Pub-set ::= medline {
{
uid 88055872,
em std { year 1988, month 3 },
cit {
title {
name "Developmental regulation of a constitutively expressed mouse mRNA encodi
ng a 72-kDa heat shock-like protein." },
authors {
names ml {
"Giebel LB",
"Dworniczak BP",
"Bautz EK" },
affil str "Zentrum fur Molekulare Biologie, Universitat Heidelberg (ZMBH), Fed
eral Republic of Germany." },
from journal {
title  { ml-jta "Dev Biol" },
imp {
date std {
year 1988,
month 1
},
volume "125",
issue "1",
pages "200-7"} } -- end Cit-jour
}, -- end Cit-art
abstract "Multiple heat shock cognate (hsc70) cDNA clones were isolated from t
he mouse embryonal carcinoma cell line F9. They all encode a single 72-kDa pro
tein, which is constitutively expressed in all mouse cell lines and tissues te
sted, and which is only slightly induced by hyperthermia. hsc70 RNA is very ab
undant in F9 stem cells and brain, but very little is found in 14-day-old embr
yos. Upon differentiation of F9 stem cells induced by retinoic acid and cyclic
 AMP, expression of the hsc70 gene decreases only slightly, suggesting that hs
c70 is highly expressed in early mouse development and is then down-regulated 
towards the end of embryogenesis. In adult tissues only the brain retains the 
high level of hsc70 gene expression found in F9 stem cells. We also show that 
expression of hsc70 protein and clathrin is uncoupled in F9 cells, indicating 
that the uncoating activity of coated vesicles may not be the only function of
 hsc70 protein.",
mesh {
{ term "Amino Acid Sequence" },
{ term "Animal" },
{ term "Base Sequence" },
{ term "Cell Differentiation" },
{ term "Clathrin",
qual { { subh "metabolism" }}},
{ term "Cloning, Molecular" },
{ term "DNA",
qual { { subh "analysis" }}},
{ term "Gene Expression Regulation" },
{ term "Heat-Shock Proteins",
qual { { mp TRUE, subh "genetics" }}},
{ term "Mice" },
{ term "Molecular Sequence Data" },
{ term "RNA, Messenger",
qual { { mp TRUE, subh "analysis" }}},
{ term "Stem Cells",
qual { { subh "cytology" }}},
{ term "Support, Non-U.S. Gov't" },
{ term "Translation, Genetic" }},
substance {
{ type cas, cit "9007-49-2", name "DNA" }},
xref {
{ type genbank, cit "M19141" }}
}, -- end Medline-entry
{
uid 88055881,
em std { year 1988, month 3 },
cit {
title {
name "Complex developmental regulation of the Drosophila affinidisjuncta alcoh
ol dehydrogenase gene in Drosophila melanogaster." },
authors {
names ml {
"Brennan MD",
"Dickinson WJ" },
affil str "Department of Biology, University of Alabama, Tuscaloosa 35486." },
from journal {
title  { ml-jta "Dev Biol" },
imp {
date std {
year 1988,
month 1
},
volume "125",
issue "1",
pages "64-74"} } -- end Cit-jour
}, -- end Cit-art
abstract "During development, the alcohol dehydrogenase genes of Drosophila me
lanogaster and D. affinidisjuncta are expressed in similar, yet distinct, tiss
ue- and stage-specific patterns. Transcripts from both of these genes arise fr
om two promoters (distal and proximal) that also display tissue and stage spec
ificity. We used P-element-mediated transformation to introduce the D. affinid
isjuncta Adh gene into the germ line of D. melanogaster. We show that the D. a
ffinidisjuncta Adh gene is expressed at comparable overall levels in both spec
ies and that the tissue- and stage-specific expression for this gene (includin
g promoter utilization) is similar in the donor and the host species. However,
 in some details, the expression of the D. affinidisjuncta gene in D. melanoga
ster resembles the host pattern, and one novel tissue-specific expression phen
otype is displayed by transformants. In general, our results suggest that ther
e has been strong conservation of cis- and trans-acting regulatory factors sin
ce the divergence of the two species but that this conservation has not been p
erfect.",
mesh {
{ term "Alcohol Dehydrogenase",
qual { { mp TRUE, subh "genetics" }}},
{ term "Animal" },
{ term "Drosophila",
qual { { mp TRUE, subh "genetics" }}},
{ term "Drosophila Melanogaster",
qual { { mp TRUE, subh "genetics" }}},
{ term "Female" },
{ term "Gene Expression Regulation" },
{ term "Male" },
{ term "Nucleic Acid Hybridization" },
{ term "Promoter Regions (Genetics)" },
{ term "Support, U.S. Gov't, P.H.S." },
{ term "Transcription, Genetic" }},
substance {
{ type ec, cit "1.1.1.1", name "Alcohol Dehydrogenase" }},
idnum {
"1RO1-GM34961",
"5RO1-HD10723" }
}, -- end Medline-entry
{
uid 88055884,
em std { year 1988, month 3 },
cit {
title {
name "Transcripts of the Drosophila blastoderm-specific locus, terminus, are c
oncentrated posteriorly and encode a potential DNA-binding finger." },
authors {
names ml {
"Baldarelli RM",
"Mahoney PA",
"Salas F",
"Gustavson E",
