 | Thuluvancheri K MohandasDepartment of Pathology, Dartmouth Medical School Lebanon, New Hampshire | Department of Pathology, Dartmouth‐Hitchcock Medical Center, Lebanon, NH, USA | Department of ... |
Is this your profile? Claim your profile Copy URL Embed Link to your profile |
Thuluvancheri K Mohandas:Expert Impact
Concepts for whichThuluvancheri K Mohandashas direct influence:Human chromosome,Human pair,Short arm,Situ hybridization,Chromosomes human,Human chromosomes,Human genes,Hybrid cells.
Thuluvancheri K Mohandas:KOL impact
Concepts related to the work of other authors for whichfor which Thuluvancheri K Mohandas has influence:Dna methylation,Gene expression,Situ hybridization,Human chromosome,Tyrosine kinase,Amino acid,Lipoprotein lipase.
KOL Resume for Thuluvancheri K Mohandas
| Year | |
|---|---|
| 2002 | Department of Pathology, Dartmouth Medical School Lebanon, New Hampshire |
| 2001 | Department of Pathology, Dartmouth‐Hitchcock Medical Center, Lebanon, NH, USA |
| 2000 | Department of Pathology, Dartmouth-Hitchcock Medical Center, Lebanon, NH, USA |
| 1999 | Department of Pathology, Dartmouth-Hitchcock Medical Center, Lebanon, New Hampshire 03756 |
| 1998 | Department of Pathology, Dartmouth Medical School, Lebanon, New Hampshire, 03756 |
| 1997 | Dartmouth Medical School, Hanover NH;, Department of Pathology and, Department of Medicine, Division of Endocrinology and Metabolism Lahey-Hitchcock Clinic, Lebanon NH (USA) |
| 1996 | Department of Pathology, Darmouth Medical School, 03755, Hanover, New Hampshire, USA |
| 1994 | Division of Medical Genetics, Harbor‐UCLA Medical Center, Torrance, California 90502 |
| 1993 | Renal Division, Brigham and Women's Hospital and Harvard Medical School, Boston, Massachusetts 02115, and Division of Medical Genetics, Harbor-UCLA Medical Center, Torrance, California 90509 Department of Microbiology and Molecular Genetics, Department of Medicine, and Molecular Biology Institute, University of California, Los Angeles, California 90024; Howard Hughes Medical Institute, Eukaryotic Regulatory Biology Program, University of California at San Diego School of Medicine, 9500 Gillman Drive, La Jolla, California 92093-0648; and Division of Medical Genetics, Harbor UCLA Medical Center, Torrance, California 90502 |
| 1992 | Department of Pediatrics, UCLA School of Medicine, Harbor-UCLA Medical Center, Torrance, California 90509 USA |
| 1991 | Division of Medical Genetics, Harbor-UCLA Medical Center, Torrance, California USA Howard Hughes Medical Institute, University of California, Los Angeles |
| 1990 | ZMBH, University of Heidelberg, FRG Howard Hughes Medical Institute Laboratories, Departments of Pediatrics and Biological Chemistry, UCLA School of Medicine and the Division of Medical Genetics, Harbor/UCLA Medical CenterTorrance, CA 90509, USA Mental Retardation Research Center, UCLA Medical School, Los Angeles, California, U.S.A. |
| 1989 | Department of Biological Chemistry, University of California, School of Medicine, Los Angeles 90024-1737. Howard Hughes Medical Institute Laboratories, University of California, Los Angeles. Division of Medical Genetics, Harbor General Hospital, Torrance, California 90509 |
| 1988 | Department of Pediatrics, Harbor-UCLA Medical Center, Torrance, CA 90509. Division of Medical Genetics, Harbor-UCLA Medical Center, Torrance, California 90502 USA |
| 1987 | Harbor UCLA Medical Center, Los Angeles, CA 90509 Department of Medicine, The University of Sydney, Sydney, Department of Medicine, The University of Sydney, Concord Hospital, Concord, Division of Medical Genetics, UCLA Medical Center, Torrance, CA, and, Molecular Biology and Hypertension Laboratory, Department of Physiology, The University of Sydney, Sydney |
| 1986 | Departments of Pediatrics, Harbor‐UCLA Medical Center, Torrance, California |
