bluuebunny/crossref_metadata_2025_split huggingface dataset:
VMA6
Authors: Bauerle B M , Stevens T H 
Published: November 2023

Abstract
The VMA6 gene was cloned using a reverse genetic strategy. Peptide sequence data from tryptic fragments of gel purified 36 kDa polypeptide was used to design corresponding “sense” and “antisense” oligonucleotides. Pairs of degenerate oligonucleotides were used as primers to amplify sequences from yeast genomic DNA by PCR, and the PCR fragment was used to obtain the intact VMA6 gene. The DNA sequence of VMA6 (GenBank accession # L11584) contains an open reading frame that is predicted to encode a polypeptide of 345 amino acids with a molecular mass of 39.8 kDa. All five of the originally determined internal peptide sequences of the 36 kDa polypeptide were found within the open reading frame. The predicted polypeptide is hydrophilic overall, with many acidic charged residues dispersed throughout the sequence.
CHG1
Authors: Payne H S , Lemmon S K 
Published: November 2023

Abstract
Depending on the genetic background, deletions of CHC1 may result in slow-growing viable haploid cells or inviable haploid cells (see Genetic interaction section below)1·4. Viable mutants grow at rates roughly 2-6 times slower than wild-type cells. chc1-!l cells display genetic instability that can result from increases in genome copy number2A. In cultures of chc1-!l strains, cells with multiple nuclei can be present at levels approaching 1% of the population.
END3,END4
Authors: Raths S , Reizman- H 
Published: November 2023

Abstract
The mutant, end3, was identified by screening an ethylmethanesulfonate (EMS) mutagenized bank of Saccharomyces cerevisiae for strains that bind but fail to internalize 35S-a-factor. This mutation is recessive and renders cells unable to grow at temperatures of 37°C. end3 strains, however, can bind but not internalize a-factor at permissive (24°C) and restrictive temperatures (37°(). Lucifer yellow, a fluid phase endocytic marker, is also not accumulated in the vacuole of end3 mutants at either temperature. Other vesicle-mediated processes seem to be normal in end3 as invertase secretion and carboxypeptidase Y maturation proceed unimpaired. The end3 gene was cloned by complementation of the temperature-sensitive growth defect of the end3 mutant.
Clathrin-associated protein complexes (APs)
Authors: Kirchhausen T 
Published: November 2023

Abstract
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Clathrin-associated proteins are also referred to as assem bly proteins and adaptors. The term “associated proteins” is a general term used to indicate that their in vivo function is still not completely understood. “Assembly proteins” refers to the in vitro property that under physiological ionic conditions APs interact with clathrin and assemble with it into small coats1 The term “adaptor”2 was introduced to indicate that a possible role of the APs is to interact with clathrin and with the cytoplasmic tails of some membrane proteins, leading to their selection and concentration into coated pits and coated vesicles2,3.
End3
Authors: Draper R K 
Published: November 2023

Abstract
This complementation group contains one mutant, termed G.7.1, isolated by exposing mutagenized Chinese hamster ovary cells to both diphtheria toxin and the plant toxin modeccin1. At the restrictive temperature, G.7.1 cells are defective in endosomal, but not lysosomal, acidification13. The acidification of endosomes prepared from mutant cells harvested at the permissive temperature is hypersensitive to thermal inactivation in vitro, demonstrating that a thermosensitive component is a resident of vesicles from the mutant cells. Coated vesicle preparations made from G.7.1 cells grown at the permissive temperature have a thermolabile acidification activity and a thermolabile proton-translocating ATPase activity.
End4
Authors: Draper R K 
Published: November 2023

Abstract
This complementation group was originally defined in genetic studies with mutant V.24.1, isolated by exposing Chinese hamster ovary cells to diphtheria toxin1 Two other Chinese hamster ovary cell mutants, DS28-6 and HRP-1, have recently been added to the group by complementation analysis2. DS28-6 was isolated by Nakano et al. using a replica-plating technique to rescue temperaturesensitive mutants defective in secretion3 HRP-1 was isolated by Wang et al. using a new procedure to obtain mutants defective in fluid-phase endocytosis2.
Rab4
Authors: Mellman I 
Published: November 2023