"Boyer PD",
"Chang MF",
"Roark M",
"Lengyel JA" },
affil str "Molecular Biology Institute, UCLA 90024." },
from journal {
title  { ml-jta "Dev Biol" },
imp {
date std {
year 1988,
month 1
},
volume "125",
issue "1",
pages "85-95"} } -- end Cit-jour
}, -- end Cit-art
abstract "The commitment of cells to specific fates, as well as the transition
s in the cell cycle and transcription that occur at the cellular blastoderm st
age of Drosophila embryogenesis, suggest that there are genes with unique func
tions expressed specifically at this stage. In an attempt to identify such gen
es, we used molecular screening to isolate several loci which encode blastoder
m-specific transcripts (Roark et al., (1985). Dev. Biol. 109, 476-488). We rep
ort here the complete nucleotide sequence of one of these genes, terminus (ter
), which maps to 75C1,2. The predicted ter protein possesses a transcription f
actor IIIA (TFIIIA)-like putative Zn-binding, DNA-binding finger. The ter RNA,
 detected by in situ hybridization, is distributed uniformly in the embryo dur
ing the syncytial blastoderm stage, and then becomes more concentrated in the 
posterior during the late cellular blastoderm stage. During gastrulation, the 
RNA is most concentrated in the amnioproctodeal invagination; it is also found
 at a lower concentration in the ventral furrow and in the anterodorsal neurog
enic region. By the end of germ band extension, ter RNA is no longer detected.
",
mesh {
{ term "Amino Acid Sequence" },
{ term "Animal" },
{ term "Base Sequence" },
{ term "Blastoderm",
qual { { mp TRUE, subh "analysis" }}},
{ term "Chromosome Mapping" },
{ term "Drosophila",
qual { { mp TRUE, subh "genetics" }}},
{ term "DNA-Binding Proteins",
qual { { mp TRUE, subh "genetics" }}},
{ term "Molecular Sequence Data" },
{ term "Support, U.S. Gov't, Non-P.H.S." },
{ term "Support, U.S. Gov't, P.H.S." },
{ term "Transcription Factors",
qual { { subh "genetics" }}},
{ mp TRUE, term "Transcription, Genetic" },
{ term "Zinc",
qual { { subh "metabolism" }}}},
substance {
{ type nameonly, name "transcription factor TFIIIA" },
{ type cas, cit "7440-66-6", name "Zinc" }},
xref {
{ type genbank, cit "M19140" }},
idnum {
"HD 09948",
"GM07185",
"07104" }
}, -- end Medline-entry
{
uid 88062968,
em std { year 1988, month 3 },
cit {
title {
name "Antigenic site II of the rabies virus glycoprotein: structure and role i
n viral virulence." },
authors {
names ml {
"Prehaud C",
"Coulon P",
"LaFay F",
"Thiers C",
"Flamand A" },
affil str "Laboratoire de Genetique des Virus, Centre National de la Recherche
 Scientifique, Gif sur Yvette, France." },
from journal {
title  { ml-jta "J Virol" },
imp {
date std {
year 1988,
month 1
},
volume "62",
issue "1",
pages "1-7"} } -- end Cit-jour
}, -- end Cit-art
abstract "Twelve monoclonal antibodies neutralizing the CVS strain of rabies v
irus were used to characterize antigenic site II of the viral glycoprotein. Ni
neteen antigenic mutants resistant to neutralization by some of these antibodi
es were selected; some continued to normally or partially bind the antibody, w
hereas others did not. Mutations conferring resistance to neutralization by si
te II-specific monoclonal antibodies were localized into two clusters, the fir
st between amino acids 34 and 42 (seven groups of mutants) and the second at a
mino acids 198 and 200 (three groups of mutants). Two intermediate mutations w
ere identified at positions 147 and 184. Four mutations resulted in reduced pa
thogenicity after intramuscular inoculation of the virus in adult mice. One of
 the mutants, M23, was 300 times and the others were 10 to 30 times less patho
genic than CVS. In three cases the attenuated phenotype was related to an impo
rtant modification of antigenic site II, whereas the other known antigenic sit
es were unchanged.",
mesh {
{ term "Amino Acid Sequence" },
{ term "Antibodies, Monoclonal",
qual { { mp TRUE, subh "immunology" }}},
{ term "Antigenic Determinants" },
{ term "Antigens, Viral",
qual { { subh "genetics" },
 { mp TRUE, subh "immunology" }}},
{ term "Glycoproteins",
qual { { subh "genetics" },
 { mp TRUE, subh "immunology" }}},
{ term "Molecular Sequence Data" },
{ term "Mutation" },
{ term "Neutralization Tests" },
{ term "Rabies Virus",
qual { { mp TRUE, subh "immunology" },
 { subh "pathogenicity" }}},
{ term "Support, Non-U.S. Gov't" },
{ term "Viral Proteins",
qual { { subh "genetics" },
 { mp TRUE, subh "immunology" }}}}
}, -- end Medline-entry
{
uid 88062969,
em std { year 1988, month 3 },
cit {
title {
name "Sequence homology and immunologic cross-reactivity of human cytomegalovi
rus with HLA-DR beta chain: a means for graft rejection and immunosuppression.
