Wyniki wyszukiwania

1

Indications for investigations of purine and pyrimidine disorders

100%

Sebesta I., Krijt J., Kmoch S., Kumsta M., Stiburkova B.

Cellular and Molecular Biology Letters

|

1999

|

tom 04

|

nr 3

2

Congenital disorders of glycosylation. Part II. Defects of protein O-glycosylation

86%

Cylwik B., Lipartowska K., Chrostek L., Gruszewska E.

Acta Biochimica Polonica

|

2013

|

tom 60

|

nr 3

Glycosylation is a form of post-translational modification of proteins and occurs in every living cell. The carbohydrate chains attached to the proteins serve various functions. There are two main types of protein glycosylation: N-glycosylation and O-glycosylation. In this paper, we describe the O-glycosylation process and currently known congenital disorders of glycosylation associated with defects of protein O-glycosylation. This process takes place in the cis Golgi apparatus after N-glycosylation and folding of the proteins. The O-glycosylation is essential in the biosynthesis of mucins, the formation of proteoglycan core proteins and blood group proteins. Most common forms of O-glycans are the mucin-type glycans. There are more than 20 known disorders related to O-glycosylation disturbances. We review 8 of the following diseases linked to defects in the synthesis of O-xylosylglycans, O-N acetylgalactosaminylglycans, O-xylosyl/N-acetylglycans, O-mannosylglycans, and O-fucosylglycans: multiple exostoses, progeroid variant of Ehlers-Danlos syndrome, progeria, familial tumoral calcinosis, Schneckenbecken dysplasia, Walker-Warburg syndrome, spondylocostal dysostosis type 3, and Peter's plus syndrome. Causes of these diseases include gene mutations and deficiency of proteins (enzymes). Their diagnosis includes syndromic presentation, organ-specific expression and laboratory findings.

3

Screening genetic disorder in cattle

86%

Citek J., Rehout V., Pavkova J., Blahova B., Hala K., Strapak P.

Animal Science Papers and Reports. Supplement

|

2004

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tom 22

|

nr 2

4

The search for a genetic defect in Polish patients with chronic granulomatous disease

86%

Jurkowska M., Kurenko-Deptuch M., Bal J., Roos D.

Archivum Immunologiae et Therapiae Experimentalis

|

2004

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tom 52

|

nr 6

5

Charcot-Marie-Tooth type 1A disease caused by a novel Ser112Arg mutation in the PMP22 gene, coexisting with a slowly progressive hearing impairment

72%

Kabzinska D., Sinkiewicz-Darol E., Hausmanowa-Petrusewicz I., Kochanski A.

Journal of Applied Genetics

|

2010

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tom 51

|

nr 2

203-209

Among 57 mutations in the peripheral myelin protein 22 gene (PMP22) identified so far in patients affected by Charcot-Marie-Tooth disease (CMT), only 8 have been shown to segregate with a mixed phenotype of CMT and hearing impairment. In this study, we report a new Ser112Arg mutation in the PMP22 gene, identified in a patient with early-onset CMT and slowly progressive hearing impairment beginning in the second decade of life. We suggest that the Ser112Arg mutation in the PMP22 gene might have a causative role in the early-onset CMT with hearing impairment. Thus, our study extends the spectrum of CMT phenotypes putatively associated with PMP22 gene mutations.

6

Congenital disorders of glycosylation. Part I. Defects of protein N-glycosylation

72%

Cylwik B., Naklicki M., Chrostek L., Gruszewska E.

Acta Biochimica Polonica

|

2013

|

tom 60

|

nr 2

Glycosylation is the most common chemical process of protein modification and occurs in every living cell. Disturbances of this process may be either congenital or acquired. Congenital disorders of glycosylation (CDG) are a rapidly growing disease family, with about 50 disorders reported since its first clinical description in 1980. Most of the human diseases have been discovered recently. CDG result from defects in the synthesis of the N- and O-glycans moiety of glycoproteins, and in the attachment to the polypeptide chain of proteins. These defects have been found in the activation, presentation, and transport of sugar precursors, in the enzymes responsible for glycosylation, and in proteins that control the traffic of component. There are two main types of protein glycosylation: N-glycosylation and O-glycosylation. Most diseases are due to defects in the N-glycosylation pathway. For the sake of convenience, CDG were divided into 2 types, type I and II. CDG can affect nearly all organs and systems. The considerable variability of clinical features makes it difficult to recognize patients with CDG. Diagnosis can be made on the basis of abnormal glycosylation display. In this paper, an overview of CDG with a new nomenclature limited to the group of protein N-glycosylation disorders, clinical phenotype and diagnostic approach, have been presented. The location, reasons for defects, and the number of cases have been also described. This publication aims to draw attention to the possibility of occurrence of CDG in each multisystem disorder with an unknown origin.

7

Partial hypoxanthine - guanine phosphoribosyltransferase deficiency in young man

72%

Kumsta M., Krijt J., Sebesta I.

Cellular and Molecular Biology Letters

|

1999

|

tom 04

|

nr 3

8

Is a genetic defect in Fkbp6 a common cause of azoospermia in humans?

72%

Miyamato T., Sato H., Yogev L., Kleiman S., Namiki M., Koh E., Sakugawa N., Hayashi H., Ishikawa M., Lamb D. J., Sengoku K.

