bluuebunny/crossref_metadata_2025_split huggingface dataset:
p145
Authors: martin T J f. , Walent J H , Porter B W , Hay J C 
Published: November 2023

Abstract
The regulated exocytotic release of secretory granule constituents from neural, endocrine and exocrine cells has been studied in cells permeabilized by a variety of methods5. Secretion from permeable cells is ATP-dependent and stimulated by Ca2+ over the range of 0.1-10 M. Permeabilization methods that generate large plasma membrane lesions result in a progressive loss of ATPdependent, Ca2+-activated secretion, indicating that regulated secretion requires soluble macromolecular factors5.
VPS5
Authors: Horazdovsky B F , Emr S D 
Published: November 2023

Abstract
could correspond to a signal sequence or to membrane spanning domains. A comparison of the deduced amino acid sequence of the VP55 gene product with sequences of other known proteins revealed no significant similarities. Gene disruption experiments have shown that the VPS5 gene product is not essential for cell viability1. However, cells carrying the null allele exhibit differential defects in vacuolar protein sorting. Greater than 95% of carboxypeptidase Y (CPY) is secreted from these cells in its Golgi modified p2 precursor form.
VPS27
Authors: Raymond C K , Stevens T H 
Published: November 2023

Abstract
Strains bearing mutations within the VPS27 gene share phenotypic characteristics in common with mutants representing at least twelve other vps complementation groups1. These mutants secrete modest amounts (30-60%) of the newly synthesized soluble vacuolar protein carboxypeptidase Y (CPY). Proteolytic processing of the intracellular proCPY is normal1·3 Similarly, visual inspection and/or vacuolar vital staining of these mutant strains suggests they assemble a relatively normal vacuolar compartment.
VPS35
Authors: Horazdovsky B , Par,ivicini, G , Enu S D 
Published: November 2023

Abstract
““ “ p - _-
Cells carrying a null allele of VPS35 exhibit a differential vacuolar protein sorting defect. The sorting of CPY is drastically affected in !wps35 mutant cells; &gt;95% of CPY is secreted in its Golgi modified p2 precursor form. However, the vast majority of two other soluble vacuolar proteases, proteinase A (Pr A) and proteinase B (PrB) are retained and matured in these mutants, indicating delivery to the vacuole. These results suggest that CPY sorting is completely dependent on the presence of functional Vps35p. Yet the sorting and processing of other soluble hydrolases (PrA and PrB), as well as the vacuolar membrane protein alkaline phosphatase can occur in a Vps35p-independent manner. Apparently only a subset of soluble vacuolar proteins, like CPY, require Vps35p for their efficient sorting to the vacuole. It is possible that CPY and Pr A may utilize different receptor complexes for their sorting and/or delivery to the vacuole.
PEP7
Authors: Zhang J Q , Webb, C C , Jones E W 
Published: November 2023

Abstract
hole contents by the bud is profoundly impaired in these mutants; however, vacuoles do eventually form. In addition, intervacuole communication in zygotes14 is greatly diminished. Whereas lack of the VAC1/PEP7 gene has a profound effect on vacuole segregation, the accurate segregation of the nucleus, mitochondria and Golgi apparatus does not require VAC7/PEP7function.
VMA13
Authors: Ho M N , Stevens T H 
Published: November 2023

Abstract
Mutant phenotypes associated with vma13 cells are identical to those found for vma2 mutants (see VMA2 entry p. 261)1,3_ However, deletion of the VMA13 gene in yeast results in strains that are deficient for vacuolar acidification12. The remaining vacuolar H+-ATPase subunits (Vma1p, Vma2p, Vma3p, Vma4p, Vma5p, and Vph 1p) continue to associate with the vacuolar membrane in the absence of Vma13p. This is surprising given that several of the remaining subunits, including the Vma1, Vma2, Vma4, and Vma5 polypeptides, are hydrophilic proteins that are thought to peripherally associate with the vacuolar membrane only when the H+-ATPase is fully assembled45. These results suggest that although Vma13p is essential for the activity of the vacuolar W-ATPase, it is not required for some level of enzyme assembly onto the vacuolar membrane.
CLC1
Authors: Silveira L , Schekman R 
Published: November 2023