" },
authors {
names ml {
"Fujinami RS",
"Nelson JA",
"Walker L",
"Oldstone MB" },
affil str "Department of Pathology, University of California, San Diego, La Jo
lla 92093." },
from journal {
title  { ml-jta "J Virol" },
imp {
date std {
year 1988,
month 1
},
volume "62",
issue "1",
pages "100-5"} } -- end Cit-jour
}, -- end Cit-art
abstract "A peptide (Leu-Gly-Arg-Pro-Asp-Glu-Asp-Ser-Ser-Ser-Ser-Ser-Ser-Ser-C
ys) that was identical to residues 82 through 96 of a predicted protein of 208
 amino acids from the immediate-early region (IE-2) nucleic acid sequence of h
uman cytomegalovirus was chemically synthesized. By computer analysis, the fir
st five amino acids of this peptide showed sequence homology to the beta chain
 of the human histocompatibility complex HLA-DR. The homologous amino acids, 5
3 through 57, were located in a region that is conserved between the human DR 
beta chain and the beta chain of the H-2 class II histocompatibility antigen f
or mice. The shared region between the IE-2 protein and DR beta chain were sim
ilar in both hydrophilicity and predicted beta-turn potential. The IE-2 viral 
peptide induced antibodies that specifically recognized the human DR beta chai
n. These observations describe a protein encoded by the IE-2 region of human c
ytomegalovirus that contains sequence homology and shows immunologic cross-rea
ctivity with a conserved domain of HLA-DR and suggest a mechanism to explain h
ow human cytomegalovirus infection contributes to graft rejection after transp
lantation.",
mesh {
{ term "Amino Acid Sequence" },
{ term "Antigenic Determinants" },
{ term "Antigens, Viral",
qual { { mp TRUE, subh "immunology" }}},
{ term "Cross Reactions" },
{ term "Cytomegaloviruses",
qual { { mp TRUE, subh "immunology" }}},
{ term "Graft Rejection" },
{ term "HLA-D Antigens",
qual { { mp TRUE, subh "immunology" }}},
{ term "HLA-DR Antigens",
qual { { mp TRUE, subh "immunology" }}},
{ term "Immune Tolerance" },
{ term "Immunosorbent Technics" },
{ term "Sequence Homology, Nucleic Acid" },
{ term "Support, Non-U.S. Gov't" },
{ term "Support, U.S. Gov't, P.H.S." },
{ term "Viral Proteins",
qual { { mp TRUE, subh "immunology" }}}},
idnum {
"AI-07007",
"AI-21640",
"CA-35048",
"+" }
}, -- end Medline-entry
{
uid 88062973,
em std { year 1988, month 3 },
cit {
title {
name "Localization of sequences responsible for trans-activation of the equine
 infectious anemia virus long terminal repeat." },
authors {
names ml {
"Sherman L",
"Gazit A",
"Yaniv A",
"Kawakami T",
"Dahlberg JE",
"Tronick SR" },
affil str "Department of Human Microbiology, Sackler Faculty of Medicine, Tel-
Aviv University, Israel." },
from journal {
title  { ml-jta "J Virol" },
imp {
date std {
year 1988,
month 1
},
volume "62",
issue "1",
pages "120-6"} } -- end Cit-jour
}, -- end Cit-art
abstract "We used the Escherichia coli chloramphenicol acetyltransferase gene 
(cat) to study sequences that influence expression of the equine infectious an
emia virus (EIAV) genome. The EIAV long terminal repeat (LTR) directed CAT act
ivity in a canine cell line, but at levels much lower than those achieved with
 other eucaryotic viral promoters. In the same cells infected with EIAV or cot
ransfected with molecularly cloned EIAV genomic DNA, LTR-directed activity was
 markedly enhanced. Comparison of cat mRNA and protein levels in these cells i
ndicated that this trans-activating effect could be accounted for by a bimodal
 mechanism in which both transcriptional and posttranscriptional events are en
hanced. trans-Activation but not promoter activity was abolished by deletion o
f the R-U5 region of the EIAV LTR. EIAV sequences responsible for the trans-ac
tivating function could be localized to a region encompassing the 3' and 5' te
rmini of the pol and env genes, respectively (nucleotides 4474 to 5775). Inter
estingly, this stretch harbors a short open reading frame with some amino acid
 sequence similarity to the human immunodeficiency virus type I tat gene produ
ct.",
mesh {
{ term "DNA Mutational Analysis" },
{ term "Equine Infectious Anemia Virus",
qual { { mp TRUE, subh "genetics" }}},
