scholarly journals A Rare Branch-Point Mutation Is Associated with Missplicing of Fibrillin-2 in a Large Family with Congenital Contractural Arachnodactyly

1997 ◽  
Vol 60 (6) ◽  
pp. 1389-1398 ◽  
Author(s):  
Cheryl Maslen ◽  
Darcie Babcock ◽  
Michael Raghunath ◽  
Beat Steinmann
Keyword(s):  
Point Mutation ◽  
Branch Point ◽  
Large Family ◽  
Congenital Contractural Arachnodactyly

scholarly journals A trans-acting suppressor restores splicing of a yeast intron with a branch point mutation.

1987 ◽  
Vol 1 (5) ◽  
pp. 445-455 ◽  
Author(s):  
J R Couto ◽  
J Tamm ◽  
R Parker ◽  
C Guthrie
Keyword(s):  
Point Mutation ◽  
Branch Point

A KCNH2 branch point mutation causing aberrant splicing contributes to an explanation of genotype-negative long QT syndrome

Heart Rhythm ◽  
2009 ◽  
Vol 6 (2) ◽  
pp. 212-218 ◽  
Author(s):  
Lia Crotti ◽  
Marzena A. Lewandowska ◽  
Peter J. Schwartz ◽  
Roberto Insolia ◽  
Matteo Pedrazzini ◽  
...  
Keyword(s):  
Point Mutation ◽  
Branch Point ◽  
Long Qt Syndrome ◽  
Aberrant Splicing ◽  
Long Qt ◽  
Qt Syndrome

scholarly journals A point mutation in the lariat branch point of intron 6 ofNPC1 as the cause of abnormal pre-mRNA splicing in Niemann-Pick type C disease

2004 ◽  
Vol 24 (5) ◽  
pp. 440-440 ◽  
Author(s):  
Enza Di Leo ◽  
Francesca Panico ◽  
Patrizia Tarugi ◽  
Carla Battisti ◽  
Antonio Federico ◽  
...  
Keyword(s):  
Point Mutation ◽  
Branch Point ◽  
Mrna Splicing ◽  
Type C ◽  
Niemann Pick

Ectodermal dysplasia with immunodeficiency caused by a branch-point mutation in IKBKG/NEMO

2016 ◽  
Vol 138 (6) ◽  
pp. 1706-1709.e4 ◽  
Author(s):  
Sofie E. Jørgensen ◽  
Pernille Bøttger ◽  
Emil Kofod-Olsen ◽  
Mette Holm ◽  
Nanna Mørk ◽  
...  
Keyword(s):  
Point Mutation ◽  
Branch Point ◽  
Ectodermal Dysplasia

Lariat branch point mutation in the dysferlin gene with mild limb-girdle muscular dystrophy

Neurology ◽  
2006 ◽  
Vol 66 (7) ◽  
pp. 1114-1116 ◽  
Author(s):  
Michael Sinnreich ◽  
Christian Therrien ◽  
George Karpati
Keyword(s):  
Muscular Dystrophy ◽  
Point Mutation ◽  
Branch Point ◽  
Null Allele ◽  
Exon Skipping ◽  
Limb Girdle Muscular Dystrophy ◽  
Compound Heterozygous ◽  
Null Mutation ◽  
Phenotype Correlation ◽  
Mild Phenotype

The authors report a genotype-phenotype correlation in a limb-girdle muscular dystrophy 2B family. Two severely affected sisters were homozygous for a dysferlin null mutation. Their mildly affected compound heterozygous mother harbored, in addition to one null allele, an in-frame exon-skipping allele caused by a novel lariat branch point mutation. The dysferlin molecule arising from the latter allele appeared to partially complement the null mutation, likely accounting for the mother's mild phenotype.

Crystal chemistry of high-Tc superconductors

1990 ◽  
Vol 48 (4) ◽  
pp. 1118-1119
Author(s):  
Maryvonne Hervieu
Keyword(s):  
Oxygen Deficiency ◽  
Large Family ◽  
Copper Oxides ◽  
High Tc Superconductors ◽  
High Tc ◽  
Single Mechanism ◽  
Square Planar ◽  
History Of ◽  
Bismuth Cuprates ◽  
New Compounds

Four years after the discovery of superconductivity at high temperature in the Ba-La-Cu-O system, more than thirty new compounds have been synthesized, which can be classified in six series of copper oxides: La2CuO4 - type oxides, bismuth cuprates, YBa2Cu3O7 family, thallium cuprates, lead cuprates and Nd2CuO4 - type oxides. Despite their quite different specific natures, close relationships allow their structures to be simply described through a single mechanism. The fifth first families can indeed be described as intergrowths of multiple oxygen deficient perovskite slabs with multiple rock salt-type slabs, according to the representation [ACuO3-x]m [AO]n.The n and m values are integer in the parent structures, n varying from 0 to 3 and m from 1 to 4; every member of this large family can thus be symbolized by [m,n]. The oxygen deficient character of the perovskite slabs involves the existence or the co-existence of several types of copper environment: octahedral, pyramidal and square planar.Both mechanisms, oxygen deficiency and intergrowth, are well known to give rise easily to nonstoichiometry phenomena. Numerous and various phenomena have actually been characterized in these cuprates, strongly depending on the thermal history of the samples.

Paris I Dysfibrinogenemia: A Point Mutation in Intron 8 Results in Insertion of a 15 Amino Acid Sequence in the Fibrinogen γ-Chain

1993 ◽  
Vol 69 (03) ◽  
pp. 217-220 ◽  
Author(s):  
Jonathan B Rosenberg ◽  
Peter J Newman ◽  
Michael W Mosesson ◽  
Marie-Claude Guillin ◽  
David L Amrani
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Point Mutation ◽  
Genomic Dna ◽  
Comparative Sequence Analysis ◽  
Chain Gene ◽  
Molecular Defect ◽  
Nucleotide Position ◽  
Normal Individuals ◽  
Polymerase Chain

SummaryParis I dysfibrinogenemia results in the production of a fibrinogen molecule containing a functionally abnormal γ-chain. We determined the basis of the molecular defect using polymerase chain reaction (PCR) to amplify the γ-chain region of the Paris I subject’s genomic DNA. Comparative sequence analysis of cloned PCR segments of normal and Paris I genomic DNA revealed only an A→G point mutation occurring at nucleotide position 6588 within intron 8 of the Paris I γ-chain gene. We examined six normal individuals and found only normal sequence in this region, indicating that this change is not likely to represent a normal polymorphism. This nucleotide change leads to a 45 bp fragment being inserted between exons 8 and 9 in the mature γparis I chain mRNA, and encodes a 15 amino acid insert after γ350 [M-C-G-E-A-L-P-M-L-K-D-P-C-Y]. Alternative splicing of this region from intron 8 into the mature Paris I γ-chain mRNA also results after translation into a substitution of S for G at position γ351. Biochemical studies of 14C-iodoacetamide incorporation into disulfide-reduced Paris I and normal fibrinogen corroborated the molecular biologic predictions that two additional cysteine residues exist within the γpariS I chain. We conclude that the insertion of this amino acid sequence leads to a conformationallyaltered, and dysfunctional γ-chain in Paris I fibrinogen.

Skeletal and bone material phenotype in recessive osteogenesis imperfecta due to a novel homozygous point mutation in TMEM38B

2015 ◽  
Author(s):  
Emma Webb ◽  
Meena Balasubramanian ◽  
Trevor Cole ◽  
Sue Stewart ◽  
Nicola Crabtree ◽  
...  
Keyword(s):  
Osteogenesis Imperfecta ◽  
Point Mutation ◽  
Bone Material
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