bluuebunny/crossref_metadata_2025_split huggingface dataset:
Rab5b and Rab5c
Authors: Bucci Cecilia , Liitcke Anne , Dupree Paul , Zerial Marino 
Published: November 2023

Abstract
Rab5b and Rab5c were identified by Chavrier etal. (1992), using a PCR approach to amplify Rab proteins from embryonic day 17 mouse kidney cDNA. The two oligonucleotides used corresponded to the GXXXXGKS/T and to the WDTAGQE conserved regions. Using modified RACE protocols (Frohman et al. 1988; Walker et al. 1992), cDNA clones encoding Rab5b and Rab5c from mouse kidney RNA were identified. Rab5b was also independently cloned from a human endothelial cDNA library (Wilson and Wilson 1992).
Rabll
Authors: Urbe Sylvie , Parton Robert G 
Published: November 2023

Abstract
Rab11 was identified by screening a Madin-Darby canine kidney (MDCK)-cell cDNA library (Chavrier eta/. 1990) using degenerate oligonucleotides corresponding to the sequence WDTAGQE shared by members of the Ypt1/Sec4/Rab subfamily (Valencia et al. 1991). A human homologue termed YL8 (Drivas and Rush 1991) was cloned from two human cDNA libraries by a polymerase chain reaction (PCR)-approach based on oligonucleotide primer pairs specific to the four highly-conserved coding domains of the ras genes. Furthermore, a PCR approach based on oligonucleotides derived from the amino acid sequences of a rat homologue referred to as 24K G has led to the cloning of a homologous gene from a rat liver cDNA library (Sakurada etal. 1991).
Rabl6
Authors: Elferink Lisa A , Schellers Richard H 
Published: November 2023

Abstract
Rab16 was originally identified from a rat brain cDNA library, during a screen for GTPases involved in membrane trafficking and regulated secretion (Elferink et al. 1992). The nucleotide and deduced amino acid sequence of Rab16 is presented in Fig. 1. The GenBank accession number is M83681.
Rabl8
Authors: Lutcke Anne , Zerial Marino 
Published: November 2023

Abstract
Like Rab17 and Rab20, the Rab18 cDNA was isolated from an embryonic day 17 mouse kidney cDNA library using a polymerase chain reaction (PCR) fragment identified by Chavrier et al. (1992) as a probe. As expected from the size of the mRNA on Northern blots (-2.4 kb), the longest clone obtained (∼1.9 kb) was still lacking the first four nucleotides from the 5’-end. As these nucleotides were contained within the partial clone isolated by Chavrier et al. (1992), a full-length clone was constructed by PCR. The nucleotide and deduced amino acid sequences are shown in Fig. 1 and can be obtained from the EMBL/GenBank/DDB under the accession number X80333.
Rab19
Authors: Liitcke Anne , Zerial Marino 
Published: November 2023

Abstract
A 1.1 -kb cDNA clone spanning the region from the 5’-end of the Rabi 9 coding region to the poly A tail was obtained by 3’RACE (Frohman etal. 1988; Walker etal. 1992) based on a PCR fragment identified by Chavrier etal. (1992). The nucleotide and deduced amino acid sequences of Rab19 are shown in Fig. 1 and can be obtained from the EMBL/GenBank/DDB under the accession number X80473. By Northern blot, a corresponding mRNA of ∼1.6 kb could be detected in a subset of mouse tissues (Fig. 2) Lutcke etal. (1995).
Rab20
Authors: Lutcke Anne , Zerial Marino 
Published: November 2023

Abstract
Like Rab17 and Rab18, the Rab20 cDNA was isolated from an embryonic day 17 mouse kidney cDNA library using a polymerase chain reaction (PCR) fragment identified by Chavrier et al. (1992) as a probe. One ∼1.4-kb full-length clone was identified lacking a minor portion from the 5’ untranslated region of the corresponding mRNA (-1.6 kb). The nucleotide and deduced amino acid sequences are shown in Fig. 1 and can be obtained from the EMBL/GenBank/DDB under the accession number X80332.
Rab24
Authors: Olkkonen Vesa M 
Published: November 2023

