Kinoshita T

References (15)

Title : Plant Chemical Biology -
Author(s) : Kinoshita T , McCourt P , Asami T , Torii KU
Ref : Plant Cell Physiol , 59 :1483 , 2018
PubMedID: 30032233

Title : A femtomolar-range suicide germination stimulant for the parasitic plant Striga hermonthica - Uraguchi_2018_Science_362_1301
Author(s) : Uraguchi D , Kuwata K , Hijikata Y , Yamaguchi R , Imaizumi H , Am S , Rakers C , Mori N , Akiyama K , Irle S , McCourt P , Kinoshita T , Ooi T , Tsuchiya Y
Ref : Science , 362 :1301 , 2018
Abstract : The parasitic plant Striga hermonthica has been causing devastating damage to the crop production in Africa. Because Striga requires host-generated strigolactones to germinate, the identification of selective and potent strigolactone agonists could help control these noxious weeds. We developed a selective agonist, sphynolactone-7, a hybrid molecule originated from chemical screening, that contains two functional modules derived from a synthetic scaffold and a core component of strigolactones. Cooperative action of these modules in the activation of a high-affinity strigolactone receptor ShHTL7 allows sphynolactone-7 to provoke Striga germination with potency in the femtomolar range. We demonstrate that sphynolactone-7 is effective for reducing Striga parasitism without impinging on host strigolactone-related processes.
ESTHER : Uraguchi_2018_Science_362_1301
PubMedSearch : Uraguchi_2018_Science_362_1301
PubMedID: 30545887

Title : Discovery of Shoot Branching Regulator Targeting Strigolactone Receptor DWARF14 - Yoshimura_2018_ACS.Cent.Sci_4_230
Author(s) : Yoshimura M , Sato A , Kuwata K , Inukai Y , Kinoshita T , Itami K , Tsuchiya Y , Hagihara S
Ref : ACS Cent Sci , 4 :230 , 2018
Abstract : DWARF14 (D14) is a strigolactone receptor that plays a central role in suppression of shoot branching, and hence is a potential target to increase crop productions and biomass. Recently, we reported a fluorescence turn-on probe, Yoshimulactone Green (YLG), which generates a strong fluorescence upon the hydrolysis by D14-type strigolactone receptors. Herein, we applied a YLG-based in vitro assay to a high-throughput chemical screening and identified a novel small molecule DL1 as a potent inhibitor of D14. DL1 competes with endogenous strigolactones, thereby increasing the number of shoot branching in a model plant Arabidopsis as well as in rice. Thus, DL1 is expected to be useful not only as a tool to understand the biological roles of D14 receptors in plant growth and development, but also as a potent agrochemical to improve the crop yield.
ESTHER : Yoshimura_2018_ACS.Cent.Sci_4_230
PubMedSearch : Yoshimura_2018_ACS.Cent.Sci_4_230
PubMedID: 29532023

Title : Glycosylphosphatidylinositol (GPI) Anchors: Biochemistry and Cell Biology: Introduction to a Thematic Review Series -
Author(s) : Kinoshita T
Ref : J Lipid Res , 57 :4 , 2016
PubMedID: 26582962

Title : Biosynthesis of GPI-anchored proteins: special emphasis on GPI lipid remodeling - Kinoshita_2016_J.Lipid.Res_57_6
Author(s) : Kinoshita T , Fujita M
Ref : J Lipid Res , 57 :6 , 2016
Abstract : Glycosylphosphatidylinositols (GPIs) act as membrane anchors of many eukaryotic cell surface proteins. GPIs in various organisms have a common backbone consisting of ethanolamine phosphate (EtNP), three mannoses (Mans), one non-N-acetylated glucosamine, and inositol phospholipid, whose structure is EtNP-6Manalpha-2Manalpha-6Manalpha-4GlNalpha-6myoinositol-P-lipid. The lipid part is either phosphatidylinositol of diacyl or 1-alkyl-2-acyl form, or inositol phosphoceramide. GPIs are attached to proteins via an amide bond between the C-terminal carboxyl group and an amino group of EtNP. Fatty chains of inositol phospholipids are inserted into the outer leaflet of the plasma membrane. More than 150 different human proteins are GPI anchored, whose functions include enzymes, adhesion molecules, receptors, protease inhibitors, transcytotic transporters, and complement regulators. GPI modification imparts proteins with unique characteristics, such as association with membrane microdomains or rafts, transient homodimerization, release from the membrane by cleavage in the GPI moiety, and apical sorting in polarized cells. GPI anchoring is essential for mammalian embryogenesis, development, neurogenesis, fertilization, and immune system. Mutations in genes involved in remodeling of the GPI lipid moiety cause human diseases characterized by neurological abnormalities. Yeast Saccharomyces cerevisiae has >60 GPI-anchored proteins (GPI-APs). GPI is essential for growth of yeast. In this review, we discuss biosynthesis of GPI-APs in mammalian cells and yeast with emphasis on the lipid moiety.
ESTHER : Kinoshita_2016_J.Lipid.Res_57_6
PubMedSearch : Kinoshita_2016_J.Lipid.Res_57_6
PubMedID: 26563290