| 1985 | Division of Medical Genetics, Harbor‐UCLA Medical Center, 1000 W. Carson Street, Torrance, CA 90509 |
| 1984 | Division of Medical Genetics, Department of Pediatrics, University of California, Los Angeles Harbor-UCLA Medical Center, 90509, Torrance, California |
| 1983 | Division of Medical Genetics E‐4, Harbor‐UCLA Medical Center, Torrance, California |
| 1982 | Division of Medical Genetics, Harbor–UCLA Medical Center, 90509, Torrance, California, USA |
| 1981 | Division of Medical Genetics, Department of Pediatrics, Harbor-University of California Medical Center, Torrance 90509 |
| 1980 | Divisions of Medical Genetics and Hematology, Harbor-UCLA Medical Center, Torrance, California, USA Division of Medical Genetics, Department of Pediatrics, Harbor-UCLA Medical Center, Torrance, and, Division of Medical Genetics, Departments of Pediatrics, Medicine and Psychiatry, UCLA Center for the Health Sciences, Los Angeles, Calif. |
| 1979 | Division of Medical Genetics, Department of Pediatrics, UCLA-Harbor General Hospital, 90509, Torrance, California |
| 1978 | Division of Medical Genetics, Department of Pediatrics, UCLA—Harbor General Hospital, Torrance, CA 90509, USA |
| 1977 | Departments of Pediatrics and Medicine, U.C.L.A. School of Medicine, Division of Medical Genetics, Harbor General Hospital, Torrance |
| Concept | World rank |
|---|---|
| 11 25 women | #1 |
| duchenne sts | #1 |
| locus exceptions | #1 |
| short arm hc16 | #1 |
| lesions retinal degeneration | #1 |
| greater clinical practice | #1 |
| short arm distal | #1 |
| hybrid cells 5azacytidine | #1 |
| long arm hc16 | #1 |
| localization ak1 | #1 |
| thatzfx | #1 |
| recx g6pd | #1 |
| t615cenpl3 glo | #1 |
| hprt expression cells | #1 |
| hc16 genes | #1 |
| hc16q hybrid cells | #1 |
| qualitative polymorphisms | #1 |
| sterolsulfate sulfohydrolase | #1 |
| gla 62 clones | #1 |
| pediatric practice advances | #1 |
| area human cytogenetics | #1 |
| hb class subunits | #1 |
| hypothesis translocations | #1 |
| g6pd recx | #1 |
| 17yearold white male | #1 |
| recx duplication | #1 |
| technique dnamediated transformation | #1 |
| hprt transformants dna | #1 |
| s14 cultured breast | #1 |
| recx chromosome | #1 |
| genetic chromosome mammalian | #1 |
| sts locus inactivation | #1 |
| phosphoglycollate | #1 |
| aldehyde chromosomal assignment | #1 |
| enamelin amelogenin classes | #1 |
| p25q112 | #1 |
| homologous sequences xp | #1 |
| 1550base pair | #1 |
| markers sts | #1 |
| sts deficient patients | #1 |
| human chromosome humans | #1 |
| human chromosome aldh2 | #1 |
| frequent deletions recombination | #1 |
| human diseases xp223 | #1 |
| mll amplification mll | #1 |
| expression human pgm3 | #1 |
| Sign-in to see all concepts, it's free! | |
Prominent publications by Thuluvancheri K Mohandas
We report the regional mapping of human chromosome 19 genes for three apolipoproteins and a lipoprotein receptor as well as genes for three other markers. The regional mapping was made possible by the use of a reciprocal whole-arm translocation between the long arm of chromosome 19 and the short arm of chromosome 1. Examination of three separate somatic cell hybrids containing the long arm but not the short arm of chromosome 19 indicated that the genes for apolipoproteins CI, CII, and E ...
| Known for Human Chromosome | Long Arm | Regional Mapping | Apoc2 Apoe | 19 Genes |
Intestinal fatty acid binding protein (I-FABP) is believed to participate in the uptake, intracellular metabolism, and/or transport of long chain fatty acids within enterocytes. The 15.1-kDA rodent proteins is a member of a family of low Mr cytoplasmic proteins that have evolved to bind different ligands. We have now determined the nucleotide sequence of the gene encoding human I-FABP and defined the primary structure of its protein product. The human I-FABP gene spans 3382 nucleotides ...