Abstract
The sequence was first identified in the PCR study of Chavrier et al. (1992). Here, Rab/Rho-related sequences were amplified from adult mouse kidney cDNA using degenerated oligonucleotides corresponding to two of the conserved sequence stretches of Rab/Rho GTPases as primers. The PCR-Rab16 fragment containing the 5’-end of the open reading frame (ORF) was used for designing gene-specific primers, with which the sequence was extended to the 3’-direction with the 3’-RACE PCR technique (Frohman et al. 1988; Walker et al. 1992).
Rab25
Authors: Goldenring James R 
Published: November 2023

Abstract
The Rab25 nucelotide sequence was identified initially through amplification of carboxy-terminal sequences of rabbit parietal cell small GTP-binding proteins using a 3’-rapid amplification of cDNA ends (3’RACE) protocol based on a degenerate oligonucleotide synthesized for the WDTAGQE motif (Goldenring et al. 1993). The complete Rab25 sequence wasobtained with 5’-RACE (Fig. 1; GenBank accession number L03303).
Rab-GDI2
Authors: Shisheva Assia , Czech Michael P 
Published: November 2023

Abstract
A full-length mouse GDI2 cDNA was isolated by screening a mouse skeletal muscle cDNA library with the full-length rat brain GDI1 cDNA (Shisheva et al. 1994). A cDNA clone found to be the mouse homolog of the previously reported bovine brain smg p25A-GDI (Matsui et al. 1990) and rat brain GDI1 (Shisheva etal. 1994) was also isolated from the mouse skeletal muscle library and is denoted mGDI1 (Shisheva et al. 1994). The DNA sequence of mGDI2 is presented in Fig. 1. The GenBank accession number is UO7951.
Yptlp (Saccharomyces cerevisiae)
Authors: Gallwitz Dieter 
Published: November 2023

Abstract
The YPT1 gene was originally discovered in the course of analyzing the actin gene (ACT1) and its chromosomal surroundings (Gallwitz and Seidel 1980). The gene, provisionally called YP2 (Gallwitz etal. 1983) and later renamed YPT1 (Schmitt et al. 1986), is located on the short arm of chromosome VI between the p-tubulin gene (TUB2) and ACT1. YPT1 and TUB2 are bidirectionally transcribed and separated by an Abf1/Baf1-binding DNA segment (Halfter et al. 1989). The DNA sequence of YPT1 (Gallwitz et al. 1983) is shown in Fig. 1. The GenBank accession number is X00209.
Ypt51p
Authors: Singer-Kruger Birgit 
Published: November 2023

Abstract
S. cerevisiae YPT51 (Fig. 1) was identified by a polymerase chain reaction (PCR) approach in a search for putative yeast homolog(s) of mammalian Rab5 proteins (Singer-Kruger et al. 1994). Two degenerated oligonucleotides were used, corresponding to the sequences GXXXXGKS/T and LAPMYYR. The first sequence resembles a motif of the phosphate-binding loop of all Rab/Ypt proteins (Chavrier etal. 1992), whereas the latter is located within the helix 2 and was found to contribute to the functional specificity of Rab5a (Stenmark et al. 1994).
Sly2p/Sec22p
Authors: Schmitt Hans Dieter , Dascher Christiane , Gallwitz Dieter 
Published: November 2023

Abstract
The SLY2/SEC22 gene of S. cerevisiae was isolated as a fragment of genomic yeast DNA that could suppress the deletion of YPT1 in a dosage-dependent manner (Dascher et al. 1991). The coding sequence is not interrupted by an intron. The EMBL accession number is X54236.
Bos1p
Authors: Ferro-Novick Susan 
Published: November 2023

