Retroviridae Proteins
Retroviridae
Retroviridae Proteins, Oncogenic
Spumavirus
Terminal Repeat Sequences
Retroelements
The SH2 domain-containing inositol 5'-phosphatase (SHIP) recruits the p85 subunit of phosphoinositide 3-kinase during FcgammaRIIb1-mediated inhibition of B cell receptor signaling. (1/834)
Coligation of FcgammaRIIb1 with the B cell receptor (BCR) or FcepsilonRI on mast cells inhibits B cell or mast cell activation. Activity of the inositol phosphatase SHIP is required for this negative signal. In vitro, SHIP catalyzes the conversion of the phosphoinositide 3-kinase (PI3K) product phosphatidylinositol 3,4, 5-trisphosphate (PIP3) into phosphatidylinositol 3,4-bisphosphate. Recent data demonstrate that coligation of FcgammaRIIb1 with BCR inhibits PIP3-dependent Btk (Bruton's tyrosine kinase) activation and the Btk-dependent generation of inositol trisphosphate that regulates sustained calcium influx. In this study, we provide evidence that coligation of FcgammaRIIb1 with BCR induces binding of PI3K to SHIP. This interaction is mediated by the binding of the SH2 domains of the p85 subunit of PI3K to a tyrosine-based motif in the C-terminal region of SHIP. Furthermore, the generation of phosphatidylinositol 3,4-bisphosphate was only partially reduced during coligation of BCR with FcgammaRIIb1 despite a drastic reduction in PIP3. In contrast to the complete inhibition of Tec kinase-dependent calcium signaling, activation of the serine/threonine kinase Akt was partially preserved during BCR and FcgammaRIIb1 coligation. The association of PI3K with SHIP may serve to activate PI3K and to regulate downstream events such as B cell activation-induced apoptosis. (+info)Two types of HTLV-1 particles are released from MT-2 cells. (2/834)
The MT-2 cell line transformed by human T-cell leukemia virus type 1 (HTLV-1) contains one complete provirus and seven defective proviruses. Four defective genomes have an identical structure (LTR-MA-deltaCA-pX-LTR) with an open reading frame that spans from MA to pX, giving rise to a 3.4-kb (24S) RNA transcript encoding a chimeric Gag-pX protein, p28. MT-2 cells release two distinct types of virions. The major "classic" type of particle has a buoyant density of 1.155-1.16 g/cm3 and contains the standard HTLV-I structural proteins and reverse transcriptase (RT). In addition, about 5% of particles are "light," approximately 1.12 g/cm3, and contain p28, RT activity, and the 3.4-kb RNA transcript. RT-PCR and in vitro translation indicate that some of the classic HTLV-1 particles package 3.4-kb RNA as well as full-length 8.5-kb RNA. In addition to matrix features, the p28 protein has a motif resembling a zinc finger at the C-terminal, pX0 region, which may play a role in the assembly of the defective light virions. (+info)Regulation of human immunodeficiency virus type 1 infectivity by the ERK mitogen-activated protein kinase signaling pathway. (3/834)
ERK1 and ERK2 mitogen-activated protein kinases (MAPK) play a critical role in regulation of cell proliferation and differentiation in response to mitogens and other extracellular stimuli. Mitogens and cytokines that activate MAPK in T cells have been shown to activate human immunodeficiency virus type 1 (HIV-1) replication. Little is known about the signal transduction pathways that activate HIV-1 replication in T cells upon activation by extracellular stimulation. Here, we report that activation of MAPK through the Ras/Raf/MEK signaling pathway enhances the infectivity of HIV-1 virions. Virus infectivity was enhanced by treatment of cells with MAPK stimulators, such as serum and phorbol myristate acetate, as well as by coexpression of constitutively activated Ras, Raf, or MEK (MAPK kinase) in the absence of extracellular stimulation. Treatment of cells with PD 098059, a specific inhibitor of MAPK activation, or with a MAPK antisense oligonucleotide reduced the infectivity of HIV-1 virions without significantly affecting virus production or the levels of virion-associated Gag and Env proteins. MAPK has been shown to regulate HIV-1 infectivity by phosphorylating Vif (X. Yang and D. Gabuzda, J. Biol. Chem. 273:29879-29887, 1998). However, MAPK activation enhanced virus infectivity in some cells lines that do not require Vif function. The HIV-1 Rev, Tat, p17(Gag), and Nef proteins were directly phosphorylated by MAPK in vitro, suggesting that other HIV-1 proteins are potential substrates for MAPK phosphorylation. These results suggest that activation of the ERK MAPK pathway plays a role in HIV-1 replication by enhancing the infectivity of HIV-1 virions through Vif-dependent as well as Vif-independent mechanisms. MAPK activation in producer cells may contribute to the activation of HIV-1 replication when T cells are activated by mitogens and other extracellular stimuli. (+info)A direct interaction between the adaptor protein Cbl-b and the kinase zap-70 induces a positive signal in T cells. (4/834)
