8 Congenital dyserythropoietic anaemia type II (HEMPAS) and its molecular basis

1993 ◽  
Vol 6 (2) ◽  
pp. 493-511 ◽  
Author(s):  
Michiko N. Fukuda
Keyword(s):  
Molecular Basis ◽  
Type Ii

The Molecular Basis of Antithrombin Deficiency in Belgian and Dutch Families

1998 ◽  
Vol 80 (09) ◽  
pp. 376-381 ◽  
Author(s):  
W. Lissens ◽  
S. Seneca ◽  
P. Capel ◽  
B. Chatelain ◽  
P. Meeus ◽  
...  
Keyword(s):  
Molecular Basis ◽  
Gene Deletion ◽  
Direct Sequencing ◽  
Genetic Defect ◽  
Polymorphism Analysis ◽  
Type I ◽  
Type Ii ◽  
Antithrombin Deficiency ◽  
Venous Thromboembolic Events ◽  
At Deficiency

SummaryThe molecular basis of hereditary antithrombin (AT) deficiency has been investigated in ten Belgian and three Dutch unrelated kindreds. Eleven of these families had a quantitative or type I AT deficiency, with a history of major venous thromboembolic events in different affected members. In the other two families a qualitative or type II AT deficiency was occasionally diagnosed.DNA studies of the AT gene were performed, using polymerase chain reaction single-strand conformation polymorphism (PCR-SSCP) analysis, followed by direct sequencing of the seven exons and intronexon junction regions. Six novel point mutations were identified: four missense, one nonsense mutation and a single nucleotide deletion near the reactive site, causing a frameshift with premature translation termination. In two kindreds the underlying genetic defect was caused by a whole gene deletion, known as a rare cause of AT deficiency. In these cases, Southern blot and polymorphism analysis of different parts of the AT gene proved useful for diagnosis. In another kindred a partial gene deletion spanning 698 basepairs could precisely be determined to a part of intron 3B and exon 4. In two type I and in both type II AT deficient families a previously reported mutation was identified. In all cases, the affected individuals were heterozygous for the genetic defect.

Vitamin D-dependent rickets type II: Studies of the molecular basis of the disease using cultured skin fibroblasts

Bone ◽  
1985 ◽  
Vol 6 (1) ◽  
pp. 55-56
Author(s):  
L.J. Fraher ◽  
G.N. Hendy ◽  
H. Jani ◽  
L. Nicholson ◽  
F.R.J. Hinde ◽  
...  
Keyword(s):  
Vitamin D ◽  
Molecular Basis ◽  
Skin Fibroblasts ◽  
Type Ii ◽  
Cultured Skin

scholarly journals Further study of chromosome 7p22 to identify the molecular basis of familial hyperaldosteronism type II

2010 ◽  
Vol 25 (9) ◽  
pp. 560-564 ◽  
Author(s):  
K J Carss ◽  
M Stowasser ◽  
R D Gordon ◽  
K M O'Shaughnessy
Keyword(s):  
Molecular Basis ◽  
Type Ii ◽  
Familial Hyperaldosteronism

1.2 Molecular basis for hypertension in the type II variant of apparent mineralocorticoid excess

1997 ◽  
Vol 15 (12) ◽  
pp. 1529-1530
Author(s):  
A Li ◽  
R Tedde ◽  
M Palermo ◽  
C H.L. Shackleton ◽  
P M. Stewart
Keyword(s):  
Molecular Basis ◽  
Type Ii ◽  
Apparent Mineralocorticoid Excess

scholarly journals The Molecular Basis for Hereditary Porcine Membranoproliferative Glomerulonephritis Type II

2002 ◽  
Vol 161 (6) ◽  
pp. 2027-2034 ◽  
Author(s):  
Guido A. Hegasy ◽  
Tamara Manuelian ◽  
Kolbjorn Hogasen ◽  
Johan H. Jansen ◽  
Peter F. Zipfel
Keyword(s):  
Molecular Basis ◽  
Membranoproliferative Glomerulonephritis ◽  
Type Ii

A large Alu -mediated deletion, identified by PCR, as the molecular basis for glycogen storage disease Type II (GSDII)

1999 ◽  
Vol 104 (1) ◽  
pp. 94-98 ◽  
Author(s):  
M. L. Huie ◽  
A. L. Shanske ◽  
J. S. Kasper ◽  
R. W. Marion ◽  
R. Hirschhorn
Keyword(s):  
Glycogen Storage Disease ◽  
Molecular Basis ◽  
Storage Disease ◽  
Glycogen Storage Disease Type ◽  
Glycogen Storage ◽  
Disease Type ◽  
Type Ii

scholarly journals Cryo-EM reveals unique structural features of the FhuCDB Escherichia coli ferrichrome importer

2021 ◽  
Vol 4 (1) ◽  
Author(s):  
Wenxin Hu ◽  
Hongjin Zheng
Keyword(s):  
Electron Microscopy ◽  
Escherichia Coli ◽  
Molecular Basis ◽  
Iron Uptake ◽  
Structural Features ◽  
Biological Processes ◽  
Type Ii ◽  
Functional Studies ◽  
Cryo Electron Microscopy ◽  
Translocation Pathway

