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Wyszukujesz frazę ""MESH: Protein Binding"" wg kryterium: Temat


Tytuł:
The HSP90/R2TP assembly chaperone promotes cell proliferation in the intestinal epithelium
Autorzy:
Maurizy, Chloé
Abeza, Claire
Lemmers, Bénédicte
Gabola, Monica
Longobardi, Ciro
Pinet, Valérie
Ferrand, Marina
Paul, Conception
Bremond, Julie
Langa, Francina
Gerbe, François
Jay, Philippe
Verheggen, Céline
Tinari, Nicola
Helmlinger, Dominique
Lattanzio, Rossano
Bertrand, Edouard
Hahne, Michael
Pradet-Balade, Bérengère
Pokaż więcej
Temat:
General Physics and Astronomy
General Biochemistry, Genetics and Molecular Biology
General Chemistry
Science
MESH: Animals
MESH: Cell Proliferation
MESH: Intestinal Mucosa
MESH: Mice, Inbred C57BL
MESH: Mice, Knockout
MESH: Mice, Transgenic
MESH: Microscopy, Confocal
MESH: Molecular Chaperones
MESH: Protein Binding
MESH: Stem Cells
MESH: Cells, Cultured
MESH: Epithelial Cells
MESH: HSP90 Heat-Shock Proteins
MESH: Humans
[SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology
Animals
Cell Proliferation
Cells, Cultured
Epithelial Cells/cytology/metabolism
HSP90 Heat-Shock Proteins/metabolism
Humans
Intestinal Mucosa/cytology/metabolism
Mice, Inbred C57BL
Mice, Knockout
Mice, Transgenic
Microscopy, Confocal
Molecular Chaperones/metabolism
Protein Binding
Stem Cells/cytology/metabolism
Biochemistry, biophysics & molecular biology [Life sciences]
Biochimie, biophysique & biologie moléculaire [Sciences du vivant]
Article
Chaperones
Intestinal stem cells
Źródło:
Nature Communications, Vol 12, Iss 1, Pp 1-19 (2021)
Nature Communications
Nature Communications, Nature Publishing Group, 2021, 12 (1), pp.4810. ⟨10.1038/s41467-021-24792-4⟩
The HSP90/R2TP assembly chaperone promotes cell proliferation in the intestinal epithelium. Nature Communications, 12(1), 4810., United KingdomNature Publishing Group. (2021).
Dostępność:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::66a684d2b37d0731f7bbb1ca0f5ddd57
https://www.nature.com/articles/s41467-021-24792-4.pdf
Tytuł:
Critical assessment of protein intrinsic disorder prediction
Autorzy:
Necci, Marco
Piovesan, Damiano
Tosatto, Silvio C. E.
Hoque, Md Tamjidul
Walsh, Ian
Iqbal, Sumaiya
Vendruscolo, Michele
Sormanni, Pietro
Wang, Chen
Raimondi, Daniele
Sharma, Ronesh
Zhou, Yaoqi
Litfin, Thomas
Galzitskaya, Oxana Valerianovna
Lobanov, Michail Yu.
Vranken, Wim
Wallner, Björn
Mirabello, Claudio
Malhis, Nawar
Dosztányi, Zsuzsanna
Erdős, Gábor
Mészáros, Bálint
Gao, Jianzhao
Wang, Kui
Hu, Gang
Wu, Zhonghua
Sharma, Alok
Hanson, Jack
Paliwal, Kuldip
Callebaut, Isabelle
Bitard-Feildel, Tristan
Orlando, Gabriele
Peng, Zhenling
Xu, Jinbo
Wang, Sheng
Jones, David T.
Cozzetto, Domenico
Meng, Fanchi
Yan, Jing
Gsponer, Jörg
Cheng, Jianlin
Wu, Tianqi
Kurgan, Lukasz
Promponas, Vasilis J.
Tamana, Stella
Marino-Buslje, Cristina
Martínez-Pérez, Elizabeth
Chasapi, Anastasia
Ouzounis, Christos
Dunker, A. Keith
Kajava, Andrey V.
Leclercq, Jeremy Y.
Aykac-Fas, Burcu
Lambrughi, Matteo
Maiani, Emiliano
Papaleo, Elena
Chemes, Lucia Beatriz
Álvarez, Lucía
González-Foutel, Nicolás S.