Engagement of the T-cell receptor (TCR)-CD3 complex induces a rapid increase in the activities of Src-family and Syk/Zap-70-family kinases [1] [2]. These activated kinases then induce the tyrosine phosphorylation of multiple intracellular proteins, eventually leading to T-cell activation. One of the prominent substrates for these kinases is the adaptor protein Cbl [3] and recent studies suggest that Cbl negatively regulates upstream kinases such as Syk and Zap-70 [4] [5]. Cbl-b, a homologue of Cbl, is widely expressed in many tissues and cells including hematopoietic cells [6] [7]. Cbl-b undergoes rapid tyrosine phosphorylation upon stimulation of the TCR and cytokine receptors [8] [9]. The role of Cbl-b is unclear, however. Here, we show that overexpression of Cbl-b in T cells induced the constitutive activation of the transcription factor nuclear factor of activated T cells (NFAT). A loss-of-function mutation in Cbl-b disrupted the interaction between Cbl-b and Zap-70 and nearly completely abrogated the Cbl-b-mediated activation of NFAT. Unlike the proposed role of Cbl as a negative regulator, our results suggest that the Cbl homologue Cbl-b has a positive role in T-cell signaling, most likely via a direct interaction with the upstream kinase Zap-70. (+info)Anti-apoptotic signaling of the IGF-I receptor in fibroblasts following loss of matrix adhesion. (5/834)
The type 1 insulin-like growth factor receptor (IGF-IR) is known to protect cells from a variety of apoptotic injuries. In several instances, the anti-apoptotic effect of the wild type IGF-IR is more evident under conditions of anchorage-independence than in cells in monolayer cultures. We have investigated IGF-IR signaling in cells in anoikis, a form of apoptosis that occurs when cells are denied attachment to the extra-cellular matrix. IGF-I protects mouse embryo fibroblasts (MEF) from anoikis caused by withdrawal of growth factors. Survival is dependent on the concentration of IGF-I and a sufficient number of functional IGF-I receptors. In this model, IGF-I protection correlates best with ras activation and cell-to-cell aggregation, while PI3-kinase, Akt and MAP kinases seem to play a lesser, alternative role. (+info)Role of Nr13 in regulation of programmed cell death in the bursa of Fabricius. (6/834)
Apoptotic cell death is developmentally regulated in the chicken bursa of Fabricius. Although apoptosis is low in the embryonic bursa, cell death increases markedly after hatching. The expression of Bcl2 family cell death antagonists was examined to identify the genes that regulate bursal cell apoptosis. The expression of Bcl-xL, A1, and Mcl1 was detected in both embryos and hatched birds, whereas Nr13 was expressed at high levels in embryonic bursa, and decreased significantly after hatching, correlating inversely with apoptosis. The oncogene v-reland phorbol myristate acetate, two known inhibitors of bursal cell apoptosis, induced Nr13 expression. Overexpression of Nr13 in DT40 bursal lymphoma cells protected them from low serum-induced apoptosis. The mechanism of inhibition of apoptosis by Nr13 is likely to involve a critical BH4 domain and interaction with death agonist Bax. Deletion of the BH4 domain converted Nr13 into a death agonist. Bax coimmunoprecipitated with Nr13 and Bax was induced, whereas Nr13 levels diminished when bursal lymphoblasts were induced to apoptosis by dispersion. Bursal transplantation studies demonstrated that Nr13 could prevent the in vivo programmed elimination of bursal stem cells after hatching, suggesting that Nr13 plays a role in maintaining bursal stem cells. (+info)Cell surface retention sequence binding protein-1 interacts with the v-sis gene product and platelet-derived growth factor beta-type receptor in simian sarcoma virus-transformed cells. (7/834)
The cell surface retention sequence (CRS) binding protein-1 (CRSBP-1) is a newly identified membrane glycoprotein which is hypothesized to be responsible for cell surface retention of the oncogene v-sis and c-sis gene products and other secretory proteins containing CRSs. In simian sarcoma virus-transformed NIH 3T3 cells (SSV-NIH 3T3 cells), a fraction of CRSBP-1 was demonstrated at the cell surface and underwent internalization/recycling as revealed by cell surface 125I labeling and its resistance/sensitivity to trypsin digestion. However, the majority of CRSBP-1 was localized in intracellular compartments as evidenced by the resistance of most of the 35S-metabolically labeled CRSBP-1 to trypsin digestion, and by indirect immunofluorescent staining. CRSBP-1 appeared to form complexes with proteolytically