AbstractAs one of the most elegant biological processes developed in bacteria, the siderophore-mediated iron uptake demands the action of specific ATP-binding cassette (ABC) importers. Although extensive studies have been done on various ABC importers, the molecular basis of these iron-chelated-siderophore importers are still not fully understood. Here, we report the structure of a ferrichrome importer FhuCDB from Escherichia coli at 3.4 Å resolution determined by cryo electron microscopy. The structure revealed a monomeric membrane subunit of FhuB with a substrate translocation pathway in the middle. In the pathway, there were unique arrangements of residues, especially layers of methionines. Important residues found in the structure were interrogated by mutagenesis and functional studies. Surprisingly, the importer’s ATPase activity was decreased upon FhuD binding, which deviated from the current understanding about bacterial ABC importers. In summary, to the best of our knowledge, these studies not only reveal a new structural twist in the type II ABC importer subfamily, but also provide biological insights in the transport of iron-chelated siderophores.

scholarly journals A global analytical molecular pharmacological study of the endocrinological pharmacotherapeutic rationale of anti-diabetic prescriptions appraisal attributes for metformin and sitagliptin, with evaluation of anti-diabetic tertiary medical healthcare patient satisfaction

2021 ◽  
Vol 10 (12) ◽  
pp. 1391
Author(s):  
Moumita Hazra
Keyword(s):  
Patient Satisfaction ◽  
Combination Therapy ◽  
Molecular Basis ◽  
Pharmacological Study ◽  
Dipeptidyl Peptidase ◽  
Type Ii ◽  
Dipeptidyl Peptidase 4 ◽  
Dipeptidyl Peptidase 4 Inhibitors ◽  
Type Ii Diabetics ◽  
Medical Healthcare

Background: The inhibition of dipeptidyl peptidase-4 by anti-diabetic drugs dipeptidyl peptidase-4 inhibitors enhances hormonal activity of incretins (GLP-1, GIP, GRP), stimulates insulin release and reduces glucagon secretion, producing anti-hyperglycaemic activity among type II diabetics. The objective of this study was a global analytical molecular pharmacological study of the endocrinological rationale of anti-diabetic prescriptions appraisal attributes for metformin and sitagliptin, along with anti-diabetic tertiary medical healthcare patient satisfaction evaluation.Methods: 100 new early moderate grade type II diabetics were prescribed oral metformin 500 mg or sitagliptin 25 mg once daily for 3 months, in monotherapy, or in combination therapy, or in a mixed regimen of monotherapy and combination therapy. The patients’ endocrinological pharmacotherapeutic compliance was analysed. The number of prescriptions for metformin and sitagliptin was recorded; and prescription percentages were calculated. The completeness and molecular basis of prescription content attributes were analysed. The molecular basis of anti-diabetic pharmacotherapeutics, was analysed. The anti-diabetic tertiary medical healthcare patient satisfaction was evaluated by patient response to different attributes of anti-diabetic treatment.Results: All the patients had completed the study, with no adverse effects related drop-out, lost to follow-up or voluntarily withdrawn patients. The prescription rates of metformin was 75% (75 prescriptions), followed by sitagliptin: 25% (25 prescriptions).100% prescriptions were complete for each prescription content attribute. The molecular pharmacotherapeutic response mechanisms were significantly efficacious. All the patients were satisfied with each anti-diabetic medical healthcare attribute. Conclusions: The patient endocrinological pharmacotherapeutic compliance was significantly high. Metformin was most commonly prescribed, followed by sitagliptin. The prescription content analyses showed 100% completeness, with significant pharmacotherapeutic molecular efficacy. There was ample anti-diabetic medical healthcare satisfaction.

scholarly journals Characterization of a Gene Encoding an Acetylase Required for Pyoverdine Synthesis in Pseudomonas aeruginosa

2006 ◽  
Vol 188 (8) ◽  
pp. 3149-3152 ◽  
Author(s):  
Iain L. Lamont ◽  
Lois W. Martin ◽  
Talia Sims ◽  
Amy Scott ◽  
Mary Wallace
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Molecular Basis ◽  
Type Ii ◽  
Gene Encoding ◽  
Different Strains ◽  
Pyoverdine Synthesis

ABSTRACT Strains of Pseudomonas aeruginosa secrete one of three pyoverdine siderophores (types I to III). We have characterized a gene, pvdY II (for the pvdY gene present in type II P. aeruginosa strains), that is only present in strains that make type II pyoverdine. A mutation in pvdY II prevented pyoverdine synthesis. Bioinformatic, genetic, and biochemical approaches indicate that the PvdYII enzyme catalyzes acetylation of hydroxyornithine. Expression of pvdY II is repressed by the presence of iron and upregulated by the presence of type II pyoverdine. Characterization of pvdY II provides insights into the molecular basis for production of different pyoverdines by different strains of P. aeruginosa.

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