Abstract
Rab4 was first localized to early endosomes by screening subcellular fractions prepared from CHO cells using the original panel of polyclonal anti-rab antibodies prepared by Bruno Goud3 Free-flow electrophoresis fractions were analyzed by immunoblotting, and only antibody to rab4 was found to yield a clear signal in the anodally-shifted fractions that co-migrated with transferrin receptor. This localization was confirmed by immunofluorescence performed on cells (Hela, CHO) stably or transiently transfected with wild type rab4a cDNAs. lmmunoelectron microscopy (immuno-EM) on frozen thin sections is also consistent with an early endosome/recycling vesicle localization4; very little rab4 is detectable on the plasma membrane. Since rab5 has also been localized by immunofluorescence, cell fractionation, and immune-EM to early endocytic compartments (see rab5 entry, p. 295), it has been presumed that rab4 and rab5 are themselves co-localized.
Bet2p
Authors: Ferro-Novick Susan 
Published: November 2023

Abstract
The DNA sequence of BET2 predicts a hydrophilic protein of-36 500 daltons (Peterson-Bjorn et al. 1990; Rossi et al. 1991). Antibody raised to this protein has confirmed this prediction (Jiang et al. 1993). Bet2 shares 56.6% similarity and 34% identity with Dpr1 (Ram1), an essential component of a protein prenyltransferase that adds farnesyl (a 15 carbon lipid) to the COCH-terminus of Ras and the yeast mating pheromone afactor (Schafer et al. 1990; Goodman et al. 1990; He et al. 1991).8ET2wasalsofoundto be the same as ORF2, an essential yeast gene of unknown function (Peterson-Bjorn et al. 1990; Rossi et al. 1991). The DNA sequences of BET2 andORF2 are identical with one exception that results in a conserved amino acid change (asparagine in Orf2 and lysine in Bet2 at position 22) in the protein. This change may be attributable to differences in strain backgrounds.
Dras2
Authors: III John G Bishop , Corces Victor G 
Published: November 2023

Abstract
Dras2 was identified by cross-homology with the Harvey murine sarcoma virus (Neuman-Silbergerg et al. 1984; Mozer et al. 1985). It maps to chromosomal subdivision 64B on Drosophila polytene chromosomes. The nucleotide sequence of Dras2 is shown in Fig. 1. This sequence differs from that reported initially from sequence analysis of genomic clones (Neuman-Silberberg etal. 1984; Mozer et al. 1985), and was obtained by sequencing full-length cDNA clones (Bishop and Corces 1988). The nucleotide sequence of Dras2 is deposited in the GenBank database with accession numbers M10759 and M10803; the sequence of the promoter region is under accession number X12558, and the updated sequence of the exon2/exon3 borders is under X12559.
Sevenless
Authors: Mlodzik Marek 
Published: November 2023

Abstract
The rescue fragment contains a single 8.2-kb transcript (Hafen et al. 1987). The complete nucleotide sequence of the 12 kb rescue fragment has been determined (Basler and Hafen 1988; Bowtell et al. 1988). The GenBank accession numbers are J03158 and Y00218, respectively.ProteinIn comparison to other known tyrosine kinases, the sev gene product is unique in size and structure. The nucleotide sequence predicts a protein of 2554 amino acids with two transmembrane segments (Basler and Hafen 1988; Bowtell et al. 1988).
Dm Gapl
Authors: Gaul Ulrike 
Published: November 2023

Abstract
Mutations in Gap1 have been obtained by P enhancer trap insertion and chemical mutagenesis (Buckles et al. 1992; Gaul etal. 1992; Rogge etal. 1992). Gap1 was identified by screening cDNA libraries using genomic sequences flanking the P insertion (Gaul et al. 1992). The P enhancer trap is inserted into the open reading frame (ORF) of the Gap1 transcript, which is the cause of its mutagenicity. The DNA sequence of Drosophila Gap1 (Gaul etal. 1992) is shown in Fig. 1. The GenBank accession number is M86655.
Bcl2
Authors: Bischoff James R , Fernandez-Sarabia Maria Jose 
Published: November 2023