Title : Genome evolution in the allotetraploid frog Xenopus laevis - Session_2016_Nature_538_336
Author(s) : Session AM , Uno Y , Kwon T , Chapman JA , Toyoda A , Takahashi S , Fukui A , Hikosaka A , Suzuki A , Kondo M , van Heeringen SJ , Quigley I , Heinz S , Ogino H , Ochi H , Hellsten U , Lyons JB , Simakov O , Putnam N , Stites J , Kuroki Y , Tanaka T , Michiue T , Watanabe M , Bogdanovic O , Lister R , Georgiou G , Paranjpe SS , van Kruijsbergen I , Shu S , Carlson J , Kinoshita T , Ohta Y , Mawaribuchi S , Jenkins J , Grimwood J , Schmutz J , Mitros T , Mozaffari SV , Suzuki Y , Haramoto Y , Yamamoto TS , Takagi C , Heald R , Miller K , Haudenschild C , Kitzman J , Nakayama T , Izutsu Y , Robert J , Fortriede J , Burns K , Lotay V , Karimi K , Yasuoka Y , Dichmann DS , Flajnik MF , Houston DW , Shendure J , DuPasquier L , Vize PD , Zorn AM , Ito M , Marcotte EM , Wallingford JB , Ito Y , Asashima M , Ueno N , Matsuda Y , Veenstra GJ , Fujiyama A , Harland RM , Taira M , Rokhsar DS
Ref : Nature , 538 :336 , 2016
Abstract : To explore the origins and consequences of tetraploidy in the African clawed frog, we sequenced the Xenopus laevis genome and compared it to the related diploid X. tropicalis genome. We characterize the allotetraploid origin of X. laevis by partitioning its genome into two homoeologous subgenomes, marked by distinct families of 'fossil' transposable elements. On the basis of the activity of these elements and the age of hundreds of unitary pseudogenes, we estimate that the two diploid progenitor species diverged around 34 million years ago (Ma) and combined to form an allotetraploid around 17-18 Ma. More than 56% of all genes were retained in two homoeologous copies. Protein function, gene expression, and the amount of conserved flanking sequence all correlate with retention rates. The subgenomes have evolved asymmetrically, with one chromosome set more often preserving the ancestral state and the other experiencing more gene loss, deletion, rearrangement, and reduced gene expression.
ESTHER : Session_2016_Nature_538_336
PubMedSearch : Session_2016_Nature_538_336
PubMedID: 27762356
Gene_locus related to this paper: xenla-a0a1l8f4t7 , xenla-a0a1l8fbc6 , xenla-a0a1l8fct2 , xenla-q2tap9 , xenla-q4klb6 , xenla-q5xh09 , xenla-q6ax59 , xenla-q6dcw6 , xenla-q6irp4 , xenla-q6pad5 , xenla-q7sz70 , xenla-Q7ZXQ6 , xenla-q66kx1 , xenla-q640y7 , xenla-q642r3 , xenla-Q860X9 , xenla-BCHE2 , xenla-a0a1l8g7v4 , xenla-a0a1l8g1u7 , xenla-a0a1l8fmc5 , xenla-a0a1l8g467 , xenla-a0a1l8g4e4 , xenla-a0a1l8ga66 , xenla-a0a1l8gaw4 , xenla-a0a1l8gt68 , xenla-a0a1l8h0b2 , xenla-a0a1l8fdr1 , xenla-a0a1l8fdt7 , xenla-a0a1l8fi72 , xenla-a0a1l8fi73 , xenla-a0a1l8fi77 , xenla-a0a1l8fi96 , xenla-a0a1l8hc38 , xenla-a0a1l8hn27 , xenla-a0a1l8hry6 , xenla-a0a1l8hw96 , xenla-a0a1l8i2x6 , xenla-a0a1l8hei7 , xenla-a0a1l8gnd1 , xenla-a0a1l8i2g3 , xenla-a0a1l8hdn0 , xenla-a0a1l8h622

