Titre : Conformation des protéines

Conformation des protéines : Questions médicales fréquentes

Termes MeSH sélectionnés :

Immunophenotyping

Questions fréquentes et termes MeSH associés

Diagnostic 5

#1

Comment diagnostiquer une anomalie de conformation protéique ?

Des techniques comme la spectroscopie RMN et la cristallographie aux rayons X sont utilisées.
Protéines Spectroscopie Cristallographie
#2

Quels tests sont utilisés pour évaluer la conformation des protéines ?

Les tests incluent la chromatographie et l'électrophorèse sur gel.
Électrophorèse Chromatographie Protéines
#3

Quels marqueurs biologiques indiquent des problèmes de conformation ?

Des biomarqueurs comme les protéines mal repliées peuvent être détectés dans le sang.
Biomarqueurs Protéines Maladies protéiques
#4

Peut-on utiliser l'imagerie pour diagnostiquer des anomalies protéiques ?

Oui, l'imagerie par résonance magnétique peut aider à visualiser des anomalies.
Imagerie par résonance magnétique Protéines Diagnostic
#5

Quels symptômes cliniques peuvent indiquer une anomalie de conformation ?

Des symptômes comme la fatigue, la douleur articulaire ou des troubles neurologiques peuvent survenir.
Symptômes Protéines Maladies

Symptômes 5

#1

Quels symptômes sont associés aux maladies de conformation protéique ?

Les symptômes varient, incluant troubles neurologiques, douleurs et fatigue.
Symptômes Maladies protéiques Troubles neurologiques
#2

Comment les anomalies de conformation affectent-elles le corps ?

Elles peuvent entraîner des dysfonctionnements cellulaires et des maladies dégénératives.
Dysfonctionnement cellulaire Maladies dégénératives Protéines
#3

Les troubles cognitifs peuvent-ils être liés à des anomalies protéiques ?

Oui, certaines maladies comme Alzheimer sont liées à des protéines mal repliées.
Alzheimer Protéines Troubles cognitifs
#4

Quels signes cliniques indiquent une maladie de prion ?

Des signes incluent des troubles neurologiques rapides et des changements de comportement.
Maladie de prion Troubles neurologiques Comportement
#5

Les douleurs musculaires peuvent-elles être causées par des anomalies protéiques ?

Oui, des maladies comme la myopathie peuvent résulter de protéines mal conformées.
Myopathie Douleurs musculaires Protéines

Prévention 5

#1

Comment prévenir les maladies liées à la conformation des protéines ?

Une alimentation équilibrée, l'exercice et l'évitement de toxines peuvent aider.
Prévention Alimentation Exercice
#2

Les tests génétiques peuvent-ils aider à prévenir des maladies protéiques ?

Oui, ils permettent d'identifier les prédispositions génétiques aux maladies protéiques.
Tests génétiques Prédispositions Maladies protéiques
#3

L'éducation sur les maladies protéiques est-elle importante ?

Oui, elle aide à reconnaître les symptômes précoces et à chercher un traitement.
Éducation Symptômes Traitement
#4

Les vaccinations peuvent-elles prévenir des maladies liées aux protéines ?

Certaines vaccinations peuvent réduire le risque d'infections qui affectent les protéines.
Vaccinations Infections Protéines
#5

Le stress peut-il influencer la conformation des protéines ?

Oui, le stress oxydatif peut perturber le repliement des protéines et causer des maladies.
Stress oxydatif Protéines Maladies

Traitements 5

#1

Quels traitements existent pour les maladies liées à la conformation protéique ?

Les traitements incluent des thérapies géniques, des médicaments et des approches symptomatiques.
Thérapie génique Médicaments Maladies protéiques
#2

Peut-on corriger la conformation des protéines par des médicaments ?

Oui, certains médicaments peuvent stabiliser ou corriger le repliement des protéines.
Médicaments Protéines Repliement
#3

Les thérapies biologiques sont-elles efficaces contre les anomalies protéiques ?

Oui, elles peuvent cibler des protéines spécifiques et améliorer la fonction cellulaire.
Thérapies biologiques Protéines Fonction cellulaire
#4

Quels rôles jouent les chaperonnes dans le traitement des maladies protéiques ?

Les chaperonnes aident à replier correctement les protéines, réduisant les agrégats.
Chaperonnes Protéines Agrégats
#5

Les approches diététiques peuvent-elles influencer la conformation des protéines ?

Oui, une alimentation riche en antioxydants peut aider à maintenir la santé protéique.
Alimentation Antioxydants Protéines

Complications 5

#1

Quelles complications peuvent survenir avec des anomalies protéiques ?