processed forms (generated at and/or after the trans-Golgi network) of the v-sis gene product and with a approximately 140-kDa proteolytically cleaved form of the platelet-derived growth factor (PDGF) beta-type receptor, as demonstrated by metabolic labeling and co-immunoprecipitation. CRSBP-1, like the v-sis gene product and PDGF beta-type receptor, underwent rapid turnover which was blocked in the presence of 100 microM suramin. In normal and other transformed NIH 3T3 cells, CRSBP-1 was relatively stable and did not undergo rapid turnover and internalization/recycling at the cell surface. These results suggest that in SSV-NIH 3T3 cells, CRSBP-1 interacts with and forms ternary and binary complexes with the newly synthesized v-sis gene product and PDGF beta-type receptor at the trans-Golgi network and that the stable binary (CRSBP-1.v-sis gene product) complex is transported to the cell surface where it presents the v-sis gene product to unoccupied PDGF beta-type receptors during internalization/recycling. (+info)Analysis of human lymphotropic T-cell virus type II-like particle production by recombinant baculovirus-infected insect cells. (8/834)
The molecular processes involved in retrovirus assembly and budding formation remain poorly understood. The gag-pro-pol genes of human lymphotropic T-cell virus type II (HTLV-II) are translated into Gag, Gag-Pro, or Gag-Pro-Pol by frameshift events. In the present study, we investigated the roles of the gag, pro, and pol regions of HTLV-II in viral particle formation using recombinant baculoviruses. In this study we could successfully produce mature HTLV-II viral particles containing core structures using a construct expressing the entire gag-pro-pol region. We also investigated the role of the pol region in particle formation. Deletion of the pol region affects viral particle assembly or release very little, indicating that the gag-pro region is sufficient for viral particle formation and maturation. Expression of the Gag proteins alone or Gag proteins with inactivated viral proteases (Pro) resulted in the formation of viral particles; however, these particles did not contain core structures. These results suggest the intracellular expression of Gag with Pro of HTLV-II is essential for the production of mature virus particles, whereas that of Pol is not. (+info)Retroviridae is a family of viruses that includes HIV (Human Immunodeficiency Virus). Retroviridae proteins refer to the various structural and functional proteins that are encoded by the retroviral genome. These proteins can be categorized into three main groups:
1. Group-specific antigen (Gag) proteins: These proteins make up the viral matrix, capsid, and nucleocapsid. They are involved in the assembly of new virus particles.
2. Polymerase (Pol) proteins: These proteins include the reverse transcriptase, integrase, and protease enzymes. Reverse transcriptase is responsible for converting the viral RNA genome into DNA, which can then be integrated into the host cell's genome by the integrase enzyme. The protease enzyme is involved in processing the polyprotein precursors of Gag and Pol into their mature forms.
3. Envelope (Env) proteins: These proteins are responsible for the attachment and fusion of the virus to the host cell membrane. They are synthesized as a precursor protein, which is then cleaved by a host cell protease to form two distinct proteins - the surface unit (SU) and the transmembrane unit (TM). The SU protein contains the receptor-binding domain, while the TM protein forms the transmembrane anchor.
Retroviral proteins play crucial roles in various stages of the viral life cycle, including entry, reverse transcription, integration, transcription, translation, assembly, and release. Understanding the functions of these proteins is essential for developing effective antiretroviral therapies and vaccines against retroviral infections.
Retroviridae is a family of viruses that includes human immunodeficiency virus (HIV) and other viruses that primarily use RNA as their genetic material. The name "retrovirus" comes from the fact that these viruses reverse transcribe their RNA genome into DNA, which then becomes integrated into the host cell's genome. This is a unique characteristic of retroviruses, as most other viruses use DNA as their genetic material.
Retroviruses can cause a variety of diseases in animals and humans, including cancer, neurological disorders, and immunodeficiency syndromes like AIDS. They have a lipid membrane envelope that contains glycoprotein spikes, which allow them to attach to and enter host cells. Once inside the host cell, the viral RNA is reverse transcribed into DNA by the enzyme reverse transcriptase, which is then integrated into the host genome by the enzyme integrase.