| Known for Acid Binding | Intestinal Fatty | Human Pair | Mouse Chromosome | Protein Genes |
Human Gastric Cathepsin E Predicted Sequence, Localization to Chromosome 1, and Sequence Homology with other Aspartic Proteinases*
[ PUBLICATION ]
The predicted sequence of human gastric cathepsin E (CTSE) was determined by analysis of cDNA clones isolated from a library constructed with poly(A+) RNA from a gastric adenocarcinoma cell line. The CTSE cDNA clones were identified using a set of complementary 18-base oligonucleotide probes specific for a 6-residue sequence surrounding the first active site of all previously characterized human aspartic proteinases. Sequence analysis of CTSE cDNA clones revealed a 1188-base pair open ...
| Known for Aspartic Proteinases | Human Gastric | Sequence Homology | Cdna Clones | Active Site |
Human genes involved in lipolysis of plasma lipoproteins: Mapping of loci for lipoprotein lipase to 8p22 and hepatic lipase to 15q21
[ PUBLICATION ]
We have used cDNA probes for lipoprotein lipase and hepatic lipase to determine the chromosomal and subchromosomal locations of the human genes for these lipolytic enzymes. Southern blot analysis of genomic DNA from 17 independent mouse-human somatic cell hybrids demonstrated the presence of the gene for human lipoprotein lipase on chromosome 8, whereas the gene for hepatic lipase was on chromosome 15. Regional mapping of the genes by in situ hybridization to human chromosomes indicated ...
| Known for Hepatic Lipase | Plasma Lipoproteins | Chromosome Gene | Human Lipoprotein | Situ Hybridization |
Conversion of cholesterol to pregnenolone is mediated by P450scc [cholesterol, reduced-adrenal-ferrodoxin: oxygen oxidoreductase (side-chain-cleaving), EC 1.14.15.67]. RNA from several human adrenal samples was translated in vitro and immunoprecipitated with anti-bovine P450scc, indicating that P450scc mRNA represents about 0.5% of human adrenal mRNA in normal, hypertrophied, and malignant adrenals. A 1626-base-pair human adrenal P450scc cDNA was cloned in bacteriophage lambda gt10. ...
| Known for Cdna Cloning | Chain Cleavage | Human P450scc | Chromosome 15 | Sequence Cholesterol |
The expression of steroid sulfatase (SS; sterol-sulfatase; sterol-sulfate sulfohydrolase, EC 3.1.6.2), a microsomal enzyme that catalyzes the hydrolysis of a variety of 3beta-hydroxysteroid sulfates, was evaluated in mouse-human hybrid clones. The mouse parental line, A9, was found to have little SS as determined by activity measurements. Human SS can be separated from mouse SS by electrophoresis. Two human fibroblast lines, one carrying an X/13 translocation [46,X,t(X;13)(p22;q12)] and ...
| Known for Short Arm | Steroid Sulfatase | Regional Assignment | Human Chromosome | Linked Ichthyosis |
Cloning and chromosomal localization of a human kidney cDNA involved in cystine, dibasic, and neutral amino acid transport.
[ PUBLICATION ]
We have recently cloned, sequenced, and characterized a rat kidney cDNA (D2) that stimulates cystine as well as dibasic and neutral amino acid transport. In order to evaluate the role of this protein in human inherited diseases such as cystinuria, we have isolated a human D2 clone (D2H) by low stringency screening of a human kidney cDNA library using the radiolabeled D2 insert as a probe. The D2H cDNA is 2284 nucleotides long and encodes a 663 amino acid protein that is 80% identical to ...
| Known for Acid Transport | Human Kidney | Neutral Amino | Chromosomal Localization | Pair 2 Cloning |
Acyl-CoA:cholesterol acyltransferase (ACAT) plays important roles in cellular cholesterol homeostasis. Four human ACAT-1 mRNAs (7.0, 4.3, 3.6, and 2.8 kilobases (kb)) share the same short 5'-untranslated region (exon 1) and coding sequence (exons 2-15). The 4.3-kb mRNA contains an additional 5'-untranslated region (1289 nucleotides in length; exons Xa and Xb) immediately upstream from the exon 1 sequence. One ACAT-1 genomic DNA insert covers exons 1-16 and a promoter (the P1 promoter). A ...
| Known for Cholesterol Acyltransferase | Chromosomes Human | Genetic Rna | Chromosome Exon | Promoter Regions |
Two cDNAs encoding variants (alpha 1 and alpha 2) of the strychnine binding subunit of the inhibitory glycine receptor (GlyR) were isolated from a human fetal brain cDNA library. The predicted amino acid sequences exhibit approximately 99% and approximately 76% identity to the previously characterized rat 48 kd polypeptide. Heterologous expression of the human alpha 1 and alpha 2 subunits in Xenopus oocytes resulted in the formation of glycine-gated strychnine-sensitive chloride ...
