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Core protein

Bdttcher B, Wynne S A and Crowther R A 1997 Determination of the foid of the core protein of hepatitis B virus by eiectron cryomicroscopy Nature 386 88-91... [Pg.1651]

The core protein of alphavirus has a chymotrypsin-like fold... [Pg.340]

Figure 16.21 Structure of one subunit of the core protein of Slndbls virus. The protein has a similar fold to chymotrypsin and other serine proteases, comprising two Greek key motifs separated by an active site cleft. The C-terminus of the protein is bound in the catalytic site, making the coat protein inactive (Adapted from S. Lee et al., Structure 4 531-541, 1996.)... Figure 16.21 Structure of one subunit of the core protein of Slndbls virus. The protein has a similar fold to chymotrypsin and other serine proteases, comprising two Greek key motifs separated by an active site cleft. The C-terminus of the protein is bound in the catalytic site, making the coat protein inactive (Adapted from S. Lee et al., Structure 4 531-541, 1996.)...
Choi, H.-K., et al. Structure of Sindbis virus core protein reveals a chymotrypsin-like serine proteinase and the organization of the virion. Nature 354 37-43, 1991. [Pg.345]

Glycosydation AChE and BChE carry 3 and 9, respectively, N-glycosylation consensus sequences attaching carbohydrate residues to the core protein via asparagines. Different molecular forms of the enzymes in various tissues, show different number and composition of carbohydrate residues. N-glycosylation at all sites was shown to be important for effective biosynthesis, secretion and clearance of ChEs from the circulation. Altered patterns of AChE glycosylation have been observed in the brain and cerebrospinal fluid of Alzheimer s disease (AD) patients, with potential diagnostic value. [Pg.359]

The most ingenious exocytosis toxins, however, come from the anaerobic bacteria Clostridium botulinum and Clostridium tetani. The former produces the seven botulinum neurotoxins (BoNTs) A-G the latter produces tetanus neurotoxin (TeNT). All eight toxins consist of a heavy (H) chain and a light (L) chain that are associated by an interchain S-S bond. The L-chains enter the cytosol of axon terminals. Importantly, BoNT L-chains mainly enter peripheral cholinergic terminals, whereas the TeNT L-chain mainly enters cerebral and spinal cord GABAergic and glycinergic terminals. The L-chains are the active domains of the toxins. They are zinc-endopeptidases and specifically split the three core proteins of exocytosis, i.e. the SNAREs (Fig. 1 inset). Each ofthe eight toxins splits a... [Pg.1173]

Fig. 1 Antiviral genes inhibit virus replication at different stages of the viral life cycle. Early inhibitors prevent the establishment of the viral genome in the target cell (class I, e.g., entry inhibitors, RT inhibitors for HIV). Intermediate inhibitors prevent viral gene expression or amplification of the viral genome (class II, e.g., siRNAs, antisense RNAs). Late inhibitors prevent virion assembly or release, or inactivate the mature virions (class III, e.g., transdominant core proteins, capsid-targeted virion inactivation, CTVI). A list of antiviral genes in each class is found in Table 1... Fig. 1 Antiviral genes inhibit virus replication at different stages of the viral life cycle. Early inhibitors prevent the establishment of the viral genome in the target cell (class I, e.g., entry inhibitors, RT inhibitors for HIV). Intermediate inhibitors prevent viral gene expression or amplification of the viral genome (class II, e.g., siRNAs, antisense RNAs). Late inhibitors prevent virion assembly or release, or inactivate the mature virions (class III, e.g., transdominant core proteins, capsid-targeted virion inactivation, CTVI). A list of antiviral genes in each class is found in Table 1...
Yamamoto M, Hayashi N, Takehara T, Ueda K, Mita E, Tatsumi T, Sasaki Y, Kasahara A, Hori M (1999) Intracellular single-chain antibody against hepatitis B virus core protein inhibits the replication of hepatitis B virus in cultured cells. Hepatology 30 300-307 Yang 00, Tran AC, Kalams SA, Johnson RP, Roberts MR, Walker BD (1997) Lysis of HIV-1-infected cells and inhibition of viral replication by universal receptor T cells, Proc Natl Acad Sci USA 94 11478-11483... [Pg.298]