Iglesias, Valentin
Pujols, Jordi
Ventura, Salvador
Palopoli, Nicolás
Benítez, Guillermo Ignacio
Parisi, Gustavo
Bassot, Claudio
Elofsson, Arne
Govindarajan, Sudha
Lamb, John
Salvatore, Marco
Hatos, András
Monzon, Alexander Miguel
Bevilacqua, Martina
Mičetić, Ivan
Minervini, Giovanni
Paladin, Lisanna
Quaglia, Federica
Leonardi, Emanuela
Davey, Norman
Horvath, Tamas
Kovacs, Orsolya Panna
Murvai, Nikoletta
Pancsa, Rita
Schad, Eva
Szabo, Beata
Tantos, Agnes
Macedo-Ribeiro, Sandra
Manso, Jose Antonio
Pereira, Pedro José Barbosa
Davidović, Radoslav
Veljkovic, Nevena
Hajdu-Soltész, Borbála
Pajkos, Mátyás
Szaniszló, Tamás
Guharoy, Mainak
Lazar, Tamas
Macossay-Castillo, Mauricio
Tompa, Peter
Pokaż więcej
Temat:
Computational platforms and environments
Machine learning
Protein structure predictions
Proteins
Software
MESH: Amino Acid Sequence
MESH: Computational Biology
MESH: Databases, Protein
MESH: Intrinsically Disordered Proteins
MESH: Protein Binding
MESH: Protein Conformation
MESH: Protein Folding
MESH: Software
[SDV]Life Sciences [q-bio]
[INFO]Computer Science [cs]
Analysis
631/114/2398
631/114/794
631/45/612
631/114/2411
631/114/1305
Źródło:
Nature Methods
Nature Methods, Nature Publishing Group, 2021, 18 (5), pp.472-481. ⟨10.1038/s41592-021-01117-3⟩
Dostępność:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6644b1ab401186fe5f30549fca5ccd18
https://hal.sorbonne-universite.fr/hal-03329755
Tytuł:
Differential activity and selectivity of N‐terminal modified CXCL12 chemokines at the CXCR4 and ACKR3 receptors
Autorzy:
Françoise Baleux
Agnieszka Jaracz-Ros
Angélique Levoye
Pasquale Cutolo
Martin Gustavsson
Guillaume Bernadat
Tracy M. Handel
Carmen Gallego
Françoise Bachelerie
Erika Cecon
Irina Kufareva
Pokaż więcej
Temat:
Cell Biology
Immunology
Immunology and Allergy
Chemokine
biology.protein
biology
Selectivity
Chemokine receptor
Receptor
Helix
GPCR Signaling
Cell biology
CXCR4
Agonist
medicine.drug_class
medicine
Signal Transduction and Genes
pluridimensional efficacy Receptors
GPCR signaling
chemokine variants
CXCL12
ACKR3
pluridimensional efficacy
MESH: Amino Acid Sequence
MESH: Binding Sites
MESH: Mutation
MESH: Oligopeptides
MESH: Protein Binding
MESH: Protein Conformation, alpha-Helical
MESH: Protein Conformation, beta-Strand
MESH: Protein Interaction Domains and Motifs
MESH: Receptors, CXCR
MESH: Receptors, CXCR4
MESH: Recombinant Proteins
MESH: beta-Arrestins
MESH: Chemokine CXCL11
MESH: Chemokine CXCL12
MESH: Cyclic AMP
MESH: Gene Expression
MESH: HEK293 Cells
MESH: Heterocyclic Compounds
MESH: Humans
MESH: Molecular Dynamics Simulation
[SDV]Life Sciences [q-bio]
Article
biological factors
biological phenomena, cell phenomena, and immunity
embryonic structures
Źródło:
Journal of Leukocyte Biology
Journal of Leukocyte Biology, Society for Leukocyte Biology, 2020, 107 (6), pp.1123-1135. ⟨10.1002/jlb.2ma0320-383rr⟩
J Leukoc Biol
Dostępność:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0c8ab59a65992cf5ae58cc65116784d0
https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2FJLB.2MA0320-383RR
Tytuł:
Inositol pyrophosphates promote the interaction of SPX domains with the coiled-coil motif of PHR transcription factors to regulate plant phosphate homeostasis
Autorzy:
Joka Pipercevic
Kristina Sturm
Jinsheng Zhu
Dorothea Fiedler
Sebastian Hiller
Larissa Broger
Martina Katharina Ried
Ludwig A. Hothorn
Robert K. Harmel
Michael Hothorn
Rebekka Wild
Luciano A. Abriata
Pokaż więcej
Temat:
MESH: Amino Acid Motifs
MESH: Arabidopsis
MESH: Inositol Phosphates
MESH: Mutation
MESH: Nuclear Proteins
MESH: Protein Binding
MESH: Protein Domains
MESH: Recombinant Proteins
MESH: Signal Transduction
MESH: Transcription Factors
MESH: Arabidopsis Proteins
MESH: Crystallography, X-Ray
MESH: Diphosphates
MESH: Gene Expression Regulation, Plant
[SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM]
lcsh:Science
lcsh:Q
ddc:580
Amino Acid Motifs
Arabidopsis/physiology