Abstract
Probes for the IgH locus were used to clone t(14; 18) breakpoint DNAs. These DNAs allowed the identification of a transcriptional unit on chromosome 18, which was named bc!2. The bcl2 gene is transcribed by alternative splicing into three mRNAs of different sizes. bcl2 contains two exons and encodes two proteins that only differ at their C-terminal regions (Tsujimoto and Croce 1986). The open reading frame of the human bcl2 gene and its amino acid sequence is shown in Fig. 1. The accession number for the genomic sequence is M13994.
Rsr lp
Authors: Bender Alan , Pringle John R 
Published: November 2023

Abstract
RSR1 was identified both as a multicopy suppressor of a cdc24ts mutation (Bender and Pringle 1989) and on the basis of a mutation (bud1) that randomized bud position (Chant and Herskowitz 1991). Its nucleotide and predicted amino acid sequences (Bender and Pringle 1989; GenBank accession number M26928) are shown in Fig. 1.
Rho2p
Authors: Madaule Pascal , Myers Alan 
Published: November 2023

Abstract
The RHO2 gene was identified by a low stringency screen of a Saccharomyces cerevisiae genomic library, using as a probe a Rho cDNA from Aplysia californica (Madaule and Axel 1985; Madaule et al. 1987). RHO2 is not an essential gene. GenBank accession number is M15190.
Cdc24p
Authors: Bender Alan , Pringle John R 
Published: November 2023

Abstract
CDC24 was identified both during a screen for temperature-sensitive (Ts_) cell-division-cycle mutants that fail to initiate bud emergence but can initiate the nuclear-division cycle (Hartwell et al. 1973, 1974) and during a screen for mutants that are sensitive to high levels of Ca2+ in the medium (Ohya etal. 1986a, b). Its nucleotide and predicted amino acid sequences (Miyamoto et al. 1987, 1991; GenBank accession number M16809) are shown in Fig. 1.
Rab proteins
Authors: Zerial Marino 
Published: November 2023

Abstract
The intracellular localization of Rab proteins has provided a first clue into their function. Rab proteins are present in two intracellular pools, one minor, cytosolic, and another major, membrane-bound. A characteristic feature of the members of this subfamily is their intracellular compartmentalization. A number of organelles of the exocytic and endocytic transport pathways contain a characteristic set of membrane-associated Rab proteins. Figure 1 and Table 1 summarise the subcellular localization of these proteins. This distribution is consistent with a function of Rab proteins in distinct intracellular transport processes.
RabSc
Authors: Kikuchi Akira , Takai Yoshimi 
Published: November 2023

Abstract
Bovine Rab3c cDNA was isolated from a bovine brain cDNA library using oligonucleotide probes of Rab3a (Matsui etal. 1988). The nucleotide sequence of bovine Rab3c and its deduced amino acid sequence are shown in Fig. 1. The GenBank accession number is J03943.
Ypt52p
Authors: Singer-Kruger Birgit 
Published: November 2023

Abstract
Sequence analysis of chromosome XI of S. cerevisiae in the yeast genome sequence project of the European community led to the identification of a small GTPase that contained 55%/70% sequence identity/homology to Rab5a, and 54%/71% and 51%/66% identity/homology to Ypt51p and Ypt53p, respectively (Singer-Kruger et al. 1994). Due to the close phylogenetic relationship of these proteins and their functional similarities, this gene was named YPT52 and its gene product Ypt52p (Fig. 1).
Gdilp/Secl9p
Authors: Garrett Michelle D , Novick Peter 
Published: November 2023

