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Identification of the KRIT1 Protein by LexA-Based Yeast Two-Hybrid System

2020
Cerebral cavernous malformation (CCM) is a vascular malformation of the central nervous system that is associated with leaky capillaries, and a predisposition to serious clinical conditions including intracerebral hemorrhage and seizures. Germline or sporadic mutations in the CCM1/KRIT1 gene are responsible for the majority of cases of CCM.
Serebriiskii I.G.   +2 more
openaire   +2 more sources

Identification of a novel KRIT1 mutation in an Italian family with cerebral cavernous malformation by the protein truncation test

Journal of the Neurological Sciences, 2003
Familial cerebral cavernous malformation (CCM) exhibits autosomal dominant inheritance and is characterized by vascular disorders of the brain, which can lead to seizures, focal neurological deficits, hemorrhagic stroke, and migraine. Three CCM loci have been mapped, but the gene for only one locus--KRIT1 coding for Krev-1/rap1 interaction trapped 1 ...
Valeria, Marini   +6 more
openaire   +2 more sources

PTEN/PI3K/Akt/VEGF signaling and the cross talk to KRIT1, CCM2, and PDCD10 proteins in cerebral cavernous malformations

Neurosurgical Review, 2014
Cerebral cavernous malformations (CCM) are common vascular malformation of the brain and are associated with abnormal angiogenesis. Although the exact etiology and the underlying molecular mechanism are still under investigation, recent advances in the identification of the mutations in three genes and their interactions with different signaling ...
Hartmann, Christian   +2 more
openaire   +3 more sources

KRIT1/Cerebral Cavernous Malformation 1 Protein Localizes to Vascular Endothelium, Astrocytes, and Pyramidal Cells of the Adult Human Cerebral Cortex

Neurosurgery, 2004
Mutations in KRIT1 cause familial cerebral cavernous malformation, an autosomal dominant disorder affecting primarily the central nervous system vasculature. Although recent studies have suggested that Krev-1 interaction trapped 1 (KRIT1) is a microtubule-associated protein that interacts with integrin cytoplasmic domain-associated protein-1alpha, the ...
Ozlem, Guzeloglu-Kayisli   +5 more
openaire   +2 more sources

Sorting nexin 17, a non-self-assembling and a PtdIns(3)P high class affinity protein, interacts with the cerebral cavernous malformation related protein KRIT1

Biochemical and Biophysical Research Communications, 2006
The mammalian sorting nexin (SNX) proteins are involved in the endocytosis and the sorting machinery of transmembrane proteins. Additionally to the family defining phox homology (PX) domain, SNX17 is the only member with a truncated FERM (4.1, ezrin, radixin, and moesin) domain and a unique C-terminal region (together designated as FC unit).
Martin, Czubayko   +4 more
openaire   +2 more sources

The contemporary management of cancers of the sinonasal tract in adults

Ca-A Cancer Journal for Clinicians, 2023
Rajat Thawani
exaly  

Highly accurate protein structure prediction with AlphaFold

Nature, 2021
John M Jumper   +2 more
exaly  

The protein corona from nanomedicine to environmental science

Nature Reviews Materials, 2023
Assist Prof Morteza Mahmoudi   +2 more
exaly  

Treatment of renal cell carcinoma: Current status and future directions

Ca-A Cancer Journal for Clinicians, 2017
Pedro Coelho Barata, Brian I Rini
exaly  

Current recommendations and recent progress in endometrial cancer

Ca-A Cancer Journal for Clinicians, 2019
Gini F Fleming
exaly  

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