{ term "Gene Expression Regulation" },
{ term "Genes, Viral" },
{ mp TRUE, term "Promoter Regions (Genetics)" },
{ mp TRUE, term "Regulatory Sequences, Nucleic Acid" },
{ mp TRUE, term "Repetitive Sequences, Nucleic Acid" },
{ term "Transcription Factors",
qual { { mp TRUE, subh "physiology" }}},
{ term "Transcription, Genetic" },
{ term "Translation, Genetic" }}
}, -- end Medline-entry
{
uid 88062986,
em std { year 1988, month 3 },
cit {
title {
name "Molecular cloning and characterization of cytoplasmic polyhedrosis virus
 polyhedrin and a viable deletion mutant gene." },
authors {
names ml {
"Arella M",
"Lavallee C",
"Belloncik S",
"Furuichi Y" },
affil str "Department of Virology, Institut Armand-Frappier, University of Que
bec, Montreal, Canada." },
from journal {
title  { ml-jta "J Virol" },
imp {
date std {
year 1988,
month 1
},
volume "62",
issue "1",
pages "211-7"} } -- end Cit-jour
}, -- end Cit-art
abstract "The double-stranded RNA genome of Bombyx mori cytoplasmic polyhedros
is virus (CPV) was converted to double-stranded DNA and cloned into plasmid pB
R322. The complete nucleotide sequence of cloned genome segment 10, which enco
des virus polyhedrin polypeptide, was determined. The CPV polyhedrin gene cons
ists of 942 based pairs and possesses a long open reading frame that codes for
 a polypeptide of 248 amino acids (molecular weight, 28,500), consistent with 
an apparent molecular weight of 28,000 previously determined for purified poly
hedrin. No sequence homology was found between CPV polyhedrin and polyhedrins 
from several nuclear polyhedrosis viruses. In addition to the polyhedrin gene,
 we completed the sequence analysis of a small deletion mutant gene derived fr
om the polyhedrin gene. This mutant gene consists of two subset domains of the
 polyhedrin gene, i.e., the 5'-terminal 121 base pairs and the 3'-terminal 200
 base pairs. An in vitro transcription demonstrated that the small mutant gene
 is transcribed by virion-associated RNA polymerases. These data confirm the i
mportance of CPV terminal sequences in virus genome replication.",
mesh {
{ term "Amino Acid Sequence" },
{ term "Base Sequence" },
{ term "Cloning, Molecular" },
{ term "DNA Mutational Analysis" },
{ term "Genes, Structural" },
{ term "Genes, Viral" },
{ term "In Vitro" },
{ term "Molecular Sequence Data" },
{ term "Polyhedrosis Viruses",
qual { { mp TRUE, subh "genetics" }}},
{ term "Protein Conformation" },
{ term "RNA, Viral",
qual { { subh "genetics" }}},
{ term "Transcription, Genetic" },
{ term "Viral Proteins",
qual { { mp TRUE, subh "genetics" }}}},
substance {
{ type nameonly, name "polyhedral protein" }},
xref {
{ type genbank, cit "M19112" }}
}, -- end Medline-entry
{
uid 88062990,
em std { year 1988, month 3 },
cit {
title {
name "Sigma 1 protein of mammalian reoviruses extends from the surfaces of vir
al particles." },
authors {
names ml {
"Furlong DB",
"Nibert ML",
"Fields BN" },
affil str "Department of Microbiology and Molecular Genetics, Harvard Medical 
School, Boston, Massachusetts." },
from journal {
title  { ml-jta "J Virol" },
imp {
date std {
year 1988,
month 1
},
volume "62",
issue "1",
pages "246-56"} } -- end Cit-jour
}, -- end Cit-art
abstract "Electron microscopy revealed structures consisting of long fibers to
pped with knobs extending from the surfaces of virions of mammalian reoviruses
. The morphology of these structures was reminiscent of the fiber protein of a
denovirus. Fibers were also seen extending from the reovirus top component and
 intermediate subviral particles but not from cores, suggesting that the fiber
s consist of either the mu 1C or sigma 1 outer capsid protein. Amino acid sequ
ence analysis predicts that the reovirus cell attachment protein sigma 1 conta
ins an extended fiber domain (R. Bassel-Duby, A. Jayasuriya, D. Chatterjee, N.
 Sonenberg, J. V. Maizell, Jr., and B. N. Fields, Nature [London] 315:421-423,
 1985). When sigma 1 protein was released from viral particles with mild heat 
and subsequently obtained in isolation, it was found to have a morphology iden
tical to that of the fiber structures seen extending from the viral particles.