Des complications incluent des maladies neurodégénératives et des troubles métaboliques.
Complications Maladies neurodégénératives Troubles métaboliques
#2

Les maladies de prion entraînent-elles des complications graves ?

Oui, elles peuvent causer des démences rapides et des troubles neurologiques sévères.
Maladies de prion Démences Troubles neurologiques
#3

Comment les anomalies protéiques affectent-elles le système immunitaire ?

Elles peuvent altérer la réponse immunitaire, rendant l'organisme plus vulnérable.
Système immunitaire Anomalies protéiques Vulnérabilité
#4

Les complications cardiovasculaires sont-elles liées à des anomalies protéiques ?

Oui, certaines protéines mal conformées peuvent contribuer à des maladies cardiovasculaires.
Complications cardiovasculaires Protéines Maladies
#5

Les troubles métaboliques peuvent-ils résulter d'anomalies protéiques ?

Oui, des protéines mal repliées peuvent perturber le métabolisme et causer des troubles.
Troubles métaboliques Protéines Perturbation

Facteurs de risque 5

#1

Quels facteurs de risque sont associés aux maladies protéiques ?

Les facteurs incluent des prédispositions génétiques, l'âge et l'exposition à des toxines.
Facteurs de risque Prédispositions génétiques Toxines
#2

Le vieillissement est-il un facteur de risque pour les anomalies protéiques ?

Oui, le vieillissement peut affecter le repliement et la fonction des protéines.
Vieillissement Protéines Anomalies
#3

L'alimentation influence-t-elle le risque de maladies protéiques ?

Oui, une alimentation pauvre en nutriments essentiels peut augmenter le risque.
Alimentation Nutriments Risque
#4

Le stress environnemental peut-il affecter la conformation des protéines ?

Oui, des facteurs comme la pollution peuvent perturber le repliement des protéines.
Stress environnemental Pollution Protéines
#5

Les infections virales sont-elles un facteur de risque pour les maladies protéiques ?

