Výsledky vyhľadávania - "Intrinsically Disordered Proteins/genetics"

Specificity in clustering of gene-specific transcription factors is encoded in the genome

Autori: Shivali Dongre Nadine L Vastenhouw

Zdroj: Nucleic Acids Res
Nucleic acids research, vol. 53, no. 13

Predmety: Gene regulation, Chromatin and Epigenetics, Animals, Zebrafish/genetics, Zebrafish/embryology, Zebrafish/metabolism, Transcription Factors/genetics, Transcription Factors/metabolism, Transcription Factors/chemistry, Zebrafish Proteins/genetics, Zebrafish Proteins/metabolism, Zebrafish Proteins/chemistry, Genome, Multigene Family, Octamer Transcription Factor-3/genetics, Octamer Transcription Factor-3/metabolism, Octamer Transcription Factor-3/chemistry, Nanog Homeobox Protein/genetics, Nanog Homeobox Protein/metabolism, Intrinsically Disordered Proteins/metabolism, Intrinsically Disordered Proteins/genetics, DNA/metabolism, Embryo, Nonmammalian/metabolism

Popis súboru: application/pdf

Prístupová URL adresa: https://serval.unil.ch/notice/serval:BIB_4CD68E481E64
http://nbn-resolving.org/urn/resolver.pl?urn=urn:nbn:ch:serval-BIB_4CD68E481E641
https://serval.unil.ch/resource/serval:BIB_4CD68E481E64.P001/REF.pdf

Periostin C-Terminal Is Intrinsically Disordered and Interacts with 143 Proteins in an In Vitro Epidermal Model of Atopic Dermatitis

Autori: Christian E. Rusbjerg-Weberskov Mette Liere Johansen Jan S. Nowak a ďalší

Zdroj: Biochemistry
Rusbjerg-Weberskov, C E, Johansen, M L, Nowak, J S, Otzen, D, Pedersen, J S, Enghild, J J & Nielsen, N S 2023, 'Periostin C-Terminal Is Intrinsically Disordered and Interacts with 143 Proteins in an In Vitro Epidermal Model of Atopic Dermatitis', Biochemistry, vol. 62, no. 19, pp. 2803-2815. https://doi.org/10.1021/acs.biochem.3c00176

Predmety: Intrinsically Disordered Proteins, Intrinsically Disordered Proteins/genetics, Humans, Exons, Cell Adhesion Molecules/genetics, Cell Adhesion Molecules, 3. Good health, Dermatitis, Atopic

Popis súboru: application/pdf

Prístupová URL adresa: https://pubmed.ncbi.nlm.nih.gov/37704583
https://pure.au.dk/portal/en/publications/ae02f609-2260-466a-b639-d781958acee8
https://pure.au.dk/portal/en/publications/ae02f609-2260-466a-b639-d781958acee8
https://pure.au.dk/ws/files/417147180/rusbjerg-weberskov-et-al-2023-periostin-c-terminal-is-intrinsically-disordered-and-interacts-with-143-proteins-in-an-in.pdf
https://doi.org/10.1021/acs.biochem.3c00176

Grape ASR-Silencing Sways Nuclear Proteome, Histone Marks and Interplay of Intrinsically Disordered Proteins

Autori: Atanassov, Hristo Parrilla, Jonathan Artault, Caroline a ďalší

Prispievatelia: Atanassov, Hristo Parrilla, Jonathan Artault, Caroline a ďalší

Zdroj: ISSN: 1661-6596.

Predmety: VvMSA-RNAi silencing, ASR, IDPs, LEA D-29, nuclear proteome, iTRAQ, histone PTMs, grape embryogenic cells, MESH: Abscisic Acid / metabolism, MESH: Cell Line, MESH: Epigenesis, Genetic / drug effects, MESH: Gene Expression Regulation, Plant, MESH: Gene Knockdown Techniques, MESH: Histone Code, MESH: Histones / metabolism, MESH: Intrinsically Disordered Proteins / genetics, MESH: Intrinsically Disordered Proteins / metabolism, MESH: Protein Processing, Post-Translational, MESH: Proteomics / methods, MESH: Vitis / cytology, MESH: Vitis / genetics, MESH: Vitis / metabolism, MESH: Cell Nucleus / genetics, MESH: Cell Nucleus / metabolism, [SDV]Life Sciences [q-bio]