Retroviruses can remain dormant in the host genome for extended periods of time, and may be reactivated under certain conditions to produce new viral particles. This ability to integrate into the host genome has also made retroviruses useful tools in molecular biology, where they are used as vectors for gene therapy and other genetic manipulations.
Retroviridae proteins, oncogenic, refer to the proteins expressed by retroviruses that have the ability to transform normal cells into cancerous ones. These oncogenic proteins are typically encoded by viral genes known as "oncogenes," which are acquired through the process of transduction from the host cell's DNA during retroviral replication.
The most well-known example of an oncogenic retrovirus is the Human T-cell Leukemia Virus Type 1 (HTLV-1), which encodes the Tax and HBZ oncoproteins. These proteins manipulate various cellular signaling pathways, leading to uncontrolled cell growth and malignant transformation.
It is important to note that not all retroviruses are oncogenic, and only a small subset of them have been associated with cancer development in humans or animals.
Spumavirus is actually referred to as " foamy virus" in medical terminology. It's a type of retrovirus, which means it uses RNA as its genetic material and has the ability to integrate its genetic material into the DNA of the host cell.
Spumaviruses are unique among retroviruses because they don't cause the same kind of diseases that other retroviruses do, like HIV. Instead, they're associated with a slow-growing, non-cancerous infection in various animal species, including cats and non-human primates. They're called "foamy viruses" because of the foamy or bubbly appearance of the infected cells when viewed under a microscope.
It's important to note that while spumaviruses can infect human cells in laboratory experiments, there's no evidence that they cause disease in humans.
Terminal repeat sequences (TRS) are repetitive DNA sequences that are located at the termini or ends of chromosomes, plasmids, and viral genomes. They play a significant role in various biological processes such as genome replication, packaging, and integration. In eukaryotic cells, telomeres are the most well-known TRS, which protect the chromosome ends from degradation, fusion, and other forms of DNA damage.
Telomeres consist of repetitive DNA sequences (5'-TTAGGG-3' in vertebrates) that are several kilobases long, associated with a set of shelterin proteins that protect them from being recognized as double-strand breaks by the DNA repair machinery. With each cell division, telomeres progressively shorten due to the end replication problem, which can ultimately lead to cellular senescence or apoptosis.
In contrast, prokaryotic TRS are often found at the ends of plasmids and phages and are involved in DNA replication, packaging, and integration into host genomes. For example, the attP and attB sites in bacteriophage lambda are TRS that facilitate site-specific recombination during integration and excision from the host genome.
Overall, terminal repeat sequences are essential for maintaining genome stability and integrity in various organisms, and their dysfunction can lead to genomic instability, disease, and aging.
Retroelements are a type of mobile genetic element that can move within a host genome by reverse transcription of an RNA intermediate. They are called "retro" because they replicate through a retrotransposition process, which involves the reverse transcription of their RNA into DNA, and then integration of the resulting cDNA into a new location in the genome.
Retroelements are typically divided into two main categories: long terminal repeat (LTR) retrotransposons and non-LTR retrotransposons. LTR retrotransposons have direct repeats of several hundred base pairs at their ends, similar to retroviruses, while non-LTR retrotransposons lack these repeats.
Retroelements are widespread in eukaryotic genomes and can make up a significant fraction of the DNA content. They are thought to play important roles in genome evolution, including the creation of new genes and the regulation of gene expression. However, they can also cause genetic instability and disease when they insert into or near functional genes.
Retroviridae infections refer to diseases caused by retroviruses, which are a type of virus that integrates its genetic material into the DNA of the host cell. This allows the virus to co-opt the cell's own machinery to produce new viral particles and infect other cells.
Some well-known retroviruses include human immunodeficiency virus (HIV), which causes AIDS, and human T-lymphotropic virus (HTLV), which can cause certain types of cancer and neurological disorders.
Retroviral infections can have a range of clinical manifestations depending on the specific virus and the host's immune response. HIV infection, for example, is characterized by progressive immunodeficiency that makes the infected individual susceptible to a wide range of opportunistic infections and cancers. HTLV infection, on the other hand, can cause adult T-cell leukemia/lymphoma or tropical spastic paraparesis, a neurological disorder.
Prevention and treatment strategies for retroviral infections depend on the specific virus but may include antiretroviral therapy (ART), vaccination, and behavioral modifications to reduce transmission risk.