Abstract
In most strain backgrounds, haploid yeast cells lacking 93% of the CLC1 coding region are viable, but grow -2-3 times more slowly than wild-type cells. Upon propagation, fastergrowing variants arise. Cells lacking both clathrin light chain and clathrin heavy chain (encoded by CHC1 - see CHC1 entry p. 267) are also viable but slow-growing. Clathrin heavy chain is less stable in c/c1 cells than in wildtype cells4. Vesicles isolated from clc1 cells do not contain detectable clathrin heavy chain, even if prepared from cells overproducing clathrin heavy chain5 It has not been determined whether clathrin heavy chain coats on these vesicles are unstable to isolation or whether they are never formed. Light-chain-deficient cells, like cells lacking clathrin heavy chain6, secrete a heterogeneous high molecular weight form of the mating pheromone a-factor4, presumably due to the mislocalization of the processing protease Kex2p.
END2
Authors: Hamburger C , Egerton, M , Riezman H 
Published: November 2023

Abstract
The end2 mutant was isolated by screening a bank of ethanemethanesulfonate mutagenized yeast cells for their ability to accumulate lucifer yellow CH in the vacuole. The original mutant allele, end2-1, is temperature-sensitive for growth showing only slight growth at 37°C. Lucifer yellow CH accumulation in the vacuole is also thermosensitive with significant, but less than wild-type accumulation at 24°C. cx.-factor pheromone, an endocytic marker, is internalized normally at 37°C in the mutant. Pheromone degradation is strongly inhibited at this temperature indicating that transport of internalized cx.-factor to the vacuole is blocked. Vacuole morphology and maturation of the vacuolar enzyme, carboxypeptidase Y, are nearly the same as in wild-type cells. lnvertase secretion is also normal. Haploid cells carrying a disrupted open reading frame in END2 are inviable2
RENZ
Authors: Davis O G , Sprague,Jr. G F 
Published: November 2023

Abstract
The ren1 mutation was isolated by virtue of its defect in receptor endocytosis . The yeast pheromone receptors, members of the rhodopsin/j3--adrenergic receptor family, are subject to endocytosis, which proceeds rapidly and constitutively in the absence of cognate pheromoneligand. This constitutive endocytosis has been well established for the a-factor receptor. Internalized receptors are delivered to the vacuole where they are hydrolysed in a PEP4-dependent process1 (see PEP4 entry p. 247). The halflife of the receptor is about 20 min in wild-type cells; in pep4 cells receptor half-life increases to much greater than 2 hr. Moreover, when degradation is blocked in pep4cells, the a-factor receptor visualized by indirect immunofluorescence microscopy is found to accumulate in the vacuole1. The a-factor receptor also appears to be subject to constitutive endocytosis.
UDP-N-acety lglucosamine : ly sosomal enzyme N-acetylglucosaminc 1-phosphotransfcrase
Authors: Ketcham D M 
Published: November 2023

Abstract
Fibroblasts from patients with I-cell disease (mucolipidosis II) contain little or no detectable GlcNAc-phosphotransferase, whereas pseudo-Hurler (mucolipidosis Ill) fibroblasts are characterized by residual low levels of GlcNAc-phosphotransferase. Three complementation groups have been identified by cell fusion experiments5-7. Fibroblasts from all three groups are deficient in lysosomal enzyme phosphorylation, but group IIIC fibroblasts retain the ability to phosphorylate a-methylmannoside. While group IIIA and 111B mutant enzymes show decreased activities towards a-methylmannoside as well as lysosomal enzymes, the apparent Km values are normal. Group IIIC fibroblasts therefore contain a normal level of GlcNAcphosphotransferase that is deficient in the specific recognition of lysosomal enzymes, while group IIIA and 111B deficiencies may be due to decreased synthesis or instability of the enzyme, or possibly synthesis of an enzyme with a defective catalytic domain4 7-9.
Dynamin (shibire)
Authors: Vallee R B 
Published: November 2023