Relation: info:eu-repo/semantics/altIdentifier/pmid/35163458; PUBMED: 35163458; PUBMEDCENTRAL: PMC8835812

Dostupnosť: https://hal.science/hal-04403638
https://hal.science/hal-04403638v1/document
https://hal.science/hal-04403638v1/file/ijms-23-01537.pdf
https://doi.org/10.3390/ijms23031537

Defects in t6A tRNA modification due to GON7 and YRDC mutations lead to Galloway-Mowat syndrome

Autori: Justine Bacchetta Dominique Liger Eduardo Machuca a ďalší

Prispievatelia: Justine Bacchetta Dominique Liger Eduardo Machuca a ďalší

Zdroj: Nat Commun
Nature Communications, Vol 10, Iss 1, Pp 1-13 (2019)

Predmety: RNA-Binding Proteins/chemistry, Male, 0301 basic medicine, Adenosine, Science, Nuclear Proteins/chemistry, [SDV.GEN] Life Sciences [q-bio]/Genetics, Nephrosis/genetics, Article, Microcephaly/genetics, 03 medical and health sciences, RNA, Transfer, Hernia, Hiatal/genetics, GTP-Binding Proteins, GTP-Binding Proteins/chemistry, Journal Article, Humans, Child, 0303 health sciences, Research Support, Non-U.S. Gov't, Nuclear Proteins, RNA-Binding Proteins, 3. Good health, Intrinsically Disordered Proteins, Hernia, Hiatal, Multiprotein Complexes, Mutation, Microcephaly, Intrinsically Disordered Proteins/genetics, Nephrosis, Female, Adenosine/analogs & derivatives, Multiprotein Complexes/chemistry, RNA, Transfer/genetics

Popis súboru: image/pdf; application/pdf

Prístupová URL adresa: https://www.nature.com/articles/s41467-019-11951-x.pdf
https://pubmed.ncbi.nlm.nih.gov/31481669
https://doaj.org/article/77cd12b7d5974fda8810f1a228293257
https://www.hal.inserm.fr/inserm-02322309/document
https://pubmed.ncbi.nlm.nih.gov/31481669/
https://www.ncbi.nlm.nih.gov/pubmed/31481669
https://europepmc.org/article/PMC/PMC6722078
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6722078
https://dumas.ccsd.cnrs.fr/ICSN/inserm-02322309
https://dspace.library.uu.nl/handle/1874/390552

Defects in t6A tRNA modification due to GON7 and YRDC mutations lead to Galloway-Mowat syndrome

Autori: Arrondel, Christelle Missoury, Sophia Snoek, Rozemarijn a ďalší

Prispievatelia: Arrondel, Christelle Missoury, Sophia Snoek, Rozemarijn a ďalší

Predmety: Adenosine/analogs & derivatives, Child, Female, GTP-Binding Proteins/chemistry, Hernia, Hiatal/genetics, Humans, Intrinsically Disordered Proteins/genetics, Male, Microcephaly/genetics, Multiprotein Complexes/chemistry, Mutation, Nephrosis/genetics, Nuclear Proteins/chemistry, RNA, Transfer/genetics, RNA-Binding Proteins/chemistry, Journal Article, Research Support, Non-U.S. Gov't

Popis súboru: image/pdf

Relation: https://dspace.library.uu.nl/handle/1874/390552

Dostupnosť: https://dspace.library.uu.nl/handle/1874/390552

An intrinsically disordered region-mediated confinement state contributes to the dynamics and function of transcription factors

Autori: Susanne Mandrup Ville Paakinaho Diana A. Stavreva a ďalší

Zdroj: Garcia, D A, Johnson, T A, Presman, D M, Fettweis, G, Wagh, K, Rinaldi, L, Stavreva, D A, Paakinaho, V, Jensen, R A M, Mandrup, S, Upadhyaya, A & Hager, G L 2021, ' An intrinsically disordered region-mediated confinement state contributes to the dynamics and function of transcription factors ', Molecular Cell, vol. 81, no. 7, pp. 1484-1498 . https://doi.org/10.1016/j.molcel.2021.01.013