Arabidopsis Proteins/genetics/isolation & purification/metabolism/ultrastructure
Crystallography
X-Ray
Diphosphates/metabolism
Gene Expression Regulation
Plant
Inositol Phosphates/metabolism
Mutation
Nuclear Proteins/genetics/metabolism
Protein Binding/genetics
Protein Domains/genetics
Recombinant Proteins/genetics/isolation & purification/metabolism/ultrastructure
Signal Transduction/genetics
Transcription Factors/genetics/isolation & purification/metabolism/ultrastructure
General Physics and Astronomy
General Biochemistry, Genetics and Molecular Biology
General Chemistry
DNA
chemistry.chemical_compound
chemistry
Cell signaling
medicine.disease_cause
medicine
Transcription factor
Cell biology
Starvation response
MYB
Coiled coil
Inositol
Article
X-ray crystallography
Transcription
Plant physiology
Źródło:
Nature Communications
Nature Communications, Nature Publishing Group, 2021, 12 (1), pp.384. ⟨10.1038/s41467-020-20681-4⟩
Nature Communications, Vol 12, Iss 1, Pp 1-13 (2021)
Nature Communications, Vol. 12, No 384 (2021)
Dostępność:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a8b14105c08592d3d2097a82178d60b5
https://hal.archives-ouvertes.fr/hal-03328790
Tytuł:
Novel ribonucleotide discrimination in the RNA polymerase-like two-barrel catalytic core of Family D DNA polymerases
Autorzy:
Andrew F. Gardner
Ece Alpaslan
Ludovic Sauguet
Thomas C. Evans
Kelly M. Zatopek
Pokaż więcej
Temat:
MESH: Amino Acid Sequence
MESH: Archaeal Proteins
MESH: Genome, Archaeal
MESH: Histidine
MESH: Kinetics
MESH: Models, Molecular
MESH: Mutation
MESH: Protein Binding
MESH: Protein Conformation, alpha-Helical
MESH: Protein Conformation, beta-Strand
MESH: Protein Interaction Domains and Motifs
MESH: Recombinant Proteins
MESH: Binding Sites
MESH: Ribonucleotides
MESH: Sequence Alignment
MESH: Sequence Homology, Amino Acid
MESH: Substrate Specificity
MESH: Thermococcus
MESH: Catalytic Domain
MESH: Cloning, Molecular
MESH: DNA Replication
MESH: DNA, Archaeal
MESH: DNA-Directed DNA Polymerase
MESH: Gene Expression
MESH: Gene Expression Regulation, Archaeal
[SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology
AcademicSubjects/SCI00010
Genome Integrity, Repair and Replication
Genetics
Biochemistry
DNA polymerase
biology.protein
biology
RNA
DNA replication
Thermococcus
biology.organism_classification
Nucleotide
chemistry.chemical_classification
chemistry
Ribonucleotide
RNA polymerase
chemistry.chemical_compound
Polymerase
Źródło:
Nucleic Acids Research
Nucleic Acids Research, Oxford University Press, 2020, 48 (21), pp.12204-12218. ⟨10.1093/nar/gkaa986⟩
Dostępność:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::85fbf1b87ad50a09fe8aa5c33da49784
https://hal-pasteur.archives-ouvertes.fr/pasteur-03086156
Tytuł:
Evolution of abiotic cubane chemistries in a nucleic acid aptamer allows selective recognition of a malaria biomarker
Autorzy:
Ahmed Haouz
Young Lo
AB Kinghorn
Patrick Weber
Yee-Wai Cheung
Marcel Hollenstein
G. Paul Savage
Pascal Röthlisberger
Alvin W C Wong
Ariel E. Mechaly
Fabienne Levi-Acobas
Julian A. Tanner
Pokaż więcej
Temat:
M.H
malaria diagnosis Author Contributions J.A.T
cubane
X-ray crystallography
SELEX
Modified aptamer
Y.W.C. and P.R. were responsible
malaria diagnosis
MESH: Aptamers, Nucleotide
MESH: Biomarkers
MESH: Protein Binding
MESH: Protozoan Proteins
MESH: Humans
MESH: Hydrogen Bonding
MESH: L-Lactate Dehydrogenase
MESH: Malaria
MESH: Molecular Diagnostic Techniques
MESH: Molecular Dynamics Simulation
MESH: Plasmodium vivax
[CHIM]Chemical Sciences
[CHIM.ORGA]Chemical Sciences/Organic chemistry
Multidisciplinary
Computational biology
Aptamer
Nucleotide
chemistry.chemical_classification
chemistry
Plasmodium falciparum
biology.organism_classification
biology
Plasmodium vivax
Cubane
chemistry.chemical_compound
Nucleic acid
Systematic evolution of ligands by exponential enrichment
Hydrogen bond
Physical Sciences
Źródło:
Proceedings of the National Academy of Sciences of the United States of America
Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2020, 117 (29), pp.16790-16798. ⟨10.1073/pnas.2003267117⟩
Proc Natl Acad Sci U S A
Dostępność:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fdffd90d6dacf4d61f52342b6cd179ac
https://hal-pasteur.archives-ouvertes.fr/pasteur-03138380
Tytuł:
Molecular Basis of Host-Adaptation Interactions between Influenza Virus Polymerase PB2 Subunit and ANP32A
Autorzy:
Martin Blackledge
Nicola Salvi
Darren J. Hart
Damien Maurin
Elise Delaforge
Sissy Kalayil
Stephen Cusack
Sigrid Milles
Malene Ringkjøbing Jensen
Aldo R. Camacho-Zarco
Pokaż więcej
Temat:
Host adaptation
Protein subunit
Influenza A virus subtype H5N1
medicine.disease_cause
medicine
Chemistry
Virus
Polymerase
biology.protein
biology
Mutation
Binding site
Mutant
Cell biology
lcsh:Science
lcsh:Q
[SDV]Life Sciences [q-bio]
General Physics and Astronomy
General Biochemistry, Genetics and Molecular Biology
General Chemistry
Heterotrimeric G protein
MESH: Animals
MESH: Avian Proteins
MESH: Humans
MESH: Influenza A Virus, H5N1 Subtype
MESH: Influenza in Birds
MESH: Influenza, Human
MESH: Mutation
MESH: Nuclear Magnetic Resonance, Biomolecular
MESH: Nuclear Proteins
MESH: Protein Binding
MESH: Protein Domains
MESH: RNA Replicase
MESH: RNA-Binding Proteins
MESH: Species Specificity
MESH: Viral Proteins
MESH: Virus Replication
MESH: Birds
[SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM]
Science
Article
Intrinsically disordered proteins
Influenza virus
Solution-state NMR
virus diseases
Źródło:
Nature Communications, Vol 11, Iss 1, Pp 1-12 (2020)
Nature Communications
Nature Communications, Nature Publishing Group, 2020, 11 (1), ⟨10.1038/s41467-020-17407-x⟩
Nature Communications, Nature Publishing Group, 2020, 11 (1), pp.3656. ⟨10.1038/s41467-020-17407-x⟩
Dostępność:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ce095ca25613cf9567243b52a9f08146
https://syndication.highwire.org/content/doi/10.1101/2020.03.18.996579
Tytuł:
Structures of MERS-CoV spike glycoprotein in complex with sialoside attachment receptors
Autorzy:
Park, Young-Jun
Walls, Alexandra C.
Wang, Zhaoqian
Sauer, Maximillian M.
Li, Wentao
Tortorici, M. Alejandra
Bosch, Berend-Jan
DiMaio, Frank
Veesler, David
Pokaż więcej
Temat:
MESH: Binding Sites
MESH: Carbohydrate Conformation
MESH: Protein Domains
MESH: Protein Interaction Mapping
MESH: Sialic Acids
MESH: Spike Glycoprotein, Coronavirus
MESH: Structure-Activity Relationship
MESH: Cryoelectron Microscopy
MESH: Dipeptidyl Peptidase 4
MESH: Hemagglutination, Viral
MESH: Humans
MESH: Middle East Respiratory Syndrome Coronavirus
MESH: Models, Molecular
MESH: Protein Binding
MESH: Protein Conformation
[SDV]Life Sciences [q-bio]
Article
Cryoelectron microscopy
Viral membrane fusion
Molecular Biology
Structural Biology
Neuraminic acid
chemistry.chemical_compound
chemistry
Viral entry
Protein structure
Viral protein
medicine.disease_cause
medicine
Cell biology
Plasma protein binding
Receptor
Binding site
Glycoprotein
chemistry.chemical_classification
Binding Sites
Carbohydrate Conformation
Dipeptidyl Peptidase 4/chemistry
Hemagglutination, Viral
Humans
Middle East Respiratory Syndrome Coronavirus/chemistry
Models, Molecular
Protein Binding
Protein Conformation
Protein Domains
Protein Interaction Mapping
Sialic Acids/chemistry
Spike Glycoprotein, Coronavirus/chemistry
Structure-Activity Relationship
Coronacrisis-Taverne
Hemagglutination
Viral
Models
Molecular
Spike Glycoprotein
Coronavirus/chemistry
viruses
Źródło:
Nature Structural and Molecular Biology
Nature Structural and Molecular Biology, Nature Publishing Group, 2019, 26 (12), pp.1151-1157. ⟨10.1038/s41594-019-0334-7⟩
Nature Structural & Molecular Biology
Nature Structural and Molecular Biology, 26(12), 1151
Opis pliku:
text/plain
Dostępność:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9632f9b7fea1d3a3afea62860df826ec
https://hal-pasteur.archives-ouvertes.fr/pasteur-02546517

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