Abstract
Dynamin was initially isolated from calf brain tissue by microtubule co-purification1 In this procedure microtubules are assembled from cytosolic extracts using taxol, washed, and dynamin is extracted with GTP. AMPPNP is included in this step to prevent extraction of kinesin. The dynamin is subsequently rebound to microtubules, reextracted, and further purified by DEAE-Sepharose chromatography.
SSS1
Authors: é E K épe 
Published: November 2023

Abstract
The 5551 gene (for “Sec Sixty-one Suppressor”) was isolated as a strong multicopy suppressor of the sec61-2 mutation that affects protein translocation. A conditional expression mutant was constructed by expressing the 5551 gene under the control of a galactose-inducible promoter on a plasmid, while disrupting the chromosomalrnpy of the gene. One or two generations after a shift to restrictive growth conditions, the mutant cells start accumulating precursor forms of several secretory or vacuolar proteins on the cytosolic aspect of intracellular membranes, presumably at the site of translocation/insertion. These accumulated proteins include the soluble proteins prepro-a-factor, invertase, carboxypeptidase Y, and the membrane protein dipeptidylaminopeptidase B1.
End5
Authors: Draper R K 
Published: November 2023

Abstract
Mutant 42.2, selected for resistance to diphtheria toxin, represents the End5 complementation group12 42.2 cells are temperature-sensitive for viability and accumulate less transferrin than normal at the restrictive temperature. Endosomal and lysosomal acidification are apparently unimpaired. 42.2 cells are not defective in secreti.
SEC1
Authors: Novick P 
Published: November 2023

Abstract
Temperature-sensitive, conditionally lethal sec1 mutants were isolated by a density enrichment protocol2,3. The sec1 mutants are blocked in the export of cell surface proteins and accumulate 100 nm post-Golgi vesicles containing fully glycosylated secretory proteins23,78. The best characterized sec1 allele is sec1-1.
CAAX farnesyl transferase
Authors: Seabra Miguel C , Brown Michael S , Goldstein Joseph L 
Published: November 2023

Abstract
Tase is composed of two tightly coupled subunits, designated a and p (Reiss et al. 1990). Mammalian cDNAs forboth subunits were cloned initially from a rat brain cDNA library using oligonucleotides encoding peptides present in the purified protein (Chen et al. 1991a,b). cDNAs for both subunits were subsequently cloned from bovine brain (Kohl eta/. 1991; Omer et al. 1993), human placenta (Omer et al. 1993), and human retina (Andres et al. 1993a). GenBank accession numbers for the a-subunit are M81225 (rat), M74083 (bovine), and L10413 (human). GenBank accession numbers for the P-subunit are M69056 (rat),L00633 (bovine), and L10414 (human). The genes for a andsubunits of human FTase have been mapped to chromosomes 8p22-q11 and 14q23-q24, respectively., USA
Rab escort proteins (REP1 and REP2)
Authors: Seabra Miguel C , Goldstein Joseph L , Brown Michael S 
Published: November 2023

Abstract
Two different Rab escort proteins, designated REP1 (also known as choroideremia gene product (CHM) or Component A of Rab GGTase) and REP2 (also known as choroideremia-like gene product (CHML)), have been identified. The gene for human REP1 was originally isolated by positional cloning techniques as a candidate gene for choroideremia, a retinal degeneration disease (Cremers et al. 1990). Later, the cDNA for rat REP1 was cloned from a brain library (Andres et al. 1993) based on sequences of tryptic peptides derived from REP1 purified from rat brain (Seabra et al. 1992). The cDNA for REP2 was cloned by crosshybridization with probes for REP1 (Cremers et al. 1992). USA.
Cal1p/Cdc43p
Authors: Ohya Yoshikazu , Anraku Yasuhiro , Trueblood Cynthia E 
Published: November 2023