Cellular and Molecular Biology Letters

|

2006

|

tom 11

|

nr 4

FK506-binding protein 6 (Fkbp6) is a member of a gene family containing a prolyl isomerase/FK506-binding domain and tetratricopeptide protein-protein interaction domains. Recently, the targeted inactivation of Fkbp6 in mice has been observed to result in aspermic males and the absence of normal pachytene spermatocytes. The loss of Fkbp6 results in abnormal pairing and a misalignment of the homologous chromosomes, and in non-homologous partner switches and autosynapsis of the X chromosome cores in meiotic spermatocytes. In this study, we analyzed whether human FKBP6 gene defects might be associated with human azoospermia. We performed a mutation analysis in all the coding regions of the human FKBP6 gene in 19 patients with azoospermia resulting from meiotic arrest. The expression of the human FKBP6 gene was specific to the testis, and a novel polymorphism site, 245C → G (Y60X) could be found in exon 3. Our findings suggest that the human FKBP6 gene might be imprinted in the testis based on an analysis using two polymorphism sites.

9

Energy production and Frohlich’s polar vibrations in cancer cells

58%

Pokorny J.

Current Topics in Biophysics. Supplement

|

2011

|

tom 34

|

nr A: Plenary lectures

10

Microarray of SNPs for diverse applications in commercial pig breeding

58%

Kaminski S., Brym P., Help H., Rusc A., Wojcik E.

Polish Journal of Veterinary Sciences

|

2009

|

tom 12

|

nr 1

Modern pig production needs new tools for fast, reliable, more effective breeding. In the present paper we present a chip containing 45 SNP (Single Nucleotide Polymorphisms) which enables the determining of 1 genetic disease (PSS – Porcine Stress Syndrome), 4 QTLs genes: PRKAG3, CAST, MC4R and ESR, which together with the remaining SNPs create a panel useful in marker-assisted selection and veterinary control. The SNPs were genotyped using the PCR-APEX (Arrayed Primer Extension) technique. Special attention is paid to evaluation of the 45 SNP chip as an alternative approach to parentage and identity control. Based on allele frequency estimations, for a sample of 88 individuals of commercial pig lines, the probabilities that a randomly chosen candidate parent would be excluded from paternity or maternity were estimated to be 99.9% when genotypes of both parents and a progeny were known, and 98% when the genotypes of only one parent and a piglet were available. The marker set presented here also reached a probability of identity in the order of 10-16, which allows for unequivocal discrimination of animals or their products among billions of individuals. Further improvements for upcoming chip versions were also considered.

11

Molecular mechanisms initiating amyloid beta-fibril formation in Alzheimer's disease

58%

Kirkitadze M. D., Kowalska A.

Acta Biochimica Polonica

|

2005

|

tom 52

|

nr 2

The deposition of aggregated amyloid β-protein (Aβ) in the human brain is a major lesion in Alzheimer’s disease (AD). The process of Aβ fibril formation is associated with a cascade of neuropathogenic events that induces brain neurodegeneration leading to the cognitive and behavioral decline characteristic of AD. Although a detailed knowledge of Aβ assembly is crucial for the development of new therapeutic approaches, our understanding of the molecular mechanisms underlying the initiation of Aβ fibril formation remains very incomplete. The genetic defects responsible for familial AD influence fibrillogenesis. In a majority of familial cases determined by amyloid precursor protein (APP) and presenilin (PS) mutations, a significant overproduction of Aβ and an increase in the Aβ42/Aβ40 ratio are observed. Recently, it was shown that the two main alloforms of Aβ have distinct biological activity and behaviour at the earliest stage of assembly. In vitro studies demonstrated that Aβ42 monomers, but not Aβ40, form initial and minimal structures (pentamer/hexamer units called paranuclei) that can oligomerize to larger forms. It is now apparent that Aβ oligomers and protofibrils are more neurotoxic than mature Aβ fibrils or amyloid plaques. The neurotoxicity of the prefibrillar aggregates appears to result from their ability to impair fundamental cellular processes by interacting with the cellular membrane, causing oxidative stress and increasing free Ca2+ that eventually lead to apoptotic cell death.

12

Defekty genow wystepujace u zwierzat gospodarskich

51%

Zabek T., Rys A.

Biuletyn Informacyjny. Instytut Zootechniki

|

1998

|

tom 36

|

nr 4

5-13

13

Mutacje genomu bydla oraz ich znaczenie gospodarcze

44%

Grzybowski G.

Biuletyn Informacyjny. Instytut Zootechniki

|

2002

|

tom 40

|

nr 2

59-74

Ograniczanie wyników

Indications for investigations of purine and pyrimidine disorders

Congenital disorders of glycosylation. Part II. Defects of protein O-glycosylation

Screening genetic disorder in cattle

The search for a genetic defect in Polish patients with chronic granulomatous disease

Charcot-Marie-Tooth type 1A disease caused by a novel Ser112Arg mutation in the PMP22 gene, coexisting with a slowly progressive hearing impairment

Congenital disorders of glycosylation. Part I. Defects of protein N-glycosylation

Partial hypoxanthine - guanine phosphoribosyltransferase deficiency in young man

Is a genetic defect in Fkbp6 a common cause of azoospermia in humans?

Energy production and Frohlich’s polar vibrations in cancer cells

Microarray of SNPs for diverse applications in commercial pig breeding

Molecular mechanisms initiating amyloid beta-fibril formation in Alzheimer's disease

Defekty genow wystepujace u zwierzat gospodarskich

Mutacje genomu bydla oraz ich znaczenie gospodarcze