Oui, certaines infections peuvent induire des modifications dans la conformation des protéines.
Infections virales Maladies protéiques Protéines
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conformation affectent-elles le corps ?", "position": 7, "acceptedAnswer": { "@type": "Answer", "text": "Elles peuvent entraîner des dysfonctionnements cellulaires et des maladies dégénératives." } }, { "@type": "Question", "name": "Les troubles cognitifs peuvent-ils être liés à des anomalies protéiques ?", "position": 8, "acceptedAnswer": { "@type": "Answer", "text": "Oui, certaines maladies comme Alzheimer sont liées à des protéines mal repliées." } }, { "@type": "Question", "name": "Quels signes cliniques indiquent une maladie de prion ?", "position": 9, "acceptedAnswer": { "@type": "Answer", "text": "Des signes incluent des troubles neurologiques rapides et des changements de comportement." } }, { "@type": "Question", "name": "Les douleurs musculaires peuvent-elles être causées par des anomalies protéiques ?", "position": 10, "acceptedAnswer": { "@type": "Answer", "text": "Oui, des maladies comme la myopathie peuvent résulter de protéines mal conformées." } }, { "@type": 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affectent les protéines." } }, { "@type": "Question", "name": "Le stress peut-il influencer la conformation des protéines ?", "position": 15, "acceptedAnswer": { "@type": "Answer", "text": "Oui, le stress oxydatif peut perturber le repliement des protéines et causer des maladies." } }, { "@type": "Question", "name": "Quels traitements existent pour les maladies liées à la conformation protéique ?", "position": 16, "acceptedAnswer": { "@type": "Answer", "text": "Les traitements incluent des thérapies géniques, des médicaments et des approches symptomatiques." } }, { "@type": "Question", "name": "Peut-on corriger la conformation des protéines par des médicaments ?", "position": 17, "acceptedAnswer": { "@type": "Answer", "text": "Oui, certains médicaments peuvent stabiliser ou corriger le repliement des protéines." } }, { "@type": "Question", "name": "Les thérapies biologiques sont-elles efficaces contre les anomalies protéiques ?", "position": 18, "acceptedAnswer": { "@type": "Answer", "text": "Oui, elles peuvent cibler des protéines spécifiques et améliorer la fonction cellulaire." } }, { "@type": "Question", "name": "Quels rôles jouent les chaperonnes dans le traitement des maladies protéiques ?", "position": 19, "acceptedAnswer": { "@type": "Answer", "text": "Les chaperonnes aident à replier correctement les protéines, réduisant les agrégats." } }, { "@type": "Question", "name": "Les approches diététiques peuvent-elles influencer la conformation des protéines ?", "position": 20, "acceptedAnswer": { "@type": "Answer", "text": "Oui, une alimentation riche en antioxydants peut aider à maintenir la santé protéique." } }, { "@type": "Question", "name": "Quelles complications peuvent survenir avec des anomalies protéiques ?", "position": 21, "acceptedAnswer": { "@type": "Answer", "text": "Des complications incluent des maladies neurodégénératives et des troubles métaboliques." } }, { "@type": "Question", "name": "Les maladies de prion entraînent-elles des complications graves ?", "position": 22, "acceptedAnswer": { "@type": "Answer", "text": "Oui, elles peuvent causer des démences rapides et des troubles neurologiques sévères." } }, { "@type": "Question", "name": "Comment les anomalies protéiques affectent-elles le système immunitaire ?", "position": 23, "acceptedAnswer": { "@type": "Answer", "text": "Elles peuvent altérer la réponse immunitaire, rendant l'organisme plus vulnérable." } }, { "@type": "Question", "name": "Les complications cardiovasculaires sont-elles liées à des anomalies protéiques ?", "position": 24, "acceptedAnswer": { "@type": "Answer", "text": "Oui, certaines protéines mal conformées peuvent contribuer à des maladies cardiovasculaires." } }, { "@type": "Question", "name": "Les troubles métaboliques peuvent-ils résulter d'anomalies protéiques ?", "position": 25, "acceptedAnswer": { "@type": "Answer", "text": "Oui, des protéines mal repliées peuvent perturber le métabolisme et causer des troubles." } }, { "@type": "Question", "name": "Quels facteurs de risque sont associés aux maladies protéiques ?", "position": 26, "acceptedAnswer": { "@type": "Answer", "text": "Les facteurs incluent des prédispositions génétiques, l'âge et l'exposition à des toxines." } }, { "@type": "Question", "name": "Le vieillissement est-il un facteur de risque pour les anomalies protéiques ?", "position": 27, "acceptedAnswer": { "@type": "Answer", "text": "Oui, le vieillissement peut affecter le repliement et la fonction des protéines." } }, { "@type": "Question", "name": "L'alimentation influence-t-elle le risque de maladies protéiques ?", "position": 28, "acceptedAnswer": { "@type": "Answer", "text": "Oui, une alimentation pauvre en nutriments essentiels peut augmenter le risque." } }, { "@type": "Question", "name": "Le stress environnemental peut-il affecter la conformation des protéines ?", "position": 29, "acceptedAnswer": { "@type": "Answer", "text": "Oui, des facteurs comme la pollution peuvent perturber le repliement des protéines." } }, { "@type": "Question", "name": "Les infections virales sont-elles un facteur de risque pour les maladies protéiques ?", "position": 30, "acceptedAnswer": { "@type": "Answer", "text": "Oui, certaines infections peuvent induire des modifications dans la conformation des protéines." } } ] } ] }
Dr Olivier Menir

Contenu validé par Dr Olivier Menir

Expert en Médecine, Optimisation des Parcours de Soins et Révision Médicale


Validation scientifique effectuée le 25/02/2025

Contenu vérifié selon les dernières recommandations médicales

Sous-catégories

60 au total
└─

Éléments structuraux des protéines

Protein Structural Elements D000072416 - G02.111.570.820.709.275
└─

Structure quaternaire des protéines

Protein Structure, Quaternary D020836 - G02.111.570.820.709.550
└─

Structure secondaire des protéines

Protein Structure, Secondary D017433 - G02.111.570.820.709.600
└─

Structure tertiaire des protéines

Protein Structure, Tertiary D017434 - G02.111.570.820.709.610
└─└─└─

Motifs AT-hook

AT-Hook Motifs D024761 - G02.111.570.820.709.275.500.050
└─└─└─

Motifs de knottins

Cystine Knot Motifs D047168 - G02.111.570.820.709.275.500.127
└─└─└─

Motifs F-box

F-Box Motifs D044782 - G02.111.570.820.709.275.500.205
└─└─└─

Motifs à hélice-boucle-hélice

Helix-Loop-Helix Motifs D018257 - G02.111.570.820.709.275.500.360
└─└─└─

Motif d'activation de l'immunorécepteur dépendant de la tyrosine

Immunoreceptor Tyrosine-Based Activation Motif D061625 - G02.111.570.820.709.275.500.440
└─└─└─