Abstract
ca/1-1 was originally identified as a mutation resulting in aCa2+-dependent phenotype (Ohya et al. 1984). The mutantexhibits a homogeneous terminal phenotype at 37°C witha G2/M nucleus and a small bud (Ohya et al. 1984).Independent screening of the yeast cell cycle mutants thataccumulated enlarged unbudded cells identified cdc43-2-cdc43-7 (Adams et al. 1990). The complete nucleotidesequence of Cal1/Cdc43 was determined by Johnson et al.(1990, correction appeared in 1991) and Ohya eta/. (1991).The GenBank accession numbers are M29471 and M31114.Note that another group temporarily used CAL 1 as thename of a gene encoding chitin syntase isozyme(Valdivieso et al. 1991), which is now called CHS3 (Shaw etal. 1991).59.
K-Ras
Authors: McCormick Frank 
Published: November 2023

Abstract
K-RasA and B are P01116 and P01118; for mouse K-RasA and B they are P32883 and P08643. The nucleotide sequence is shown in Fig. 1.I ProteinsViral K-Ras, transduced by the Kirsten sarcoma virus, corresponds to the splicing variant designated K-Ras 4A. This protein, when fully processed, consists of 186 amino acids and has a (-terminus modified by farensylation as well as palmitolylation.
RalB
Authors: Chardin Pierre 
Published: November 2023

Abstract
RalB was isolated from a human pheochromocytoma cDNA library using a simian RalA probe at moderate stringency (Chardin and Tavitian 1989; GenBank accession number X15015), and later from a human retina cDNA library (Hsieh et al. 1990; GenBank accession number M35416), a rat pheochromocytoma cDNA library (Wildey et al. 1993; GenBank accession number L19699), and a marine ray electric lobe cDNA library (Ngsee et al. 1991; GenBank accession number M38394).
Sos
Authors: Downward Julian 
Published: November 2023

Abstract
Drosophila Sos was cloned due to the effect of mutations in the son of sevenless locus on the development of photoreceptor cell R7 (Bonfini etal. 1992; Simon etal. 1991). Two murine Sos cDNAs, Sos1 and Sos2, were cloned by low stringency hybridization to Drosophila Sos probes (Bowtell et al. 1992). Human Sos1 was cloned by a similar method (Chardin et al. 1993). GenBank accession numbers: human Sos1, L13857; murine Sos1, Z11574; murine Sos2, Z11664; Drosophila Sos, M83931.
Cdc25 Mm (Dpd-GEF)
Authors: Martegani Enzo , Vanoni Marco , Zippel Renata , Sturani Emmapaola , Alberghina Lilia 
Published: November 2023

Abstract
CDC25Mm was identified by screening a mouse brain cDNA expression library (constructed in the yeast expression vector pGR56) by functional complementation of a Saccharomyces cerevisiae strain carrying the cdc25 temperature sensitive mutation (Martegani etal. 1992). Two clones were isolated, CDC25Mm12, encoding a protein of 287 aa, and a longer one, CDC25Mm17, encoding a protein of 472 aa (Accession number X59868). By taking advantage of the CDC25Mm12 sequence, Cen et al.
Smg-GDS
Authors: Kaibuchi Kozo , Takai Yoshimi 
Published: November 2023

Abstract
Smg-GDS was purified from bovine brain cytosol and its partial amino acid sequences were determined (Yamamoto et al. 1990). Bovine Smg-GDS cDNA was isolated from a bovine brain cDNA library using oligonucleotide probes designed from its partial amino acid sequences (Kaibuchi et al. 1991). Human Smg-GDS cDNA was isolated from a human brain cDNA library by use of bovine Smg-GDS cDNA as a probe (Kikuchi etal. 1992). The nucleotide sequence of the bovine Smg-GDS cDNA and its deduced amino acid sequence are shown in Fig. 1. GenBank accession numbers are M63325 (Bovine Smg-GDS) and X63465 (Human SmgGDS).
Rap-GAP
Authors: McCormick Frank 
Published: November 2023

Abstract
Rap-GAP is a protein of 88 kDa, comprising 663 amino acids (Rubinfeld etal. 1991). Of these, 75 to 516 are necessary for Rap-GAP activity (Rubinfeld et al. 1992). An alternative splice variant has been cloned that contains an additional 26 amino acids These residues make up a repeat of similar sequence adjacent to the splice point (Rubinfeld et al.
Extracellular signal-regulated kinases (ERKs)
Authors: vers Sally Lee , Marshall Chris 
Published: November 2023