Abstract
Complementation and linkage analysis indicates that GDI1 is allelic to sec19-1, a temperature-sensitive, conditionally lethal mutant isolated by a density enrichment protocol (Novick et al. 1980; Garrett et al. 1994). At the restrictive temperature of 37C, the sec19-1 cells are blocked for the transport of invertase and acid phosphatase; they accumulate the p1 form of the vacuolar protease carboxypeptidase Y, and are defective for the uptake of the fluid phase marker, Lucifer yellow (Novick et al. 1980; Stevens et al.
Yptl (Schizosaccharomyces pombe)
Authors: Armstrong John 
Published: November 2023

Abstract
The ypt1 gene was isolated fortuitously by hybridizing a S. pombe genomic library with a probe from the sec4 gene of 5. cerevisiae (Fawell et al. 1989) and independently with a ypt3 probe (Miyake and Yamamoto 1990). The sequence, including four introns, is given in Fig. 1(A). Note that, due to the presence of an unusual splice junction, the extreme N-terminus was originally assigned incorrectly. The correct splice pattern was determined by Northern blotting (Miyakeand Yamamoto 1990) and polymerase chain reaction (PCR) of cDNA (Newman etal. 1992). The EMBL accession numbers are X15082, X52099.
Ran/TC4
Authors: Bischoff F Ralf , Coutavas Elias , Ponstingl Peter D’Eustachio. Herwig , Ren Mindong , Rush Mark 
Published: November 2023

Abstract
Ran/TC4 was originally identified by screening a human teratocarcinoma cDNA library with degenerate oligonucleotides based on the conserved DTAGQE sequence of Ras family members (Drivas etal. 1990). The DNA sequence of Ran/TC4 (Ren et al. 1993) and its predicted open reading frame are shown in Fig. 1 (GenBank accession number M31469). To date, the coding sequences for several other Ran subfamily members have been identified in mouse (Coutavas et al. 1994),
Interleukin-4 (IL-4)
Authors: Howard M , Harada N 
Published: November 2023

Abstract
The nucleotide sequences of IL-4 cDNAs cloned from mouse and man (GenBank accession numbers M13238 and M13982) predict a protein of 153 (human) or 140 (mouse) amino acids, each containing a 20-amino-acid leader sequence (Lee et al. 1986; Noma et al. 1986; Yokota et al. 1986). These proteins are approximately 50 per cent homologous at the amino acid level, and there is no cross-reaction either biologically or at the receptor level between the two species of cytokine.
Interleukin-6 (IL-6)
Authors: Narazaki M , Kishimoto T 
Published: November 2023

Abstract
B cell stimulatory factor 2 (BSF-2), B cell differentiation factor (BCDF), interferon-P2 (IFN/J2), 26-kDa protein, hybridoma growth factor (HGF), hepatocyte-stimulating factor (HSF). Human IL-6 consists of 212 amino acids including a 28 amino acid signal peptide (Hirano et al. 1986) (GenBank accession number X04602), whereas mouse and rat IL-6 consist of 211 amino acids with a 24-amino-acid signal peptide (Van Snick et al. 1988; Northemann et al. 1989) (GenBank accession number X06203 for mouse IL-6, M26744 for rat IL-6). Comparison ofthe amino acid sequence of human IL-6 with that of mouse IL-6 shows a homology of only 42 per cent, although the mouse and rat protein sequence are 93 per cent identical. Human IL-6 acts on murine cells with the same biological activity as mouse IL-6, but not vice versa. The central portion of IL-6 is more conserved (57 per cent for the region spanning residues 42-102) and contains the four cysteine residues of the protein in perfect alignment.
Receptors for Interleukin-8 (IL-8)
Authors: Horuk R 
Published: November 2023

Abstract
Recently, cDNA clones encoding two human IL-8 receptors were isolated and characterized (Holmes et al. 1991; Murphy and Tiffany 1991). One receptor, termed the IL-BRA, was isolated (Holmes et al. 1991) from a human neutrophil cDNA library by expression cloning, using binding to 1251-IL-8 as the method of detection. The IL-8RA is a 350-aminoacid protein (GenBank accession number M68932) with five potential N-linked glycosylation sites and seven hydrophobic membrane-spanning stretches characteristic of the G-protein-linked family of molecules (Strosberg 1991). The receptor is glycosylated since the translated molecular size of the receptor is around 40 kDa, which is considerably smaller than the reported size of 55 to 69 kDa based on cross-linking oft he neutrophil receptor (Holmes et al. 1991; Samanta et al. 1989).
Tumour Necrosis Factor Receptor
Authors: Aggarwal B B , Reddy S 
Published: November 2023