Title : PARASITIC PLANTS. Probing strigolactone receptors in Striga hermonthica with fluorescence - Tsuchiya_2015_Science_349_864
Author(s) : Tsuchiya Y , Yoshimura M , Sato Y , Kuwata K , Toh S , Holbrook-Smith D , Zhang H , McCourt P , Itami K , Kinoshita T , Hagihara S
Ref : Science , 349 :864 , 2015
Abstract : Elucidating the signaling mechanism of strigolactones has been the key to controlling the devastating problem caused by the parasitic plant Striga hermonthica. To overcome the genetic intractability that has previously interfered with identification of the strigolactone receptor, we developed a fluorescence turn-on probe, Yoshimulactone Green (YLG), which activates strigolactone signaling and illuminates signal perception by the strigolactone receptors. Here we describe how strigolactones bind to and act via ShHTLs, the diverged family of alpha/beta hydrolase-fold proteins in Striga. Live imaging using YLGs revealed that a dynamic wavelike propagation of strigolactone perception wakes up Striga seeds. We conclude that ShHTLs function as the strigolactone receptors mediating seed germination in Striga. Our findings enable access to strigolactone receptors and observation of the regulatory dynamics for strigolactone signal transduction in Striga.
ESTHER : Tsuchiya_2015_Science_349_864
PubMedSearch : Tsuchiya_2015_Science_349_864
PubMedID: 26293962
Gene_locus related to this paper: strhe-ShHTL2 , strhe-ShHTL10 , strhe-ShHTL6 , strhe-ShHTL9 , strhe-ShHTL8 , strhe-ShHTL11 , strhe-ShD14 , strhe-ShHTL4 , strhe-ShHTL1 , strhe-ShHTL7 , strhe-ShHTL3 , strhe-ShHTL5

Title : Cerebral visual impairment and intellectual disability caused by PGAP1 variants - Bosch_2015_Eur.J.Hum.Genet_23_1689
Author(s) : Bosch DG , Boonstra FN , Kinoshita T , Jhangiani S , de Ligt J , Cremers FP , Lupski JR , Murakami Y , de Vries BB
Ref : Eur J Hum Genet , 23 :1689 , 2015
Abstract : Homozygous variants in PGAP1 (post-GPI attachment to proteins 1) have recently been identified in two families with developmental delay, seizures and/or spasticity. PGAP1 is a member of the glycosylphosphatidylinositol anchor biosynthesis and remodeling pathway and defects in this pathway are a subclass of congenital disorders of glycosylation. Here we performed whole-exome sequencing in an individual with cerebral visual impairment (CVI), intellectual disability (ID), and factor XII deficiency and revealed compound heterozygous variants in PGAP1, c.274_276del (p.(Pro92del)) and c.921_925del (p.(Lys308Asnfs*25)). Subsequently, PGAP1-deficient Chinese hamster ovary (CHO)-cell lines were transfected with either mutant or wild-type constructs and their sensitivity to phosphatidylinositol-specific phospholipase C (PI-PLC) treatment was measured. The mutant constructs could not rescue the PGAP1-deficient CHO cell lines resistance to PI-PLC treatment. In addition, lymphoblastoid cell lines (LCLs) of the affected individual showed no sensitivity to PI-PLC treatment, whereas the LCLs of the heterozygous carrier parents were partially resistant. In conclusion, we report novel PGAP1 variants in a boy with CVI and ID and a proven functional loss of PGAP1 and show, to our knowledge, for the first time this genetic association with CVI.
ESTHER : Bosch_2015_Eur.J.Hum.Genet_23_1689
PubMedSearch : Bosch_2015_Eur.J.Hum.Genet_23_1689
PubMedID: 25804403