Abstract
A partial cDNA for rat ERK1 (Boulton et al. 1990) and full length cDNA for rat ERK2 (Boulton et al. 1991) were the first ERK-encoding cDNAs isolated. More recently, full length human sequences encoding ERK1 (Charest et al. 1993) and ERK2 (Owaki etal. 1992) have been isolated (Fig. 1).
Ira1p
Authors: Powers Scott 
Published: November 2023

Abstract
The Ira1 gene was cloned from a yeast DNA expression library by complementation of the heat-shock sensitivity of an ira1-1 mutant (Tanaka etal. 1989). The ira1-1 mutation was isolated by virtue of its ability to counteract the growth inhibitory effect of a temperature-sensititive cyr2/cdc25 mutation (Tanaka etal. 1989). The ira1-1 mutation was originally termed ppd1-1 (Tanaka etal. 1989). The GenBank accession number is M24378.
SP-Ras
Authors: Kaziro Yoshito 
Published: November 2023

Abstract
The S. pombe ras1 gene was identified by Southern blotting of S. pombe DNA with S. cerevisiae RAS1/RAS2 (Fukui and Kaziro 1985). The coding sequence for 219 amino acids is interrupted by an intron of 67 bp between codons 2 and The sequences GTAAGT and TAG were found as splice donor and acceptor sequences, respectively, and a sequence AACTAATCA which is similar to the splice consensus sequence TACTAACA for S. cerevisiae was present in the intron. The DNA sequence of S.pombe ras1 is shown in Fig. 1. GenBank accession number is X02331. The cloning and characterization of a gene allelic to ras1 from S.pombe was also reported by Nadin-Davis et al. (1986). The GenBank accession number of the latter authors’ sequence is X03771.
RhoB
Authors: Hall Alan 
Published: November 2023

Abstract
Rho sequences were originally isolated from an Aplysia cDNA library and used to identify three distinct, but highly homologous human sequences (Madaule and Axel 1985). The complete sequence of one of these, human rhoB (originally clone 6), (Chardin et al. 1988) is shown in Fig. 1. The GenBank accession number is X06820.
RhoC
Authors: Hall Alan 
Published: November 2023

Abstract
Rho sequences were originally isolated from an Aplysia cDNA library and used to identify three distinct, but highly homologous human sequences (Madaule and Axel 1985). The complete sequence of one of these, human RhoC (originally clone 9) (Chardin etal. 1988), is shown in Fig. 1. The GenBank accession number is X06821.
Cdc42Hs
Authors: Cerione Richard 
Published: November 2023

Abstract
Cdc42Hs was identified by screening a human placental cDNA library (Shinjo et al. 1990) and a human fetal brain library (Munimetsu etal. 1990) using degenerate oligonucleotide probes from peptide sequences generated from the purified GTP-binding protein isolated from human platelets and human placenta (Polakis et al. 1989). This GTP-binding protein was originally named Gp because of its apparent high abundance in platelets and placenta (Evans etal. 1986) and then later named G25K because of its mobility on some sodium dodecyl sulfate (SDS) gel systems (Polakis et al. 1989).
Rho-GAP
Authors: Hall Alan 
Published: November 2023

Abstract
A full-length Rho-GAP clone has been isolated from a human fibrosarcoma cDNA library (Lancaster eta/. 1994). A single mRNA of approximately 3600 nucleotides encodes a protein of 50 kDa. The nucleotide sequence of human p50 Rho-GAP and its deduced amino acid sequence are shown in Fig. 1. The GenBank accession number is Z23024.
Rho-p21-associated protein kinases
Authors: Manser Edward , Leung Thomas , Lim Louis 
Published: November 2023

Abstract
A human partial ACK cDNA was isolated by expression screening of a hippocampal library with (732P]GTP-labelled recombinant Cdc42. Subsequent screening of the library by DNA hybridization yielded a full-length cDNA of 4545 nucleotides (Manser et al. 1993). The human cDNA encodes a protein of molecular mass 119 kDa with 1091 amino acid residues and contains 450 nt of 5’ non-coding sequence and 819 nt of 3’ non-coding sequence (Fig. 1).
RhoSp
Authors: Matsui Yasushi , Imai Jun , Toh-e Akio 
Published: November 2023