 The identification of an extended form of sigma 1 has important implications 
for its function in cell attachment. Other evidence suggests that sigma 1 prot
ein may occur in virions in both an extended and an unextended state.",
mesh {
{ term "Amino Acid Sequence" },
{ term "Electrophoresis" },
{ term "Microscopy, Electron" },
{ term "Molecular Sequence Data" },
{ term "Peptide Hydrolases",
qual { { subh "diagnostic use" }}},
{ term "Receptors, Virus",
qual { { subh "physiology" }}},
{ term "Reoviridae",
qual { { mp TRUE, subh "ultrastructure" }}},
{ term "Support, Non-U.S. Gov't" },
{ term "Support, U.S. Gov't, Non-P.H.S." },
{ term "Support, U.S. Gov't, P.H.S." },
{ term "Viral Proteins",
qual { { mp TRUE, subh "physiology" }}},
{ term "Virion",
qual { { subh "ultrastructure" }}}},
substance {
{ type ec, cit "3.4.", name "Peptide Hydrolases" },
{ type nameonly, name "protein sigma 1" }},
idnum {
"2 P50 NS16998-07",
"5 R37 AI13178-12",
"5 T32 GM07753-08" }
}, -- end Medline-entry
{
uid 88062996,
em std { year 1988, month 3 },
cit {
title {
name "Molecular dissection of cis-acting regulatory elements from 5'-proximal 
regions of a vaccinia virus late gene cluster." },
authors {
names ml {
"Miner JN",
"Weinrich SL",
"Hruby DE" },
affil str "Department of Microbiology, Oregon State University, Corvallis 9733
1-3804." },
from journal {
title  { ml-jta "J Virol" },
imp {
date std {
year 1988,
month 1
},
volume "62",
issue "1",
pages "297-304"} } -- end Cit-jour
}, -- end Cit-art
abstract "Promoter elements responsible for directing the transcription of six
 tightly clustered vaccinia virus (VV) late genes (open reading frames [ORFs] 
D11, D12, D13, A1, A2, and A3) from the HindIII D/A region of the viral genome
 were identified within the upstream sequences proximal to each individual loc
us. These regions were identified as promoters by excising them from the VV ge
nome, abutting them to the bacterial chloramphenicol acetyl transferase gene, 
and demonstrating their ability to drive expression of the reporter gene in tr
ansient-expression assays in an orientation-specific manner. To delineate the 
5' boundary of the upstream elements, two of the VV late gene (A1 and D13) pro
moter: CAT constructs were subjected to deletion mutagenesis procedures. A ser
ies of 5' deletions of the ORF A1 promoter from -114 to -24 showed no reductio
n in promoter activity, whereas additional deletion of the sequences from -24 
to +2 resulted in the complete loss of activity. Deletion of the ORF A1 fragme
nt from -114 to -104 resulted in a 24% increase in activity, suggesting the pr
esence of a negative regulatory region. In marked contrast to previous 5' dele
tion analyses which have identified VV late promoters as 20- to 30-base-pair c
ap-proximal sequences, 5' deletions to define the upstream boundary of the ORF
 D13 promoter identified two positive regulatory regions, the first between -2
35 and -170 and the second between -123 and -106. Background levels of chloram
phenicol acetyltransferase expression were obtained with deletions past -88. S
ignificantly, this places the ORF D13 regulatory regions within the upstream c
oding sequences of the ORF A1. A high-stringency computer search for homologie
s between VV late promoters that have been thus far characterized was carried 
out. Several potential consensus sequences were found just upstream from RNA s
tart sites of temporally related promoter elements. Three major conclusions ar
e drawn from these experiments. (i) The presence of promoters preceding each l
ate ORF supports the hypothesis that each is expressed as an individual transc
riptional unit. (ii) Promoter elements can be located within the coding portio
n of the upstream gene. (iii) Sequence homologies between temporally related p
romoter elements support the notion of kinetic subclasses of late genes.",
mesh {
{ term "Base Sequence" },
{ term "DNA Mutational Analysis" },
{ mp TRUE, term "Genes, Viral" },
{ mp TRUE, term "Promoter Regions (Genetics)" },
{ mp TRUE, term "Regulatory Sequences, Nucleic Acid" },
{ term "Sequence Homology, Nucleic Acid" },
{ term "Support, U.S. Gov't, P.H.S." },
{ term "Vaccinia Virus",
qual { { mp TRUE, subh "genetics" }}}},
idnum {
"AI-20563",
"AI-0666",
"GM07774-07" }
}, -- end Medline-entry
{
uid 88063000,
em std { year 1988, month 3 },
cit {
title {
name "Identification and gene mapping of a 14,700-molecular-weight protein enc
oded by region E3 of group C adenoviruses." },
authors {
names ml {
"Tollefson AE",