Title : Null mutation in PGAP1 impairing Gpi-anchor maturation in patients with intellectual disability and encephalopathy - Murakami_2014_PLoS.Genet_10_e1004320
Author(s) : Murakami Y , Tawamie H , Maeda Y , Buttner C , Buchert R , Radwan F , Schaffer S , Sticht H , Aigner M , Reis A , Kinoshita T , Jamra RA
Ref : PLoS Genet , 10 :e1004320 , 2014
Abstract : Many eukaryotic cell-surface proteins are anchored to the membrane via glycosylphosphatidylinositol (GPI). There are at least 26 genes involved in biosynthesis and remodeling of GPI anchors. Hypomorphic coding mutations in seven of these genes have been reported to cause decreased expression of GPI anchored proteins (GPI-APs) on the cell surface and to cause autosomal-recessive forms of intellectual disability (ARID). We performed homozygosity mapping and exome sequencing in a family with encephalopathy and non-specific ARID and identified a homozygous 3 bp deletion (p.Leu197del) in the GPI remodeling gene PGAP1. PGAP1 was not described in association with a human phenotype before. PGAP1 is a deacylase that removes an acyl-chain from the inositol of GPI anchors in the endoplasmic reticulum immediately after attachment of GPI to proteins. In silico prediction and molecular modeling strongly suggested a pathogenic effect of the identified deletion. The expression levels of GPI-APs on B lymphoblastoid cells derived from an affected person were normal. However, when those cells were incubated with phosphatidylinositol-specific phospholipase C (PI-PLC), GPI-APs were cleaved and released from B lymphoblastoid cells from healthy individuals whereas GPI-APs on the cells from the affected person were totally resistant. Transfection with wild type PGAP1 cDNA restored the PI-PLC sensitivity. These results indicate that GPI-APs were expressed with abnormal GPI structure due to a null mutation in the remodeling gene PGAP1. Our results add PGAP1 to the growing list of GPI abnormalities and indicate that not only the cell surface expression levels of GPI-APs but also the fine structure of GPI-anchors is important for the normal neurological development.
ESTHER : Murakami_2014_PLoS.Genet_10_e1004320
PubMedSearch : Murakami_2014_PLoS.Genet_10_e1004320
PubMedID: 24784135
Gene_locus related to this paper: human-PGAP1

Title : Two cases of autosomal recessive woolly hair with LIPH gene mutations - Harada_2013_Int.J.Dermatol_52_572
Author(s) : Harada K , Inozume T , Kawamura T , Shibagaki N , Kinoshita T , Deguchi N , Shimada S
Ref : Int J Dermatol , 52 :572 , 2013
Abstract : BACKGROUND: Woolly hair is a hereditary disorder characterized by fine and tightly curled hair. Autosomal recessive woolly hair (ARWH) was recently determined to result from mutations in either the lipase H (LIPH) or the LPAR6 (P2RY5) gene. CASE REPORT: An 8-year-old boy (proband) and his 11-year-old brother presented with tightly coiled and sparse scalp hair. The boys did not have cardiomyopathy, palmoplantar keratoderma, or facial dysmorphism. Their parents had normal hair growth and no woolly hair. The sequence analysis of their genomic DNA revealed that the proband and his brother had a homozygous mutation of c.736T > A in the LIPH gene. On the basis of these findings, these patients were diagnosed with ARWH. CONCLUSIONS: To the best of our knowledge, only 20 cases of ARWH have been previously reported in Japan. However, several reports showed that one mutation was detected in the 4/200 normal and unrelated alleles in healthy Japanese control individuals, indicating the presence of ARWH in patients with extremely mild symptoms.
ESTHER : Harada_2013_Int.J.Dermatol_52_572
PubMedSearch : Harada_2013_Int.J.Dermatol_52_572
PubMedID: 23590372
Gene_locus related to this paper: human-LIPH