Abstract
The p80 form of the TNF receptor contains 461 amino acid residues consisting of an extracellular domain (ECD), a single transmembrane domain, and a cytoplasmic domain of 235, 30, and 174 amino acid residues, respectively. In contrast, the p60 form of the TNF receptor contains 455 amino acid residues consisting of extracellular, transmembrane, and cytoplasmic domains of 182, 21, and 223 amino acid residues, respectively. The ECD of the p80 receptor has two potential N-linked and several O-linked glycosylation sites, whereas the p60 receptor has only three N-linked sites. The ECD of the p60 and p80 receptors have 24 and 22 cysteine residues, respectively, organized into four cysteine-rich domains. The theoretical molecular masses of p60 and p80 receptor protein are 47 526 and 46 000 Da, respectively. Both receptors have one net positive charge. The ECD of both are highly susceptible to cleavage by proteases activated by kinases and phosphatase inhibitors. The soluble form of both the p60 and p80 receptors, consisting primarily of the ECD, has been detected in cell-conditioned media, urine, serum, amniotic fluids, and synovial fluids.
Receptors for Leukaemia Inhibitory Factor (LIF) and Oncostatin M (OSM)
Authors: Gearing D P 
Published: November 2023

Abstract
The a-subunit of the human LIF receptor is produced as a 1097 amino acid precursor with a predicted 44-amino-acid leader sequence (Gearing et al. 1991). There is a single predicted transmembrane segment of 26 amino acids, an extracellular domain of 789 amino acids and a relatively long cytoplasmic domain of 238 amino acids. The predicted molecular weight of the protein is 111 000 Da but the observed molecular weight on 5D5-PAGE gels is 200000 Da due to extensive N-glycosylation at several of the predicted20 N-glycosylation sites. Distal to the transmembrane region the extracellular region comprises two haemapoietin receptor domains separated by an immunoglobulin-like domain and three membrane-proximal fibronectin type Ill domains.
Neu Differentiation Factor (NDF) and the Neuregulin (NRG) Family
Authors: Yarden Y , Wen D 
Published: November 2023

Abstract
The heat-stable rodent factor and its human homologue (named HRG) are secreted proteins that were purified by heparin-chromatography from the media conditioned by cancer cells (Peles et al. 1992; Holmes et al. 1992). NDF is sensitive to reduction but resists extremes of pH. N- and O-linked sugars account for approximately one-quarter of the mass of the mature 44 kDa glycoprotein, but they are not required for receptor recognition.
Neu/ErbB-2 Receptor
Authors: Yarden Y , Levy R B 
Published: November 2023

Abstract
The rodent 185 kD glycoprotein consists of 1260 amino acids (Bargmann et a/. 1986) (GenBank accession number X03662), whereas the human protein is 1255 amino acids long (Coussens eta/. 1985; Yamamoto et al. 1986) (GenBank accession number M11730). An insect homologue of neu has been identified in Drosophila melanogaster (Livneh et al. 1985). The protein is bisected by a single hydrophobic stretch that functions as a transmembrane domain and separates the extracellular ligand-binding portion from the cytoplasm-facing tyrosine kinase domain (Fig. 1). Neu is related in its molecular architecture and amino acid sequence to three other receptor tyrosine kinases. These are the receptor for EGF, erbB-3/HER3 (Kraus et al. 1989; Plowman et al. 1990) and erbB-4/HER-4 (Plowman et al. 1993).
Receptors for Granulocyte-Macrophage Colony-Stimulating Factor (GM-CSF)
Authors: Nicola N A 
Published: November 2023