"Wold WS" },
affil str "Institute for Molecular Virology, St. Louis University School of Me
dicine, Missouri 63110." },
from journal {
title  { ml-jta "J Virol" },
imp {
date std {
year 1988,
month 1
},
volume "62",
issue "1",
pages "33-9"} } -- end Cit-jour
}, -- end Cit-art
abstract "Early region E3 of adenovirus type 5 should encode at least nine pro
teins as judged by the DNA sequence and the spliced structures of the known mR
NAs. Only two E3 proteins have been proved to exist, a glycoprotein (gp19K) an
d an 11,600-molecular-weight protein (11.6K protein). Here we describe an abun
dant 14.7K protein coded by a gene in the extreme 3' portion of E3. To identif
y this 14.7K protein, we constructed a bacterial vector which synthesized a Tr
pE-14.7K fusion protein, then we prepared antiserum against the fusion protein
. This antiserum immunoprecipitated the 14.7K protein from cells infected with
 adenovirus types 5 and 2, as well as with a variety of E3 deletion mutants. S
ynthesis of the 14.7K protein correlated precisely with the presence or absenc
e of the 14.7K gene and with the synthesis of the mRNA (mRNA h) which encodes 
the 14.7K protein. The 14.7K protein appeared as a triplet on immunoprecipitat
ion gels and Western blots (immunoblots).",
mesh {
{ term "Adenoviruses, Human",
qual { { mp TRUE, subh "genetics" }}},
{ term "Amino Acid Sequence" },
{ term "Cloning, Molecular" },
{ mp TRUE, term "Genes, Viral" },
{ term "Immunologic Technics" },
{ term "Molecular Sequence Data" },
{ term "Molecular Weight" },
{ term "Recombinant Fusion Proteins",
qual { { subh "immunology" }}},
{ term "Support, U.S. Gov't, P.H.S." },
{ term "Viral Proteins",
qual { { mp TRUE, subh "genetics" }}}},
idnum {
"CA24710" }
}, -- end Medline-entry
{
uid 88063001,
em std { year 1988, month 3 },
cit {
title {
name "Four phosphoproteins with common amino termini are encoded by human cyto
megalovirus AD169." },
authors {
names ml {
"Wright DA",
"Staprans SI",
"Spector DH" },
affil str "Department of Biology, University of California, San Diego, La Joll
a 92093." },
from journal {
title  { ml-jta "J Virol" },
imp {
date std {
year 1988,
month 1
},
volume "62",
issue "1",
pages "331-40"} } -- end Cit-jour
}, -- end Cit-art
abstract "In this report, we identify the proteins encoded by the 2.2-kilobase
 class of early transcripts arising from a region of the strain AD169 human cy
tomegalovirus genome (map units 0.682 to 0.713) which contains cell-related se
quences. These transcripts, encoded by adjacent EcoRI fragments R and d, have 
a complex spliced structure with 5' and 3' coterminal ends. Antiserum directed
 against a synthetic 11-amino-acid peptide corresponding to the predicted amin
o terminus of the proteins was generated and found to immunoprecipitate four i
nfected-cell proteins of 84, 50, 43, and 34 kilodaltons. These proteins were p
hosphorylated and were associated predominantly with the nuclei of infected ce
lls. The 43-kilodalton protein was the most abundant of the four proteins, and
 its level of expression remained relatively constant throughout the infection
. Expression of the other proteins increased as the infection progressed. Puls
e-chase analysis failed to show a precursor-product relationship between any o
f the proteins. A comparison of the [35S]methionine-labeled tryptic peptide ma
ps of the four proteins from infected cells and an in vitro-generated polypept
ide derived from the putative first exon showed that all four infected-cell pr
oteins were of viral origin and contained a common amino-terminal region.",
mesh {
{ term "Amino Acid Sequence" },
{ term "Base Sequence" },
{ term "Cell Compartmentation" },
{ term "Cytomegaloviruses",
qual { { mp TRUE, subh "genetics" }}},
{ mp TRUE, term "Genes, Viral" },
{ term "Glycosylation" },
{ term "Immunologic Technics" },
{ term "Molecular Sequence Data" },
{ term "Molecular Weight" },
{ term "Peptide Mapping" },
{ term "Phosphoproteins",
qual { { mp TRUE, subh "genetics" }}},
{ term "Phosphorylation" },
{ term "Protein Precursors",
qual { { subh "metabolism" }}},
{ term "Protein Processing, Post-Translational" },
{ term "Support, U.S. Gov't, P.H.S." },
{ term "Trypsin" },
{ term "Viral Proteins",
qual { { mp TRUE, subh "genetics" }}}},
substance {
{ type ec, cit "3.4.21.4", name "Trypsin" }},
idnum {
"34729",
"GM07198",
"GM07240" }
}, -- end Medline-entry
{
uid 88063005,
em std { year 1988, month 3 },
cit {
title {
name "Quantitative basic residue requirements in the cleavage-activation site 