Title : Low serum level of cholinesterase at recurrence of pancreatic cancer is a poor prognostic factor and relates to systemic disorder and nerve plexus invasion - Mitsunaga_2008_Pancreas_36_241
Author(s) : Mitsunaga S , Kinoshita T , Hasebe T , Nakagohri T , Konishi M , Takahashi S , Gotohda N , Ochiai A
Ref : Pancreas , 36 :241 , 2008
Abstract : OBJECTIVES: Systemic disorder is a characteristic of advanced pancreatic cancer. Clinical prognostic factors in earlier disease state than terminal stage are expected to be sensitive markers for the foresight of systemic disorder. This study aimed to find the associations between these sensitive markers and morphological factors of primary tumor that may indicate finding a way of pathogenesis of systemic disorder.
METHODS: The current study examined 75 patients who received macroscopic curative resection for pancreatic cancer in our institution as follows: (1) identification of clinical prognostic factors at initial recurrence after resection of primary tumor and (2) analysis of correlations between clinical prognostic factors and histological findings in primary tumor.
RESULTS: Important prognostic factors were peritoneal dissemination and serum levels of carbohydrate antigen 19-9 and cholinesterase. Only low levels of serum cholinesterase correlated to nerve plexus invasion in histological findings of primary tumor. Patients with low cholinesterase levels show systemic disorder, including poor performance status, anemia, and hypoalbuminemia.
CONCLUSIONS: Nerve invasion may thus result in low functional state of the liver followed by systemic disorder. This mechanism may be useful for elucidating cancer cachexia in future studies.
ESTHER : Mitsunaga_2008_Pancreas_36_241
PubMedSearch : Mitsunaga_2008_Pancreas_36_241
PubMedID: 18362836

Title : Removal or maintenance of inositol-linked acyl chain in glycosylphosphatidylinositol is critical in trypanosome life cycle - Hong_2006_J.Biol.Chem_281_11595
Author(s) : Hong Y , Nagamune K , Morita YS , Nakatani F , Ashida H , Maeda Y , Kinoshita T
Ref : Journal of Biological Chemistry , 281 :11595 , 2006
Abstract : The protozoan parasite Trypanosoma brucei is coated by glycosylphosphatidylinositol (GPI)-anchored proteins. During GPI biosynthesis, inositol in phosphatidylinositol becomes acylated. Inositol is deacylated prior to attachment to variant surface glycoproteins in the bloodstream form, whereas it remains acylated in procyclins in the procyclic form. We have cloned a T. brucei GPI inositol deacylase (GPIdeAc2). In accordance with the acylation/deacylation profile, the level of GPIdeAc2 mRNA was 6-fold higher in the bloodstream form than in the procyclic form. Knockdown of GPIdeAc2 in the bloodstream form caused accumulation of an inositol-acylated GPI, a decreased VSG expression on the cell surface and slower growth, indicating that inositol-deacylation is essential for the growth of the bloodstream form. Overexpression of GPIdeAc2 in the procyclic form caused an accumulation of GPI biosynthetic intermediates lacking inositol-linked acyl chain and decreased cell surface procyclins because of release into the culture medium, indicating that overexpression of GPIdeAc2 is deleterious to the surface coat of the procyclic form. Therefore, the GPI inositol deacylase activity must be tightly regulated in trypanosome life cycle.
ESTHER : Hong_2006_J.Biol.Chem_281_11595
PubMedSearch : Hong_2006_J.Biol.Chem_281_11595
PubMedID: 16510441
Gene_locus related to this paper: trybb-q2pg85

Title : Inositol deacylation of glycosylphosphatidylinositol-anchored proteins is mediated by mammalian PGAP1 and yeast Bst1p - Tanaka_2004_J.Biol.Chem_279_14256
Author(s) : Tanaka S , Maeda Y , Tashima Y , Kinoshita T
Ref : Journal of Biological Chemistry , 279 :14256 , 2004
Abstract : The inositol moiety of mammalian glycosylphosphatidylinositol (GPI) is acylated at an early step in GPI biosynthesis. The inositol acylation is essential for the generation of mature GPI capable of attachment to proteins. However, the acyl group is usually absent from GPI-anchored proteins (GPI-APs) on the cell surface due to inositol deacylation that occurs in the endoplasmic reticulum (ER) soon after GPI-anchor attachment. Mammalian GPI inositol-deacylase has not been cloned, and the biological significance of the deacylation has been unclear. Here we report a GPI inositol-deacylase-deficient Chinese hamster ovary cell line established by taking advantage of resistance to phosphatidylinositol-specific phospholipase C and the gene responsible, which was termed PGAP1 for Post GPI Attachment to Proteins 1. PGAP1 encoded an ER-associated, 922-amino acid membrane protein bearing a lipase consensus motif. Substitution of a conserved putative catalytic serine with alanine resulted in a complete loss of function, indicating that PGAP1 is the GPI inositol-deacylase. The mutant cells showed a clear delay in the maturation of GPI-APs in the Golgi and accumulation of GPI-APs in the ER. Thus, the GPI inositol deacylation is important for efficient transport of GPI-APs from the ER to the Golgi.
ESTHER : Tanaka_2004_J.Biol.Chem_279_14256
PubMedSearch : Tanaka_2004_J.Biol.Chem_279_14256
PubMedID: 14734546
Gene_locus related to this paper: human-PGAP1 , ratno-q765a7 , yeast-BST1