Abstract
DNA sequence analysis predicts that the BOS1 gene contains a putative 88-bp intron with conserved 5’ and 3’ sequences for RNA splicing (Shim et al. 1991). The Bos1 protein (244 amino acids) is hydrophilic at its amino-termi- nus with a hydrophobic stretch of 18 amino acids near its carboxy-terminus. This hydrophobic domain may serve as a membrane anchor. BOS1 is 27% identical and 52% similar to SNC1, a gene whose product is 40% identical to synap- tobrevin (Gerst etal. 1992). SNC1 is required for post-Golgi secretion in yeast (Protopopov et al. 1993). The GenBank accession number is X57792.
Ryh1
Authors: Hengst Ludger , Gallwitz Dieter 
Published: November 2023

Abstract
ryh1 was identified and cloned using a protein-coding fragment of the S. cerevisiae YPT1 gene (Gallwitz etal. 1983) as hybridization probe (Hengst et al. 1990). The proteincoding part of ryh 1 is interrupted by three short introns. The ryh 1 gene has been mapped to the left arm of chromosome I, approximately 20 cM from ade3. (Miyake et al. 1991).The DNA sequence ofthegene is shown in Fig. I.The GenBank accession number is X52475.
Arf3
Authors: Kahn Richard A 
Published: November 2023

Abstract
ARF3 cDNA (accession number P16587) was cloned from a human cerebellum cDNA library using bovine ARF2 cDNA as probe (Bobak etal. 1989). The message size is about 3.7 kb with a weaker hybridizing signal detected at about 1.2 kb.
Arf5
Authors: Kahn Richard A 
Published: November 2023

Abstract
The ARF5cDNA (accession number P26437) was cloned from a human HL-60 cell lamdba ZAP library by cross-species hybridization with a bovine ARF2 probe. A message size of about 1300 bp is consistently detected in a number of differ- enttissues and species examined (Tsuchiya etal. 1991).
ArL1
Authors: Kahn Richard A 
Published: November 2023

Abstract
The arflike gene was cloned from Drosophila melanogaster as a 1.05-kb transcription unit proximal to the developmental gene, brahma (Tamkun, et al. 1991). The arflike locus is on chromosome III, in salivary gland polytene chromosome region 72AB (accession number M61127). Polymerase chain reaction (PCR) screening of a human cDNA library indentified a cDNA fragment that encoded a peptide that was highly homologous to the fly protein, but the entire open reading frame has not yet been cloned (Clark eta/. 1993).
ArL2
Authors: Kahn Richard A 
Published: November 2023

Abstract
Human ARL2 was cloned from a fibroblast cDNA library (accession number L13687) using a specific probe obtained from analysis of PCR products using degenerate oligonucleotides from highly conserved regions of Arf proteins (Clark etal. 1993). A gene encoding a homolog was cloned from D. melanogaster genomic and cDNA libraries using the same probe (accession number L14923). Messages of the human and fly ARL2 were estimated at 0.88 and 0.8 kb, respectively, with no specificity for tissue or developmental stage observed.
Sec23p
Authors: Yoshihisa Tohru , Barlowe Charles , Schekman Randy 
Published: November 2023

Abstract
The SEC23 gene (GenBank accession number X15474) was isolated by temperature-sensitive complementation of a sec23 mutant strain (Hicke and Schekman, 1989). SEC23 encodes a predicted 768 amino acid protein with a molecular weight of 85.4 kDa. The sequence has no apparent homology to any known GAPs, including p120Ras-GAP, K- Rev-GAP or Rac-GAP. Sec23 homologues have been reported recently from mouse (Wadhwa et al. 1993) and Caenorhabditis elegans (Waterston et al. 1992), although these remain to be tested as functional homologues. Sec23p may belong to a novel family of GAPs that have conserved structure and function in vesicular transport.
TC4/Ran (JDictostelium discoideum
Authors: Bush John , Cardelli James 
Published: November 2023

Abstract
The apparent Dictyostelium homologue to the TC4/ran and spi genes was cloned (Bush and Cardelli 1993) by screening a cDNA library using an oligonucleotide coding for the sequence DTAGQE which is a conserved amino acid domain found in all GTPases. The TC4/ran cDNA insert of 804 nt was sequenced on both strands and this sequence is shown in Fig. 1, the GenBank accession number is L09720.
An Introduction to Cytokine Receptors
Authors: Hilton D J 
Published: November 2023