of the fusion glycoprotein as a determinant of virulence for Newcastle disease
 virus." },
authors {
names ml {
"Glickman RL",
"Syddall RJ",
"Iorio RM",
"Sheehan JP",
"Bratt MA" },
affil str "Department of Molecular Genetics and Microbiology, University of Ma
ssachusetts Medical School, Worcester 01605." },
from journal {
title  { ml-jta "J Virol" },
imp {
date std {
year 1988,
month 1
},
volume "62",
issue "1",
pages "354-6"} } -- end Cit-jour
}, -- end Cit-art
abstract "Newcastle disease virus exhibits a wide range of pathogenicity and v
irulence which, as with all paramyxoviruses, is directly related to the cleava
bility of a precursor (F0) of the fusion glycoprotein by cellular proteases. S
equence analyses of the cleavage site of several virulent and avirulent isolat
es of the Newcastle disease virus serotype reveal a correlation between virule
nce or pathogenicity and a high content of basic amino acid residues at the cl
eavage site. A similar correlation has been seen for other paramyxoviruses.",
mesh {
{ term "Amino Acid Sequence" },
{ term "Newcastle Disease Virus",
qual { { subh "metabolism" },
 { mp TRUE, subh "pathogenicity" }}},
{ term "Peptide Hydrolases",
qual { { subh "metabolism" }}},
{ term "Protein Precursors",
qual { { subh "metabolism" }}},
{ term "Structure-Activity Relationship" },
{ term "Support, U.S. Gov't, P.H.S." },
{ term "Viral Fusion Proteins",
qual { { mp TRUE, subh "metabolism" }}}},
substance {
{ type ec, cit "3.4.", name "Peptide Hydrolases" }},
idnum {
"AI-20762-03",
"AI-12467-11" }
}, -- end Medline-entry
{
uid 88063006,
em std { year 1988, month 3 },
cit {
title {
name "Identification of point mutations in the envelope gene of Moloney murine
 leukemia virus TB temperature-sensitive paralytogenic mutant ts1: molecular d
eterminants for neurovirulence." },
authors {
names ml {
"Szurek PF",
"Yuen PH",
"Jerzy R",
"Wong PK" },
affil str "University of Texas System Cancer Center, Science Park Research Div
ision, Smithville 78957." },
from journal {
title  { ml-jta "J Virol" },
imp {
date std {
year 1988,
month 1
},
volume "62",
issue "1",
pages "357-60"} } -- end Cit-jour
}, -- end Cit-art
abstract "ts1, a temperature-sensitive mutant of Moloney murine leukemia virus
 TB, induces hind-limb paralysis in mice. The DNA of both the ts1 and Moloney 
murine leukemia virus TB env genes has been sequenced, and the encoded amino a
cid sequences have been deduced from the DNA sequences. Four amino acids in th
e ts1 envelope protein have been identified which may be responsible for the t
s1 phenotype, which includes temperature sensitivity, nonprocessing of Pr80env
, and neurovirulence.",
mesh {
{ term "Amino Acid Sequence" },
{ term "Base Sequence" },
{ term "DNA Mutational Analysis" },
{ term "Moloney Leukemia Virus",
qual { { subh "genetics" },
 { mp TRUE, subh "pathogenicity" }}},
{ term "Nervous System Diseases",
qual { { mp TRUE, subh "microbiology" }}},
{ term "Structure-Activity Relationship" },
{ term "Support, U.S. Gov't, P.H.S." },
{ term "Temperature" },
{ term "Viral Envelope Proteins",
qual { { mp TRUE, subh "genetics" }}}},
idnum {
"CA 45124" }
}, -- end Medline-entry
{
uid 88063010,
em std { year 1988, month 3 },
cit {
title {
name "Organization of the transcriptional control region of the E1b gene of ad
enovirus type 5." },
authors {
names ml {
"Parks CL",
"Banerjee S",
"Spector DJ" },
affil str "Department of Microbiology, College of Medicine, Pennsylvania State
 University, Hershey 17033." },
from journal {
title  { ml-jta "J Virol" },
imp {
date std {
year 1988,
month 1
},
volume "62",
issue "1",
pages "54-67"} } -- end Cit-jour
}, -- end Cit-art
abstract "Genetic analysis of the transcriptional control sequences of the E1b
 gene of adenovirus type 5 identified two regions that stimulated specific tra
nscription by whole cell extracts from uninfected cells. The first region, loc
ated within 50 nucleotides (position -50) 5' to the transcription initiation (
cap) site, contains a G+C-rich consensus-binding site (GC box) for the transcr
iption factor Sp1 and a TATA box. Unambiguous stimulatory activity of the seco
nd region, between positions -358 and -127, was observed only in the absence o
f the GC box. DNase I protection experiments (footprinting) with crude nuclear
 extracts from uninfected cells revealed multiple DNA-protein interactions at 
the control region. Proximal to the initiation site, both the GC box and the c
ap site were protected; however, protection of the TATA box was not observed. 
