Functional inactivation of genes by dominant negative mutations.
about
Two classes of human papillomavirus type 16 E1 mutants suggest pleiotropic conformational constraints affecting E1 multimerization, E2 interaction, and interaction with cellular proteinsGlucocorticoid receptor beta, a potential endogenous inhibitor of glucocorticoid action in humansCharacterization of a novel 350-kilodalton nuclear phosphoprotein that is specifically involved in mitotic-phase progressionTFII-I regulates Vbeta promoter activity through an initiator elementIsolated 3-methylcrotonyl-CoA carboxylase deficiency: evidence for an allele-specific dominant negative effect and responsiveness to biotin therapyA mechanism for ATP-sensitive potassium channel diversity: Functional coassembly of two pore-forming subunitsWidely dispersed p53 mutation in respiratory epithelium. A novel mechanism for field carcinogenesisA base mutation of the C-erbA beta thyroid hormone receptor in a kindred with generalized thyroid hormone resistance. Molecular heterogeneity in two other kindredsHuman piebald trait resulting from a dominant negative mutant allele of the c-kit membrane receptor geneCharacterization of seven novel mutations of the c-erbA beta gene in unrelated kindreds with generalized thyroid hormone resistance. Evidence for two "hot spot" regions of the ligand binding domainA dominant negative mutation of the alpha retinoic acid receptor gene in a retinoic acid-nonresponsive embryonal carcinoma cellPosttranslational regulation of keratins: degradation of mouse and human keratins 18 and 8Protein sequestration generates a flexible ultrasensitive response in a genetic networkRegulation of cytoplasmic dynein function in vivo by the Drosophila Glued complexDominant negative and loss of function mutations of the c-kit (mast/stem cell growth factor receptor) proto-oncogene in human piebaldismCalcium-sensing receptor mutations in familial benign hypercalcemia and neonatal hyperparathyroidismProlidase deficiency: biochemical classification of allelesThe molecular genetics of Marfan syndrome and related microfibrillopathiesLarge-scale exploration of growth inhibition caused by overexpression of genomic fragments in Saccharomyces cerevisiaeHfq variant with altered RNA binding functionsUsing large-scale genomics data to identify driver mutations in lung cancer: methods and challengesMAPping the Ndc80 loop in cancer: A possible link between Ndc80/Hec1 overproduction and cancer formationGene overexpression: uses, mechanisms, and interpretationAltered nucleotide-microtubule coupling and increased mechanical output by a kinesin mutantThe C-terminal domain of Nrf1 negatively regulates the full-length CNC-bZIP factor and its shorter isoform LCR-F1/Nrf1β; both are also inhibited by the small dominant-negative Nrf1γ/δ isoforms that down-regulate ARE-battery gene expressionTransgenic mouse model of the mild dominant form of osteogenesis imperfectaAtomic structure of a thermostable subdomain of HIV-1 gp41A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiaeInteractions among Ytm1, Erb1, and Nop7 required for assembly of the Nop7-subcomplex in yeast preribosomes.Pkh1 and Pkh2 differentially phosphorylate and activate Ypk1 and Ykr2 and define protein kinase modules required for maintenance of cell wall integrity.The splicing factor PRP2, a putative RNA helicase, interacts directly with pre-mRNASQT1, which encodes an essential WD domain protein of Saccharomyces cerevisiae, suppresses dominant-negative mutations of the ribosomal protein gene QSR1.The splicing factor Prp43p, a DEAH box ATPase, functions in ribosome biogenesis.An ARL1 mutation affected autophagic cell death in yeast, causing a defect in central vacuole formation.Reversible transdominant inhibition of a metabolic pathway. In vivo evidence of interaction between two sequential tricarboxylic acid cycle enzymes in yeast.Separation-of-function mutations in Saccharomyces cerevisiae MSH2 that confer mismatch repair defects but do not affect nonhomologous-tail removal during recombination.The majority of yeast UPF1 co-localizes with polyribosomes in the cytoplasm.Vesicle-mediated protein transport: regulatory interactions between the Vps15 protein kinase and the Vps34 PtdIns 3-kinase essential for protein sorting to the vacuole in yeastThe protein kinase homologue Ste20p is required to link the yeast pheromone response G-protein beta gamma subunits to downstream signalling components.Comprehensive mutational analysis of yeast DEXD/H box RNA helicases required for small ribosomal subunit synthesis.