Abstract
It is well-established that polypeptide hormones elicit their biological effects by binding to receptors expressed on the surface of responsive cells. The characterization of cell surface receptors has proceeded in two distinct phases. Initially, the majority of receptors were described on the basis of their ability to bind radiolabelled derivatives of a particular hormone. These studies allowed the specificity of receptors to be determined and the equilibrium and kinetic characteristics of binding to be investigated. In some cases, through the additional use of chemical cross-linking reagents, an estimate of the apparent molecular weight of receptors was also possible. In general, however, the low abundance of receptors and their integral membrane location hindered their detailed biochemical characterization. Only with the advent and application of appropriate molecular genetic techniques has the predicted primary structure of many receptors been determined. The aim of the following review is to summarize the important structural features that unite receptors of a given family and to highlight themes common to the function of receptors from different families.
Interleukin-4 Receptors
Authors: Park L S 
Published: November 2023

Abstract
Both the murine (Mosley et al. 1989) and human (ldzerda et al. 1990) IL-4 receptors have been molecularly cloned. The murine IL-4 receptor, which was cloned first (Mosley et al. 1989), is produced as an 810-amino-acid precursor with a predicted 25-amino-acid signal peptide (GenBank accession number M27959). It contains a single transmembrane domain of 24 amino acids, an extracellular domain of 208 amino acids and a cytoplasmic domain of 553 amino acids. The extracellular domain contains seven cysteine residues and five potential N-linked glycosylation sites. A cDNA clone for the human IL-4 receptor was isolated utilizing cross-species hybridization and found to encode an 825-amino-acid protein (ldzerda et al. 1990). The predicted protein sequence exhibited 53 per cent sequence identity with the murine IL-4 receptor and contained a 25-aminoacid signal peptide, 207-amino-acid extracellular domain, 24-amino-acid transmembrane domain, and a 569-aminoacid cytoplasmic domain. Five of the seven cysteine residues, and three of the six potential N-linked glycosylation sites in the extracellular domain have been conserved between mouse and human receptors.
Interleukin-5 (IL-5)
Authors: Sanderson C J 
Published: November 2023

Abstract
The cDNA sequence for human and mouse (GenBank accession numbers X04688 and X06270) predict proteins of 134 and 133 amino acids, respectively. Sequence information is available for both the human and mouse genomic genes (GenBank accession numbers J02971 and XO6271).The coding sequence of the IL-5 gene forms four exons. The introns show areas of similarity between the mouse and human sequences, although the mouse has a considerable amount of sequence (including repeat sequences) which are not present in the human gene. The mouse gene includes a 738 bp segment in the 3’ untranslated region which is not present in the human gene, giving a transcript of 1.6 kb compared to 0.9 kb in man. The gross gene structure are also shared by IL-3, IL-4, and GM-CSF (Sanderson 1994).
Interleukin-7 (IL-7)
Authors: Namen A E 
Published: November 2023

Abstract
The nucleotide sequence of murine IL-7 was derived from a cDNA isolated from a bone marrow stromal cell line and predicted a protein composed of 129 amino acids (Namen et al. 1988) (GenBank accession number X07962). The human cDNA was isolated by cross-hybridization from a human hepatoma cell line (Goodwin et al. 1989). The cDNA sequence predicted a protein containing 152 amino acids (GenBank accession number J04156). Comparison of the murine and human cDNAs shows a high homology in the coding region (81 per cent) and a lesser homology in the 5’ noncoding (73 per cent) and 3’ non-coding region (63 per cent).
Interleukin-7 Receptor
Authors: Goodwin R G , Park L S 
Published: November 2023

Abstract
The human IL-7 receptor is produced as a 459-amino-acid precursor with a predicted 20-amino-acid signal peptide (GenBank accession number M29696) (Fig. 1). It contains a single transmembrane domain of 25 amino acids, an extracellular domain of 219 amino acids, and a cytoplasmic domain of 195 amino acids. The mature protein has a predicted molecular weight of 49 500 but an observed molecular weight by SOS-PAGE analysis of about 75 000, presumably due to post-translational modification of one or more of the six potential N-linked glycosylation sites (Goodwin et al. 1990). The extracellular domain of the IL-7 receptor shows significant homology to a number of other cytokine receptors, forming what is often referred to as the haemopoietin receptor superfamily.
Interleukin-11 (IL-11)
Authors: Clark S C 
Published: November 2023