In the distal region, four protein-binding sites, designated I through IV, wer
e located between positions -250 and -120. Three of the four mapped in protein
-coding sequences of the adjacent E1a gene. Sites I and II were 5' to position
 -218 whereas sites III and IV were 3' to position -218. This finding was cons
istent with results of the transcriptional analysis indicating that subsets of
 the distal region were sufficient for stimulation of transcription in vitro i
n the absence of the GC box. Within the boundaries of site I, a 10-base-pair p
rotected sequence was similar to one located 5' to the adenovirus E1a, E2a, E3
, E4, E2 late, and polypeptide IX transcription initiation sites. Sequences wi
thin the boundaries of the other three sites were similar to those within othe
r viral and cellular enhancers.",
mesh {
{ term "Adenoviruses, Human",
qual { { mp TRUE, subh "genetics" }}},
{ term "Base Sequence" },
{ term "Binding Sites" },
{ term "Deoxyribonuclease I",
qual { { subh "diagnostic use" }}},
{ term "DNA Mutational Analysis" },
{ term "DNA-Binding Proteins",
qual { { mp TRUE, subh "physiology" }}},
{ term "Gene Expression Regulation" },
{ mp TRUE, term "Genes, Viral" },
{ term "Molecular Sequence Data" },
{ term "Nuclear Proteins",
qual { { subh "physiology" }}},
{ term "Promoter Regions (Genetics)" },
{ mp TRUE, term "Regulatory Sequences, Nucleic Acid" },
{ term "RNA, Viral",
qual { { subh "genetics" }}},
{ term "Support, Non-U.S. Gov't" },
{ term "Support, U.S. Gov't, P.H.S." },
{ term "Transcription Factors",
qual { { mp TRUE, subh "physiology" }}},
{ mp TRUE, term "Transcription, Genetic" }},
substance {
{ type ec, cit "3.1.21.1", name "Deoxyribonuclease I" }},
idnum {
"CA 09124",
"CA 34381" }
}, -- end Medline-entry
{
uid 88063012,
em std { year 1988, month 3 },
cit {
title {
name "The avian retrovirus env gene family: molecular analysis of host range a
nd antigenic variants." },
authors {
names ml {
"Bova CA",
"Olsen JC",
"Swanstrom R" },
affil str "Department of Biochemistry, University of North Carolina, Chapel Hi
ll 27599." },
from journal {
title  { ml-jta "J Virol" },
imp {
date std {
year 1988,
month 1
},
volume "62",
issue "1",
pages "75-83"} } -- end Cit-jour
}, -- end Cit-art
abstract "The nucleotide sequence of the env gp85-coding domain from two avian
 sarcoma and leukosis retrovirus isolates was determined to identify host rang
e and antigenic determinants. The predicted amino acid sequence of gp85 from a
 subgroup D virus isolate of the Schmidt-Ruppin strain of Rous sarcoma virus w
as compared with the previously reported sequences of subgroup A, B, C, and E 
avian sarcoma and leukosis retroviruses. Subgroup D viruses are closely relate
d to the subgroup B viruses but have an extended host range that includes the 
ability to penetrate certain mammalian cells. There are 27 amino acid differen
ces shared between the subgroup D sequence and three subgroup B sequences. At 
16 of these sites, the subgroup D sequence is identical to the sequence of one
 or more of the other subgroup viruses (A, C, and E). The remaining 11 sites a
re specific to subgroup D and show some clustering in the two large variable r
egions that are thought to be major determinants of host range. Biological ana
lysis of recombinant viruses containing a dominant selectable marker confirmed
 the role of the gp85-coding domain in determining the host range of the subgr
oup D virus in the infection of mammalian cells. We also compared the sequence
 of the gp85-coding domain from two subgroup A viruses, Rous-associated virus 
type 1 and a subgroup A virus of the Schmidt-Ruppin strain of Rous sarcoma vir
us. The comparison revealed 24 nonconservative amino acid changes, of which 6 
result in changes in potential glycosylation sites. The positions of 10 amino 
acid differences are coincident with the positions of 10 differences found bet
ween two subgroup B virus env gene sequences. These 10 sites identify seven do
mains in the sequence which may constitute determinants of type-specific antig
enicity. Using a molecular recombinant, we demonstrated that type-specific neu
tralization of two subgroup A viruses was associated with the gp85-coding doma
in of the virus.",
mesh {
{ term "Amino Acid Sequence" },
{ term "Animal" },
{ term "Antigenic Variation" },
{ term "Antigens, Surface",
qual { { subh "genetics" }}},
{ term "Antigens, Viral",
qual { { mp TRUE, subh "genetics" }}},
{ term "Avian Leukosis-Sarcoma Viruses",
qual { { mp TRUE, subh "genetics" }}},
{ term "Base Sequence" },
{ term "Chickens",
qual { { subh "microbiology" }}},
{ term "Genes, Viral" },
{ term "Mammals",
qual { { subh "microbiology" }}},
{ term "Molecular Sequence Data" },
{ term "Neutralization Tests" },
{ term "Receptors, Virus",
qual { { subh "physiology" }}},
{ term "Recombination, Genetic" },
{ term "Species Specificity" },
{ term "Support, Non-U.S. Gov't" },
{ term "Support, U.S. Gov't, P.H.S." },
{ term "Viral Envelope Proteins",
qual { { mp TRUE, subh "genetics" },
 { subh "immunology" }}},
{ term "Virus Replication" }},
xref {
{ type genbank, cit "M19113" },
{ type genbank, cit "M22730" }},
idnum {
"RO1 CA33147",
"U41 RR-01685" }
} -- end Medline-entry
} -- end Pub-set