Oncogenic retroviridae protein
Carcinogenesis
List of MeSH codes (D12.776)
Index of biochemistry articles
Avian sarcoma leukosis virus
Jaagsiekte sheep retrovirus
Human T-lymphotropic virus 1
Enzootic nasal tumor virus
Gibbon ape leukemia virus
Mason-Pfizer monkey virus
Retrovirus
Oncogenic retroviridae protein - Wikipedia
Transcriptional down-regulation of tumor necrosis factor-alpha gene expression by a synthetic peptide homologous to retroviral...
Janice M Andrews - Citation Index - NCSU Libraries
Analysis of Tat protein characteristics in human immunodeficiency virus type 1 sub-subtype A6 (Retroviridae: Orthoretrovirinae:...
DeCS
Gene Products, nef | Palmetto Profiles
Raf, but not MEK or ERK, is sufficient for differentiation of hippocampal neuronal cells. | Profiles RNS
Genes env. Medical search. Definitions
Gene Products, env | Colorado PROFILES
Gene Products, gag | Profiles RNS
M3i - IBMC
Background 'Intrinsic' level of resistance to retroviral infection was 1st recognised - PARP Inhibitors in Ovarian and Other...
Transativadores/genética
JAK Kinase - How NF-B is activated: the role of the IB kinase (IKK) complex
Yongseok Choi - Research output - Korea University
The virome of HPV-positive tonsil squamous cell carcinoma and neck metastasis | Oncotarget
Human LAMC2 / Laminin Gamma 2 Quant ELISA Kit | Sandwich | LSBio
Molecular epidemiology, genetic variability and evolution of HTLV-1 with special emphasis on African genotypes | Retrovirology ...
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DeCS 2014 - October 20, 2014 version
DeCS 2010 - February 12, 2010 version
Search | Global Index Medicus
Retroviral6
- Oncogenic retroviridae proteins are retroviral proteins that have the ability to transform cells. (wikipedia.org)
- Not all retroviral proteins are oncogenic. (wikipedia.org)
- Retroviral proteins, often glycosylated, coded by the envelope (env) gene. (lookformedical.com)
- Proteins coded by the retroviral gag gene. (lookformedical.com)
- Outcomes We produced retroviral vectors pseudotyped with different gamma and lentiviral Envs on MLV-B and -NB CAs formulated with a green neon proteins (GFP) news reporter. (siamtech.net)
- Over-expression, incorporation near oncogenic loci, or the website hosts' response to the protein encoded by retroviral genetics determine the type of disease demonstrated [1]. (siamtech.net)
Precursors2
- They are usually synthesized as protein precursors (POLYPROTEINS) and later cleaved into the final viral envelope glycoproteins by a viral protease. (lookformedical.com)
- The products are usually synthesized as protein precursors or POLYPROTEINS, which are then cleaved by viral proteases to yield the final products. (lookformedical.com)
Orthoretrovirinae1
- HTLV-1 is a member of the Retroviridae family, the Orthoretrovirinae subfamily and the Deltaretrovirus genus, which includes bovine leukemia virus (BLV) and T-lymphotropic viruses infecting primates (PTLV). (biomedcentral.com)
Lentivirus1
- Directed evolution of retrovirus envelope protein cytoplasmic tails guided by functional incorporation into lentivirus particles. (ucdenver.edu)
Envelope protein3
- External envelope protein of the human immunodeficiency virus which is encoded by the HIV env gene. (lookformedical.com)
- Transmembrane envelope protein of the HUMAN IMMUNODEFICIENCY VIRUS which is encoded by the HIV env gene. (lookformedical.com)
- It serves as a precursor for both the HIV ENVELOPE PROTEIN GP120 and the HIV ENVELOPE PROTEIN GP41 . (lookformedical.com)
Transcriptional4
- Proteína transcriptional, que actúa en trans, de los elementos promotores que se encuentran en las repeticiones largas del extremo (LTR) del HTLV-I y HTLV-II. (bvsalud.org)
- Transcriptional trans-acting proteins of the promoter elements found in the long terminal repeats (LTR) of HUMAN T-LYMPHOTROPIC VIRUS 1 and HUMAN T-LYMPHOTROPIC VIRUS 2. (bvsalud.org)
- As a single-strand nucleic acid binding protein it functions in both transcriptional and post-transcriptional regulation, while facilitating multiple stages of RNA metabolism to affect proliferation and control cell fate. (bvsalud.org)
- TAZ (WWTR1) is a transcriptional co-activator regulated by Hippo signaling, mechano-transduction, and G-protein couple receptors. (bvsalud.org)
Genus1
- The murine leukaemia infections (MLVs) are associates of the gamma-retrovirus genus of the Retroviridae family members. (siamtech.net)