Abstract
The nucleotide sequences of IL-11 cDNAs cloned from mouse and man (mouse sequence submitted to GenBank, human sequence GenBank accession number M37006) encode proteins with 199 amino acids (Fig. 1) (Paul eta/. 1990). At the amino acid level, the mouse and human proteins are highly conserved (88 per cent identity). The human protein has been shown to include a 21-amino-acid signal sequence which is likely to be identical given the conservation of amino acids around the processing site. That the human and murine proteins are very similar is also supported by the observation that both molecules are active with target cells from the alternate species (C. Wood, unpublished results). Careful analysis of the amino acid sequences and gene structures has revealed that IL-11, IL-6, granulocyte colonystimulating factor (G-CSF), OSM, LIF, CNTF, and growth hormone are all distantly related in evolution (Bruce et al. 1992). However, IL-11 and IL-6 do not directly compete in receptor binding (Yin et al. 1992a,b).
Human B Cell Growth Factor-12kDa (BCGF-12kDa)
Authors: Sharma S 
Published: November 2023

Abstract
The BCGF-12 kDa cDNA was first cloned using size fractionated poly (A+) mRNA from mitogen activated T cells (Sharma et al. 1987). BCGF-12 kDa mRNA was selected on the basis of its ability to encode B cell growth factor activityafter expression in Xenopus oocytes. The open reading frame in the BCGF-12 kDa cDNA predicts a protein of 120 amino acids (Fig. 1). The hydrophobicity analysis suggests a 13-amino-acid putative leader sequence. An unusual feature of the cDNA is the presence of an Alu repeat unit at the 3’ end. Even more intriguing, this Alu repeat unit contributes 40 amino acids to the carboxy terminus of the BCGF-12 kDa protein.
The Interferon-y Receptor
Authors: Schreiber R D , Ague! M 
Published: November 2023

Abstract
The a subunit of the human IFNy receptor (CDw119} is produced as a 489-amino-acid precursor that contains a 17-amino-acid signal sequence (GenBank accession number J03143} (Aguet et al. 1988) (Fig. 1). Although the mature, nonglycosylated 472 amino acid polypeptide has a predicted molecular mass of 50.5 kDa, it displays an Mr of 65 kDa when analysed by SDS-PAGE (Farrar and Schreiber 1993). The molecule is symmetrically oriented around a single 23-amino-acid transmembrane domain. The extracellulardomainconsists of 228 amino acids and includes ten cysteine residues and five potential N-linked glycosylation sites.
Leukaemia Inhibitory Factor (LIF)
Authors: Hilton D J 
Published: November 2023

Abstract
Differentiation inducing factor (DIF), differentiation stimulating factor (D-factor), differentiation inhibitory activity (DIA), differentiation retarding factor (ORF), cholinergic neuronal differentiating factor (CNDF), human interleukin for DA cells (HILDA), hepatocyte stimulating factor-Ill (HSF-111), melanocyte derived lipoprotein lipase inhibitor (MLPLI).
The Ciliary Neurotrophic Factor (CNTF) Receptor Complex
Authors: Yancopoulos G D 
Published: November 2023

Abstract
cDNAs encoding CNTFRa have been cloned from both human (GenBank accession number M73238) (Davis et al. 1991) and rat (GenBank accession number 554212) (Ip et al. 1993). The cDNAs for human and rat CNTFRa both predict protein precursors of 372 amino acids with putative leader sequences of approximately 20 amino acids and four conserved glycosylation sites.
The Nerve Growth Factor Family— Neurotrophins
Authors: Barde Y -A 
Published: November 2023