Title : Pathophysiology after pylorus-preserving pancreatoduodenectomy: a comparative study of pancreatogastrostomy and pancreatojejunostomy - Konishi_1999_Hepatogastroenterology_46_1181
Author(s) : Konishi M , Ryu M , Kinoshita T , Inoue K
Ref : Hepato-Gastroenterology , 46 :1181 , 1999
Abstract : BACKGROUND/AIMS Pylorus-preserving pancreatoduodenectomy using the pancreatogastrostomy technique may result in pancreatic exocrine insufficiency and obstruction of the pancreatic duct. A prospective randomized comparison of pancreatogastrostomy and pancreatojejunostomy was therefore performed to assess pathophysiologic changes after pylorus-preserving pancreatoduodenectomy. METHODOLOGY: The study population consisted of 23 patients (pancreatogastrostomy: 10, pancreatojejunostomy: 13) who were observed for 2 years. RESULTS: Neither physical condition (dietary intake, body weight, performance status, and frequency of bowel movements) nor nutritional parameters (serum levels of total protein, albumin, total cholesterol, and cholinesterase) differed significantly between the two groups; these parameters recovered to pre-operative levels within 1 year in both groups. Changes in pancreatic function diagnosis (PFD) test results were similar between the two groups. The glucose tolerance test results revealed deterioration of glucose tolerance in 2 patients (20%) in the pancreatogastrostomy group and 3 patients (23%) in the pancreatojejunostomy group. In 2 of 3 patients in each group with non-dilated pancreatic ducts before surgery, the pancreatic ducts dilated after surgery. Diabetes developed after surgery in one such patient in each group. No significant differences were observed between the two groups with respect to changes in glucose tolerance test results and the diameter of the pancreatic duct.
CONCLUSIONS: This prospective randomized study demonstrates no difference in pathophysiologic changes between patients undergoing pancreatogastrostomy or pancreatojejunostomy after pylorus-preserving pancreatoduodenectomy, at least in the first 2 years.
ESTHER : Konishi_1999_Hepatogastroenterology_46_1181
PubMedSearch : Konishi_1999_Hepatogastroenterology_46_1181
PubMedID: 10370688

Title : Histochemical localization of nitric oxide synthase in rat enteric nervous system - Aimi_1993_Neurosci_53_553
Author(s) : Aimi Y , Kimura H , Kinoshita T , Minami Y , Fujimura M , Vincent SR
Ref : Neuroscience , 53 :553 , 1993
Abstract : The localization of nitric oxide synthase, the enzyme responsible for producing the short-acting messenger nitric oxide, has been determined in the digestive tract of the rat using histochemistry for reduced nicotinamide adenine dinucleotide phosphate-diaphorase activity, a specific marker for neuronal nitric oxide synthase. Positively stained neurons were found throughout the entire digestive tract from the esophagus to the rectum. Positive neuronal somata were very common in the myenteric ganglia. Dense positive fibers were distributed in internodal strands, the secondary plexus, the tertiary plexus, and were particularly abundant in the deep muscular plexus, while very few were observed in the submucosal ganglia. The density of these positive structures was higher in the small and large intestine than in the esophagus and stomach. The pattern of distribution suggested that some of these positive cells innervate gut muscles. Double-staining revealed that in these enteric neurons, nitric oxide synthase does not co-localize with acetylcholinesterase. Instead, vasoactive intestinal polypeptide almost always coexists with nitric oxide synthase in the myenteric plexus. Thus, nitric oxide and vasoactive intestinal polypeptide may be co-transmitters in a population of non-adrenergic, non-cholinergic neurons in the enteric nervous system.
ESTHER : Aimi_1993_Neurosci_53_553
PubMedSearch : Aimi_1993_Neurosci_53_553
PubMedID: 7684113