033579), frog polyprotein (Xenopus laevis, Accession S33978), zebrafish polyprotein (Sanger Centre Accession dZ37K09). A color version of this figure can be viewed at www.Eurekah.com.

The Superfamily of SCAN Domain Containing Zinc Finger Transcription Factors.

Madame Curie Bioscience Database [Internet]. Austin (TX): Landes Bioscience; 2000-2013.