Abstract
Several DNA fragments were amplified by polymerase chain reaction using yeast genomic DNA as a template and convergent degenerated olignucleotides corresponding to the sequences GXXXV/CGKT/S and DTAGQE, conserved in members of Ras-, Rho-, and Rab-type GTPases (Barbacid 1987). RHOB was identified by sequencing such DNA fragments, and clones carrying the full-length RHOB gene were isolated by screening a yeast Saccharomyces cerevisiae genomic DNA library using the amplified DNA fragment as a probe (Matsui and Toh-e 1992a).
Rho4p
Authors: Matsui Yasushi , Toh-e Akio 
Published: November 2023

Abstract
Several DNA fragments were amplified by polymerase chain reaction using yeast genomic DNA as a template and using convergent degenerated olignucleotides corresponding to the sequences GXXXV/CGKT/S and DTAGQE, conserved in members of Ras-, Rho-, and Rab-type GTPases (Barbacid 1987). RHO4 was identified by sequencing these DNA fragments, and clones carrying the full-length RHO4 gene were isolated by screening a yeast Saccharomyces cerevisiae genomic DNA library using the amplified DNA fragment as a probe (Matsui and Toh-e 1992). The DNA and deduced amino acid sequences of RHO4 are shown in Fig. 1. GeneBank accession number is D10007.
Rabla, b
Authors: Balch William E 
Published: November 2023

Abstract
Rabla and 1 b isoforms have been identified by the screening of cDNA libraries from mouse, rat, human and canine sources using oligonucleotide probes specific to Rasrelated proteins (Haubruck etal. 1987; Touchot etal. 1987; Wagner eta/. 1987; Tachibana etal. 1988; Vielh eta/. 1989; Wichmann etal. 1989; Zahraoui etal. 1989; Chavrier eta/. 1990, 1992). The nucleotide sequence of the rat Rabla (Touchot et al. 1987) and the rat Rablb (Wichmann et al. 1989) isoforms are shown in Fig. 1. GenBank accession numbers are J02998 (Rabla) and X13905 (Rablb).
Rab5a
Authors: Kikuchi Akira , Takai Yoshimi 
Published: November 2023

Abstract
Rab3a cDNA was isolated by two methods. In the first, the small GTPase with an Mr of 24 kD was purified from bovine brain membranes (Kikuchi et al. 1988). Its partial amino acid sequences were determined and bovine Rab3a cDNA was isolated from a bovine brain cDNA library using oligonucleotide probes designed from its partial amino acid sequences (Matsui etal. 1988). In the second method, rat Rab3a cDNA was isolated by screening a rat brain cDNA library using oligonucleotide probes synthesized according to the sequences corresponding to the consensus sequences of the GDP/GTP-binding domains (Zahraoui et al. 1988).
Rab4a
Authors: Mellman Ira 
Published: November 2023

Abstract
Rab4a was identified by screening a rat brain (Touchot et al. 1987) and human pheochromocytoma cDNA libraries (Zahraoui etal. 1989) with an oligonucleotide corresponding to the amino acid sequence WDTAGQE, which is shared by members of the Rab and Rho protein subfamilies (Valencia etal. 1991). The GenBank accession numbers are J03001 and M28211.
Rab5a
Authors: Zerial Marino 
Published: November 2023

Abstract
Rab5a was identified by screening a cDNA library (Zahraoui et al. 1989; Chavrier et al. 1990) using degenerated oligonucleotides corresponding to the sequence WDTAGQE shared by members of the Ypt1/Sec4/Rab subfamily (Valencia et al. 1991). It was originally named Rab5 before the identification of the Rab5b and Rab5c proteins (Chavrier eta/. 1992). Rab5 is now renamed Rab5a. The DNA sequence of canine Rab5a (Chavrier etal. 1990) is shown in Fig. 1. The GenBank accession number is M35520 for canine Rab5a and M28215 for human Rab5a.