Results 21 to 30 of about 4,795 (186)

Conformational plasticity and allosteric communication networks explain Shelterin protein TPP1 binding to human telomerase

open access: yesCommunications Chemistry, 2023
The Shelterin complex protein TPP1 interacts with human telomerase (TERT) by means of the TEL-patch region, controlling telomere homeostasis. Aberrations in the TPP1-TERT heterodimer formation might lead to short telomeres and severe diseases like ...
Simone Aureli   +3 more
doaj   +2 more sources

Structural and functional analysis of the human POT1-TPP1 telomeric complex [PDF]

open access: yesNature Communications, 2017
POT1 and TPP1 are part of the shelterin complex and are essential for telomere length regulation and maintenance. Naturally occurring mutations of the telomeric POT1–TPP1 complex are implicated in familial glioma, melanoma and chronic lymphocytic ...
Duncan M. Baird   +27 more
core   +7 more sources

Dynamic peptides of human TPP1 fulfill diverse functions in telomere maintenance. [PDF]

open access: yesNucleic Acids Research, 2016
Telomeres are specialized nucleoprotein complexes that comprise the ends of linear chromosomes. Human telomeres end in a short, single-stranded DNA (ssDNA) overhang that is recognized and bound by two telomere proteins, POT1 and TPP1.
de la Fuente, Maria   +6 more
core   +6 more sources

Mutational profiling of POT1 gene and its interaction with TPP1 in cancer- A computational approach [PDF]

open access: yesInformatics in Medicine Unlocked, 2020
Telomeres are specialized structures at the end of eukaryotic chromosomes that maintain genomic stability by preventing chromosomal rearrangements and thereby enabling semi-conservative replication of telomeric DNA.
Priyanjali Bhattacharya   +7 more
doaj   +3 more sources

Structural insights into POT1-TPP1 interaction and POT1 C-terminal mutations in human cancer

open access: yesNature Communications, 2017
Human telomeres are protected by a specialized shelterin complex composed of six proteins. Here the authors structurally characterize the interaction between the POT1-TPP1 shelterin component and identify mutations associated with genome instability and ...
Cong Chen   +19 more
doaj   +2 more sources

Zebrafish as a model system to study the physiological function of telomeric protein TPP1.

open access: yesPLoS ONE, 2011
Telomeres are specialized chromatin structures at the end of chromosomes. Telomere dysfunction can lead to chromosomal abnormalities, DNA damage responses, and even cancer.
Yiying Xie   +3 more
doaj   +3 more sources

GABAergic interneurons contribute to the fatal seizure phenotype of CLN2 disease mice [PDF]

open access: yesJCI Insight
The cellular etiology of seizures in CLN2 disease, a childhood-onset neurodegenerative lysosomal storage disorder caused by a deficiency of tripeptidyl peptidase 1 (TPP1), remains elusive.
Keigo Takahashi   +13 more
doaj   +2 more sources

Prognostic implications of high- OXPHOS macrophages in gastric cancer: a single-cell transcriptomics and tumor microenvironment communication study [PDF]

open access: yesFrontiers in Oncology
BackgroundGastric cancer (GC) is characterized by heterogeneous tumor microenvironment (TME) with various cell types contributing to disease progression and patient outcomes.
Ziyuan Lin   +5 more
doaj   +2 more sources

Different Faces of the Human Telomeric Protein TPP1

open access: yes, 2019
Eukaryotic cells must overcome two major biological problems associated with linear chromosomes: the end protection and the end replication problems. The end protection problem occurs when the natural ends of linear chromosomes are misrecognized as DNA ...
Grill, Sherilyn
core   +6 more sources

Case report: Analysis of novel compound heterozygous TPP1 variants in a Chinese patient with neuronal ceroid lipofuscinosis type 2

open access: yesFrontiers in Genetics, 2022
Neuronal ceroid lipofuscinosis type 2 (CLN2) is an autosomal recessive neurodegenerative disease caused by variants in the TPP1 gene that lead to the deficiency of the lysosomal enzyme tripeptidyl peptidase I (TPP1) activity.
Sui-Bing Miao   +7 more
doaj   +1 more source

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