Predmety: 0301 basic medicine, intrinsically disordered regions, GRMON, Transcription Factors/genetics, GRDIM, CONFINEMENT, Receptors, Glucocorticoid/chemistry, Biochimie, biophysique & biologie moléculaire, PPAR, Mice, 03 medical and health sciences, Receptors, Glucocorticoid, glucocorticoid receptor, Receptors, Glucocorticoid/genetics, BI-EXPONENTIAL, Animals, POWER-LAW, Transcription Factors/metabolism, SINGLE-MOLECULE, Molecular Biology, Receptors, Glucocorticoid/metabolism, 0303 health sciences, CHROMATIN BINDING, GRmon, Intrinsically Disordered Proteins/metabolism, GRdim, chromatin binding, Cell Biology, Transcription Factors/chemistry, TRANSCRIPTION DYNAMICS, Life sciences, Rats, Intrinsically Disordered Proteins, Intrinsically Disordered Proteins/chemistry, power-law, confinement, GLUCOCORTICOID RECEPTOR, Sciences du vivant, Intrinsically Disordered Proteins/genetics, INTRINSICALLY DISORDERED REGIONS, Female, single-molecule, transcription dynamics, bi-exponential, Biochemistry, biophysics & molecular biology, Transcription Factors

Popis súboru: application/pdf

Prístupová URL adresa: https://pubmed.ncbi.nlm.nih.gov/33561389
https://pubmed.ncbi.nlm.nih.gov/33561389/
https://www.ncbi.nlm.nih.gov/pubmed/33561389
https://www.sciencedirect.com/science/article/pii/S1097276521000137
http://europepmc.org/article/MED/33561389
https://portal.findresearcher.sdu.dk/da/publications/an-intrinsically-disordered-region-mediated-confinement-state-con
http://www.ncbi.nlm.nih.gov/pubmed/33561389
https://hdl.handle.net/2268/303031
https://doi.org/10.1016/j.molcel.2021.01.013
https://portal.findresearcher.sdu.dk/da/publications/fd6e8ddf-9c32-4533-bf0c-0734c797c6cd
https://doi.org/10.1016/j.molcel.2021.01.013
https://portal.findresearcher.sdu.dk/da/publications/fd6e8ddf-9c32-4533-bf0c-0734c797c6cd
http://hdl.handle.net/11336/175283

An intrinsically disordered region-mediated confinement state contributes to the dynamics and function of transcription factors.

Autori: Garcia, David A Johnson, Thomas A Presman, Diego M a ďalší

Zdroj: Molecular Cell, 81 (7), 1484 - 1498.e6 (2021-04-01)

Predmety: GRdim, GRmon, PPAR, bi-exponential, chromatin binding, confinement, glucocorticoid receptor, intrinsically disordered regions, power-law, single-molecule, transcription dynamics, Intrinsically Disordered Proteins, Receptors, Glucocorticoid, Transcription Factors, Animals, Female, Intrinsically Disordered Proteins/chemistry, Intrinsically Disordered Proteins/genetics, Intrinsically Disordered Proteins/metabolism, Mice, Rats, Receptors, Glucocorticoid/chemistry, Receptors, Glucocorticoid/genetics, Receptors, Glucocorticoid/metabolism, Transcription Factors/chemistry, Transcription Factors/genetics, Transcription Factors/metabolism, Molecular Biology, Cell Biology, Life sciences, Biochemistry, biophysics & molecular biology, Sciences du vivant, Biochimie, biophysique & biologie moléculaire

Relation: https://api.elsevier.com/content/article/PII:S1097276521000137?httpAccept=text/xml; urn:issn:1097-2765; urn:issn:1097-4164

Prístupová URL adresa: https://orbi.uliege.be/handle/2268/303031

A rare heterozygous TREM2 coding variant identified in familial clustering of dementia affects an intrinsically disordered protein region and function of TREM2.

Autori: Karsak, Meliha Glebov, Konstantin Scheffold, Marina a ďalší

Zdroj: Human Mutation, 41 (1), 169 - 181 (2020-01)

Predmety: Alzheimer disease, TREM2, conformation, dementia, intrinsically disordered region, Intrinsically Disordered Proteins, Membrane Glycoproteins, Receptors, Immunologic, TREM2 protein, human, Aged, Alleles, Animals, Cell Line, Dementia/diagnosis, Dementia/genetics, Female, Genetic Association Studies, Humans, Intrinsically Disordered Proteins/genetics, Membrane Glycoproteins/genetics, Membrane Glycoproteins/metabolism, Middle Aged, Open Reading Frames/genetics, Pedigree, Phenotype, Protein Transport, Immunologic/genetics, Immunologic/metabolism