| Known for Human Glycine | Functional Expression | Alpha Subunit | Chromosomal Localization | Rats Receptors |
Regional assignment of genes for human α-globin and phosphoglycollate phosphatase to the short arm of chromosome 16
[ PUBLICATION ]
The human alpha-globin and phosphoglycollate phosphatase (EC 3.1.3.18) genes have been regionally localized to the short arm of human chromosome 16 (HC16). This was accomplished by fusing mouse fibroblasts (A9) to human fibroblasts that contain a reciprocal translocation between the long arms of chromosomes 16 and 11. The murine A9 cells are deficient in adenine phosphoribosyltransferase (APRT), an enzyme present on the long arm of HC16 (HC16q). Hybrid cells were grown in selection ...
| Known for Short Arm | Chromosome 16 | Hybrid Cells | Human Α | Globin Genes |
Regulation of rat liver 3-hydroxy-3-methylglutaryl coenzyme A synthase and the chromosomal localization of the human gene.
[ PUBLICATION ]
3-Hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) synthase was purified to homogeneity from rat liver cytoplasm. The active enzyme is a dimer composed of identical subunits of Mr = 53,000. The amino acid composition and the NH2-terminal sequence are presented. Partial cDNA clones for the enzyme were isolated by screening of a rat liver lambda gt11 expression library with antibodies raised against the purified protein. The identity of the clones was confirmed by hybrid selection and ...
| Known for Rat Liver | Methylglutaryl Coenzyme | Cholestyramine Mevinolin | Coa Synthase | Messenger Transcription |
Human Aromatase: cDNA Cloning, Southern Blot Analysis, and Assignment of the Gene to Chromosome 15
[ PUBLICATION ]
The amino acid sequence of human placental aromatase was determined in part (about 40%) by microsequencing methods. Using a region of overlapping peptide sequences, synthetic oligonucleotide probes were constructed and used to screen a human placental lambda gt-11 cDNA library. Of a number of positive clones, one containing a 2.4-kb insert was characterized further by restriction mapping and determination of its nucleotide sequence. The cDNA-deduced amino acid sequence is in perfect ...
| Known for Human Aromatase | Pair Cloning | Chromosome 15 | Nucleotide Sequence | Blot Analysis |
Steroid sulphatase (STS) Is an important enzyme in steroid metabolism1. The human STS gene has been cloned and mapped to Xp22.3, proximal to the pseudoautosomal region (PAR)2. Using quantitative differences in STS activity among various mouse strains, a segregation pattern consistent with autosomal linkage was first reported3–5, but more recent studies have linked Ste to the mouse PAR6–11. Failed attempts to clone the mouse Sfs gene using human reagents (STS cDNA and anti-STS antibodies) ...
| Known for Steroid Sulphatase | Mouse Pseudoautosomal | Sts Cdna | Sequence Chromosome | Mice Inbred |
Paternally derived de novo interstitial duplication of proximal 15q in a patient with developmental delay
[ PUBLICATION ]
Interstitial duplications of proximal 15q containing the Prader-Willi syndrome/Angelman syndrome (PWS/AS) region have been found in patients with autism or atypical autism. In these cases with an abnormal phenotype, the duplications were maternally derived. Paternal origin of the duplication has been associated with a normal phenotype. We report on a patient who presented with nonspecific developmental delay and partial agenesis of the rostral corpus callosum. Fluorescence in situ ...
| Known for Proximal 15q | Interstitial Duplication | Developmental Delay | Pws Region | Situ Hybridization |
Differential expression of steroid sulphatase locus on active and inactive human X chromosome
[ PUBLICATION ]
The X chromosome in mammalian somatic cells is subject to unique regulation—usually genes on a single X chromosome are expressed while those on other X chromosomes are inactivated1. The X-locus for steroid sulphatase (STS; EC 3.1.6.2), the microsomal enzyme that catalyses the hydrolysis of various 3β-hydroxysteroid sulphates, is exceptional because it seems to escape inactivation. Evidence for this comes from fibroblast clones in females heterozygous for mutations that result in a severe ...
| Known for Steroid Sulphatase | Sts Locus | Fibroblast Clones | Human Chromosome | Male Pedigree |