Abstract
The a-chain of the human GM-CSF receptor is produced as a 400-amino-acid precursor with a predicted 22-amino-acid leader sequence (GenBank accession numbers M73832 and M64445} (Fig. 1}. There is a single predicted transmembrane segment of 26 amino acids, an extracellular domain of 298 amino acids and a short cytoplasmic domain of 54 amino acids. The predicted molecular weight of the protein is 44000 but the observed molecular weight on SDS-PAGE gels is 75 000-85000 due to N-glycosylation at several of the predicted eleven N-glycosylation sites (Gearing et al. 1989}. The 200 amino acids proximal to the transmembrane region (on the extracellular side) form a haemopoietin receptor domain that is presumed to bind GM-CSF and which is homologous in many cytokine receptors (see Introductory chapters).
Hepatocyte Growth Factor
Authors: Comoglio P M , Graziani A 
Published: November 2023

Abstract
Scatter factor (SF), human lung fibroblast-derived mitogen, hepatopoietin A, hepatotrophin, tumour cytotoxic factor. HGF is a disulphide-linked heterodimer of a heavy (a) subunit of 60 kDa and a light (/J) subunit of 32 or 36 kDa, originating from proteolytic cleavage of a single 92 kDa precursor (Fig. 1) (Miyazawa et al. 1989; Nakamura et al. 1989; Weidner et al. 1991; Rubin et al. 1991).
Growth Hormone/Prolactin Receptors
Authors: Clackson T 
Published: November 2023

Abstract
The mature human GH receptor cloned from liver comprises 620 amino acids (aa) and is expressed with a signal sequence of 18 aa (GenBank accession number X06562). A 246-aa extracellular domain containing seven cysteine residues is followed by a transmembrane domain of 24 residues and a 350-aa intracellular domain. The extracellular domain (residues 1-238) is found in serum as a GH-binding protein (hGHbp) (Leung et al. 1987). In rodents the soluble binding protein bears a short (17 or 27 aa) (-terminal extension not present in the membrane receptor (Mathews 1991; Kelly et al. 1993).
Platelet-derived Growth Factor (PDGF)
Authors: Heldin C -H , Westermark B 
Published: November 2023

Abstract
cDNAs for human PDGF A-chain (Betsholtz et al. 1986) and B-chain (Josephs et al. 1984) have been cloned (GenBank accession numbers X03795 and M12782, respectively). The PDGFA-chains have also been cloned from mouse (Rorsman et al. 1992) and Xenopus (Mercola et al. 1988) and the B-chain from mouse (Bonthron eta/. 1991) and cat (Van den Ouweland et al. 1987); the conservation of the sequences between different species is very high. The human B-chain sequence predicts a 241-amino-acid polypeptide including a 20-amino-acid long leader sequence (Fig. 1). The A-chain occurs in two forms as a result of differential splicing.
Receptors for Platelet-derived Growth Factor (PDGF)
Authors: Heldin C -H , Claesson-Welsh L 
Published: November 2023

Abstract
The human a-receptor has 1089 amino acids including a 23-amino-acid leader sequence (GenBank accession number M22734 and M21574}, and the p-receptor has 1106 amino acids including a 32-amino-acid leader (GenBank accession number M21616 and JO3278) (Fig. 1). The mouse a-and p-receptors have also been cloned (GenBank accession numbers 540407 and X04367, respectively). The predicted molecular weight of the human a-receptor is 120 000 and of the /I-receptor 121 000; however, the receptors run as components of apparent molecular weights 170000 and 180000 in SDS-gel electrophoresis, respectively, due to glycosylation and other post-translational modifications. Each receptor has five immunoglobulin-like domains in the extracellular part; the amino acid sequence similarity between the receptors is 30 per cent in this region.
Three-dimensional strudure of Hsc70
Authors: Wilbanks S 
Published: November 2023

Abstract
The X-ray crystal structure of the isolated ATPase domain (residues 1-384) of bovine Hsc70 (Swiss Protein Accession # Hs7c_Bovin) has been solved (Flaherty et al., 1990). The secondary structural elements of a recombinant peptide binding fragment (residues 385-543) of rat Hsc70 (Swiss Protein Accession # Hs7c_Rat).