The Rieske protein in mitochondrial bci complexes is assembled when the protein is incorporated into the complex. The Rieske protein is encoded in the nucleus and synthesized in the cytosol with a mitochondrial targeting presequence, which is required to direct the apoprotein to the mitochondrial matrix. The C-terminus is then targeted back to the outside of the inner mitochondrial membrane where the Rieske cluster is assembled. In addition, the presequence is removed and the protein is processed to its mature size after the protein is inserted into the bci complex. In mammals, the presequence is cleaved in a single step by the core proteins 1 and 2, which are related to the general mitochondrial matrix processing protease (MPP) a and (3 subunits the bovine heart presequence is retained as a 8.0 kDa subunit of the complex (42, 107). In Saccharomyces cerevis-iae, processing occurs in two steps Initially, the yeast MPP removes 22 amino acid residues to convert the precursor to the intermediate form, and then the mitochondrial intermediate protease (MIP) removes 8 residues after the intermediate form is in the bci complex (47). Cleavage by MIP is independent of the assembly of the Rieske cluster Conversion of the intermediate to the mature form was observed in a yeast mutant that did not assemble any Rieske cluster (35). However, in most mutants where the assembly of the Rieske cluster is prevented, the amount of Rieske protein is drastically reduced, most likely because of instability (35, 44). [Pg.144]

Biosynthesis of Giycosaminogiycans Invoives Attachment to Core Proteins, Chain Eiongation, Chain Termination... [Pg.542]

The linkage between GAGs and their core proteins is generally one of three types. [Pg.542]

The synthesis of the core proteins occurs in the endoplasmic reticulum, and formation of at least some of the above linkages also occurs there. Most of the later steps in the biosynthesis of GAG chains and their subsequent modifications occur in the Golgi apparatus. [Pg.543]

Certain proteoglycans (eg, heparan sulfate) are associated with the plasma membrane of cells, with their core proteins acmally spanning that membrane. In it they may act as receptors and may also participate in the mediation of cell growth and cell-cell communication. The attachment of cells to their substramm in cul-mre is mediated at least in part by heparan sulfate. This proteoglycan is also found in the basement membrane of the kidney along with type IV collagen and laminin... [Pg.547]

The core proteins of DS-PG I and DS-PG II are homologous to those of CS-PG I and CS-PG II found In bone (Table 48-9). A possible explanation Is that osteoblasts lack the epimerase required to convert glucuronic acid to Iduronic acid, the latter of which Is found In dermatan sulfate. [Pg.551]

GAGs occur in tissues bound to various proteins (hnker proteins and core proteins), constituting proteoglycans. These structures are often of very high molecular weight and serve many functions in tissues. [Pg.554]

Hall et al. [62] identified in a separate study the same glycoprotein in H,K-ATPase vesicles isolated from porcine gastric mucosa. A stoichiometric ratio of 1.2 1.0 was found for the deglycosylated protein (35 kDa)/catalytic 94-kDa protein. Furthermore, compelling evidence that this glycoprotein is the H,K-ATPase p subunit was provided by N-terminal sequence analysis of three protease V8-obtained peptides of the 35-kDa core protein. These peptides showed 30% and 45% homology with the Na,K-ATPase pi and pi subunit, respectively. [Pg.32]

Hepatitis B is diagnosed when HBsAg is detectable in the serum. The nucleocapsid of the HBsAg contains the core protein that produces HBcAg, which is undetectable in the serum. The presence of antibodies against anti-HBc to IgM indicates active infection, and anti-HBc to IgG relates to either chronic infection or possible immunity against HBV. [Pg.348]

Many fundamental studies of PBs have been performed in yeast (Sheth and Parker, 2003 Teixeira et al., 2005). Mammalian PBs contain many core proteins found in yeast, but also contain a number of metazoan-specific proteins hence, some functions of mammalian PBs are likely lacking in yeast. Mammalian PBs (also known as GWBs [Eystathioy et al., 2002, 2003] or DCP foci [Ingelfinger et al., 2002 van Dijk et al., 2002], contain components of the 5 to 3 decay machinery (Xrnl, DCP1/DCP2,... [Pg.98]

Sternfeld, M., Ming, G., Song, H., Sela, K., Poo, M. and Soreq, H. (1998). Acetylcholinesterase enhances neutrite growth and synapse development through alternative contributions of its hydrolytic capacity, core protein, and variable C termini. Journal of Neuroscience 18 1240-1249. [Pg.166]


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See also in sourсe #XX -- [ Pg.542 , Pg.543 ]

See also in sourсe #XX -- [ Pg.223 ]




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Alphaviruses core proteins

Core protein hyaluronan

Decorin Proteoglycans protein core

Endoplasmic reticulum core protein synthesis

Golgi apparatus core protein synthesis

HMGN proteins with the nucleosome core particle

Protein glycosylation pentasaccharide core

Proteins hydrophobic core

Proteoglycans core protein

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