Abstract
Nucleotide sequences are available for several species, including rat and human for all of them (GenBank accession numbers of the human neurotrophins are: NGF VOl 511; BDNF:M61176; NT-3:M61180; and NT-4/5 M86528). About 50 per cent of the amino acids are common to all neurotrophins, including the six cysteine residues (Fig. 1). With the exception of NT-4/5, neurotrophins are highly conserved proteins between species. In all mammals analysed so far, no amino acid replacements have been found in the mature sequence of BDNF and NT-3.
The Neurotrophin Receptors
Authors: Barker P A 
Published: November 2023

Abstract
Trk receptors are ligand-regulated transmembrane tyrosine kinase receptors that bind specific members of the neurotrophin family (Barbacid 1993). The first trk to be discovered, trkA, was originally observed as a transforming oncogene in colon carcinoma (Martin-Zanca et al. 1986). Its transforming potential was due to the replacement of its normal extracellular sequence with portions of a nonmuscle tropomyosin gene. The trk family members are highly related, particularly within their tyrosine kinase domains. Numerous N-linked glycosylation sites are present extracellularly, which, in part, accounts for the fact that although the proteins have a predicted molecular weight of about 80 kDa, they run on SDS-PAGE at an apparent molecular weight of 140-145 kDa. The preferred ligand for trkA (GenBank accession number X03541, M85214) is nerve growth factor (NGF), for trkB (GenBank accession number X17647, M55291, M55292, M55293) is brain-derived neurotrophic factor (BDNF) and neurotrophin-4 (NT-4), and for trkC (GenBank accession number M80800, L03813) is neurotrophin-3 (NT-3) (Ip et al. 1993).
Stem Cell Factor (SCF)
Authors: McNiece I , Shieh J -H 
Published: November 2023

Abstract
The cDNA sequence for human SCF predicts a protein with a 25-amino-acid signal peptide, a 185-amino-acid extracellular domain, a 27-amino-acid transmembrane segment, and a 36-amino-acid intracellular domain (Martin et al. 1990). Secreted and membrane-bound forms of SCF have been identified and are due to alternative splicing of exon 6 resulting in a 248-amino-acid protein and a 220-amino-acid protein (Flanagan et al. 1991). The 248 residue form of SCF is thought to contain a proteolytic cleavage site which results in the secreted 164-amino-acid protein. Due to the lack of this proteolytic site in the 220-amino-acid form, the protein remains membrane associated.
The Growth Hormone/Prolactin Family
Authors: Clackson T 
Published: November 2023

Abstract
The cDNA sequence of human pituitary GH (hGH; GenBank accession number V00519), human PL, and GHs from most other species code for a 191-amino-acid (aa) protein preceded by a signal sequence of 26 aa (Wallis 1992). Human PL (hPL) is encoded identically from two non-allelic genes, hPL-3/hCS-B (V00573) and hPL-4/hCS-A (J00118). Thehuman pituitary PRL (hPRL) cDNA sequence (J00299) predicts a leader of 28 aa and a mature protein of 199 aa. In primates GH is highly homologous to PL (85 per cent identity in humans), whereas GH and PRL are more distantly related (23 per cent in humans: see Fig. 1).
Receptors and Binding Proteins for Insulin-like Growth Factors
Authors: LeRoith D , Roberts C T 
Published: November 2023

Abstract
The IGF-I receptor is initially synthesized as a precursor composed of a signal peptide and contiguous u and Bsubunits. Processing includes cleavage of the a andB subunits atan Arg-Lys-Arg-Arg tetrapeptide sequence, and the formation of disulphide bonds to generate a mature heterotetramic (a.2/32) receptor (Ullrich et al. 1986). The two 11subunits of the mature receptor lie entirely extracellularly, are N-glycosylated, and are involved in ligand binding.
Saccharomyces cerevisiae Ss1
Authors: Davis J , Miao B , Craig E A 
Published: November 2023

Abstract
The Ssc1 protein (Ssdp) is an abundant protein of the matrix of mitochondria (Craig et al., 1987, 1989). The nucleotide sequence of the SSC1 gene (GenBank accession number M27229) encodes a 654 amino acid polypeptide that includes a leader sequence of 23 amino acids, which is removed upon import into mitochondria.