Regulatory2
- K homology-type splicing regulatory protein (KSRP) is emerging as a key player in cancer biology, and immunology. (bvsalud.org)
- Here we provide an minireview of this important regulatory protein and describe its complex subcellular functions to affect RNA metabolism, stability, miRNA biogenesis and maturation, stress granule function, metastasis, and inflammatory processes. (bvsalud.org)
Viral2
- They play a role as accessory proteins that influence the rate of viral infectivity and the destruction of the host immune system. (musc.edu)
- DNA sequences that form the coding region for the viral envelope (env) proteins in retroviruses. (lookformedical.com)
GENE1
- The env genes contain a cis-acting RNA target sequence for the rev protein (= GENE PRODUCTS, REV ), termed the rev-responsive element (RRE). (lookformedical.com)
Primary1
- This is referred to as the primary structure of proteins. (lookformedical.com)
Determine2
- On the computer virus part, in the past, a one amino acidity (aa) in the California proteins at placement 110 is certainly idea to determine if MLVs are T or D tropic [8,9]. (siamtech.net)
- However, it must interact with other proteins to determine the fate of its bound substrate. (bvsalud.org)
Cancer1
- Oncogenic KRAS-Induced Protein Signature in the Tumor Secretome Identifies Laminin-C2 and Pentraxin-3 as Useful Biomarkers for the Early Diagnosis of Pancreatic Cancer. (lsbio.com)
Target1
- Nonstructural HIV proteins can become a promising target of future therapeutic agents and vaccines [ 1-3 ]. (crie.ru)
Oncogenes2
Retroviruses2
- In addition, rel proteins are likely to be involved in T cell diseases caused by the human retroviruses HTLV-I and HIV-1. (nih.gov)
- Genus of non-oncogenic retroviruses which establish persistent infections in many animal species but are considered non-pathogenic. (lookformedical.com)
Capsid1
- The proteins assembling the capsid of presumably icosahedral structure are encoded by the gag region as well as the protease. (medscape.com)
Mammary1
- A protein related to the main core protein of the mouse mammary cancer virus in a microparticle fraction of human milk]. (uchicago.edu)
Oncogene Protein4
- Oncogene Protein p21(ras)" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (uams.edu)
- Oncogene protein p21(ras) has been directly implicated in human neoplasms, perhaps accounting for as much as 15-20% of all human tumors. (uams.edu)
- This graph shows the total number of publications written about "Oncogene Protein p21(ras)" by people in UAMS Profiles by year, and whether "Oncogene Protein p21(ras)" was a major or minor topic of these publications. (uams.edu)
- Below are the most recent publications written about "Oncogene Protein p21(ras)" by people in Profiles over the past ten years. (uams.edu)
Genes2
- Similarly, rel family proteins control a number of genes involved in lymphoid cell growth and differentiation. (nih.gov)
- C) Prophage genes are repressed by a repressor protein coded for by the prophage. (studymoose.com)
Diseases caused1
- Virus diseases caused by the RETROVIRIDAE . (lookformedical.com)
Transforming2
- They usually have transforming and often protein kinase activities. (childrensmercy.org)
- Stacey DW, Watson T, Kung HF, Curran T. Microinjection of transforming ras protein induces c-fos expression. (childrensmercy.org)
Genetic1
- After fusion of the lipid membranes of the virus and host cell, the genetic material of the virus and the pol -encoded proteins are transferred to the cytoplasm. (medscape.com)
Infections1
- Retroviridae infections. (lookformedical.com)
Encodes1
- env encodes the transcription unit for the envelope protein. (medscape.com)
Fusion protein1
- This is a gag-onc fusion protein of about 65 kDa derived from avian sarcoma virus. (nih.gov)
Virus1
- The most frequently encountered member of this family is the Rous sarcoma virus protein. (lookformedical.com)
Family1
- Proteins from the family Retroviridae . (lookformedical.com)
Transcription1
- The two proteins required for reverse transcription of the viral RNA, reverse transcriptase and integrase, are encoded by the pol region. (medscape.com)
People1
- Below are the most recent publications written about "Retroviridae Proteins" by people in Profiles. (uchicago.edu)
Cells1
- Point mutations in the cellular ras gene (c-ras) can also result in a mutant p21 protein that can transform mammalian cells. (uams.edu)