P2860
Q24317609-C6F60154-4D62-4C42-B093-36930AB7CC6AQ24320334-FCACBE3A-E967-4747-91A8-534E8E03B469Q24336046-2944D387-FB12-481D-9312-44903DFFD15EQ24522578-38AD375B-803F-4F08-98F4-798439C7AB3EQ24534070-3660CAFB-359F-4CD0-A0E0-90899517A7AAQ24544449-513C9B7E-FB93-4ADD-B9AD-B9BB039784C1Q24561466-CAEDF210-0FA4-4B8B-AAF3-EE83EB2316D1Q24624938-C9103B8F-EB55-4291-8E69-ADAA00F91CDDQ24629192-1F5B2328-8F17-49FF-8BE4-C7F21316B577Q24629530-8D6CA747-E690-4B94-959D-9DE9CA1EE997Q24633328-6502F9FC-A983-433A-B54E-D6A74BDDDE33Q24634036-1C4BBD25-755D-41CF-BFB2-CEFA7686C3A3Q24647718-82524ABE-A2C2-485B-8BF9-06AED28AA3A3Q24651482-E08E5A0C-F93A-4B6C-92CB-9DF89577B9A3Q24670459-5BFE4EA9-1588-4951-8C3F-E002F7FFB0FAQ24677024-8A88BC01-0F47-4E74-8F17-A75B3F025D02Q24679050-EBB039AF-772E-4C3C-A136-A5C56553F3EBQ24681593-7986628E-C78D-4C91-934C-14B5C7F3823CQ24801836-F8AE2702-3213-4F05-8010-5666ED3837C9Q25257777-DA15FDA2-D316-41C0-8EF0-16EB174CD511Q26800833-CAE65A6F-FAD9-4399-B7BA-F5D580FC9211Q26991530-0802EDA3-3EC5-43D5-8621-4AFB216DCC40Q27001204-427A9A3E-88D9-4B5F-AD7E-377BBF504609Q27315014-35EFDF80-198B-4AF5-A673-EA6CAF0C1072Q27341433-E345BF31-47F3-4A14-B523-85A7C75DA4F8Q27469188-C43863E0-A9B4-41AC-ADD5-8C5941891638Q27746904-C53CCE37-E490-4C15-87DE-C1EB3ADE025BQ27860636-6FAD1894-F98D-4EEF-95AA-88ADA5DB2D3BQ27930239-29F6D3E9-F753-4FA5-B180-64A9FD0E4D48Q27930976-262981BA-DC6F-4593-8C2A-A1DFD83C6C27Q27931001-281F4B13-CE0A-4059-AF7D-FA64DDB33F4EQ27933742-5D8C9924-31D6-4504-8911-4B327DC4DD2AQ27934180-BCC40058-AC10-4843-BD9D-B3D764FC1B8CQ27935440-1D27DA45-ACF8-4950-AC7B-96A69507866CQ27937832-2C5F7AA2-25ED-4CEC-81C2-34E5FAE030F8Q27938377-BC956A54-1C66-429C-B745-0AC601E1A54DQ27938663-95504B55-EC52-4249-92D8-1441D9C9E8F4Q27938850-E0120B8A-C7EB-433A-ADA8-3456D095FA7DQ27939092-D40A0625-ECF9-4074-9EF3-3D0A5F111EAFQ27939616-A3A46DF3-C987-4311-85B8-AF3FA635BCBD
P2860
Functional inactivation of genes by dominant negative mutations.
description
article científic
@ca
article scientifique
@fr
articol științific
@ro
articolo scientifico
@it
artigo científico
@gl
artigo científico
@pt
artigo científico
@pt-br
artikel ilmiah
@id
artikull shkencor
@sq
artículo científico
@es
name
Functional inactivation of genes by dominant negative mutations.
@en
type
label
Functional inactivation of genes by dominant negative mutations.
@en
prefLabel
Functional inactivation of genes by dominant negative mutations.
@en
P356
P1433
P1476
Functional inactivation of genes by dominant negative mutations.
@en
P2093
Herskowitz I
P2888
P304
P356
10.1038/329219A0
P407
P577
1987-09-01T00:00:00Z
P6179
1005321784