Relation: urn:issn:1059-7794; urn:issn:1098-1004; https://orbilu.uni.lu/handle/10993/60949; info:hdl:10993/60949; info:pmid:31464095; wos:000486672900001

Dostupnosť: https://orbilu.uni.lu/handle/10993/60949
https://doi.org/10.1002/humu.23904

Lipid membrane templated misfolding and self-assembly of intrinsically disordered tau protein

Autori: Majewski, Jaroslaw Jones, Emmalee M. Vander Zanden, Crystal M. a ďalší

Zdroj: Scientific reports 10(1), 13324 (2020). doi:10.1038/s41598-020-70208-6

Predmety: info:eu-repo/classification/ddc/600, Humans, Intrinsically Disordered Proteins: chemistry, Intrinsically Disordered Proteins: genetics, Lipid Bilayers: chemistry, Protein Conformation, beta-Strand, Protein Folding, Protein Multimerization, tau Proteins: chemistry, tau Proteins: genetics

Geografické téma: DE

Relation: info:eu-repo/semantics/altIdentifier/pmid/pmid:32770092; info:eu-repo/semantics/altIdentifier/issn/2045-2322; https://pub.dzne.de/record/153393

Dostupnosť: https://pub.dzne.de/record/153393
https://pub.dzne.de/search?p=id:%22DZNE-2020-01390%22

Partner-Mediated Polymorphism of an Intrinsically Disordered Protein

Autori: Bignon, Christophe Troilo, Francesca Gianni, Stefano a ďalší

Prispievatelia: Bignon, Christophe Troilo, Francesca Gianni, Stefano a ďalší

Zdroj: ISSN: 0022-2836.

Predmety: N(TAIL), XD, induced folding, major inducible heat shock protein (hsp70), measles virus, MESH: Amino Acid Substitution, MESH: Binding Sites, MESH: Viral Proteins/metabolism, MESH: HSP70 Heat-Shock Proteins/metabolism, MESH: Intrinsically Disordered Proteins/chemistry, MESH: Intrinsically Disordered Proteins/genetics, MESH: Intrinsically Disordered Proteins/metabolism, MESH: Measles virus/genetics, MESH: Measles virus/metabolism, MESH: Models, Molecular, MESH: Nucleoproteins/chemistry, MESH: Nucleoproteins/genetics, MESH: Nucleoproteins/metabolism, MESH: Phosphoproteins/metabolism, MESH: Protein Binding, MESH: Protein Conformation, alpha-Helical, MESH: Protein Folding, MESH: Viral Proteins/chemistry, MESH: Viral Proteins/genetics, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM], [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM]

Relation: info:eu-repo/semantics/altIdentifier/pmid/29197511; hal-01802951; https://hal.archives-ouvertes.fr/hal-01802951; PUBMED: 29197511

Dostupnosť: https://hal.archives-ouvertes.fr/hal-01802951
https://doi.org/10.1016/j.jmb.2017.11.012

Long-range correlated dynamics in intrinsically disordered proteins.

Autori: Parigi, Giacomo Rezaei-Ghaleh, Nasrollah Giachetti, Andrea a ďalší

Zdroj: Journal of the American Chemical Society 136(46), 16201-16209 (2014). doi:10.1021/ja506820r

Predmety: info:eu-repo/classification/ddc/540, Animals, Chemical Phenomena, Intrinsically Disordered Proteins: chemistry, Intrinsically Disordered Proteins: genetics, Intrinsically Disordered Proteins: metabolism, Models, Molecular, Mutation, Protein Conformation, Protons, Temperature, Water: chemistry, alpha-Synuclein: chemistry, alpha-Synuclein: genetics, alpha-Synuclein: metabolism, Intrinsically Disordered Proteins, alpha-Synuclein, Water

Geografické téma: DE

Relation: info:eu-repo/semantics/altIdentifier/issn/1943-2984; info:eu-repo/semantics/altIdentifier/pmid/pmid:25331250; info:eu-repo/semantics/altIdentifier/issn/1520-5126; info:eu-repo/semantics/altIdentifier/issn/0002-7863; https://pub.dzne.de/record/137646

Dostupnosť: https://pub.dzne.de/record/137646
https://pub.dzne.de/search?p=id:%22DZNE-2020-03968%22