Motif d'inhibition de l'immunorécepteur dépendant de la tyrosine

Immunoreceptor Tyrosine-Based Inhibition Motif D061626 - G02.111.570.820.709.275.500.480
└─└─└─

Motifs kazal

Kazal Motifs D000074161 - G02.111.570.820.709.275.500.490
└─└─└─

Glissières à leucine

Leucine Zippers D016350 - G02.111.570.820.709.275.500.520
└─└─└─

Motif de liaison au poly-ADP-ribose

Poly-ADP-Ribose Binding Motif D000075225 - G02.111.570.820.709.275.500.695
└─└─└─

Motifs de liaison à l'ARN

RNA-Binding Motifs D000071376 - G02.111.570.820.709.275.500.869
└─└─└─

Domaine AAA

AAA Domain D000074182 - G02.111.570.820.709.275.500.913
└─└─└─

Doigts de zinc

Zinc Fingers D016335 - G02.111.570.820.709.275.500.985
└─└─└─

Domaines C2

C2 Domains D000070538 - G02.111.570.820.709.275.750.125
└─└─└─

Modules de liaison au carbohydrate

Carbohydrate Binding Modules D000094342 - G02.111.570.820.709.275.750.157
└─└─└─

Domaine catalytique

Catalytic Domain D020134 - G02.111.570.820.709.275.750.188
└─└─└─

Domaine discoïdine

Discoidin Domain D000070822 - G02.111.570.820.709.275.750.219
└─└─└─

Domaines à boîtes HMG

HMG-Box Domains D024742 - G02.111.570.820.709.275.750.235
└─└─└─

Domaines immunoglobuline

Immunoglobulin Domains D000070557 - G02.111.570.820.709.275.750.250
└─└─└─

Kringles

Kringles D018082 - G02.111.570.820.709.275.750.375
└─└─└─

Domaine de liaison aux méthyl-CpG

Methyl CpG Binding Domain D000070593 - G02.111.570.820.709.275.750.438
└─└─└─

Domaines homologues de la pleckstrine

Pleckstrin Homology Domains D000070539 - G02.111.570.820.709.275.750.469
└─└─└─

Domaines PR-SET

PR-SET Domains D000074463 - G02.111.570.820.709.275.750.477
└─└─└─

Domaines de protéine riches en proline

Proline-Rich Protein Domains D055232 - G02.111.570.820.709.275.750.485
└─└─└─

Motifs et domaines d'intéraction protéique

Protein Interaction Domains and Motifs D054730 - G02.111.570.820.709.275.750.500
└─└─└─

Répétition ankyrine

Ankyrin Repeat D017089 - G02.111.570.820.709.275.875.030
└─└─└─

Répétition kelch

Kelch Repeat D000071776 - G02.111.570.820.709.275.875.273
└─└─└─

Répétition tétratricopeptide

Tetratricopeptide Repeat D000074436 - G02.111.570.820.709.275.875.394
└─└─└─

Répétitions WD40

WD40 Repeats D000071678 - G02.111.570.820.709.275.875.515
└─└─└─└─

Motifs EF Hands

EF Hand Motifs D020832 - G02.111.570.820.709.275.500.360.240
└─└─└─└─

Motifs à hélice-tour-hélice

Helix-Turn-Helix Motifs D019077 - G02.111.570.820.709.275.500.360.360
└─└─└─└─

Motif de liaison à l'ARN double brin

Double-Stranded RNA Binding Motif D000071241 - G02.111.570.820.709.275.500.869.250
└─└─└─└─

Motif de reconnaissance de l'ARN

RNA Recognition Motif D000071377 - G02.111.570.820.709.275.500.869.500
└─└─└─└─

Doigts de zinc CYS2-HIS2

CYS2-HIS2 Zinc Fingers D000070580 - G02.111.570.820.709.275.500.985.250
└─└─└─└─

Doigts de zinc PHD

PHD Zinc Fingers D000075925 - G02.111.570.820.709.275.500.985.438
└─└─└─└─

Domaine fibronectine de type III

Fibronectin Type III Domain D000071238 - G02.111.570.820.709.275.750.250.500
└─└─└─└─

Domaine B30.2-SPRY

B30.2-SPRY Domain D000071197 - G02.111.570.820.709.275.750.500.290
└─└─└─└─

Domaine BTB-POZ

BTB-POZ Domain D000071757 - G02.111.570.820.709.275.750.500.343
└─└─└─└─

Superfamille des domaines de mort

Death Domain Superfamily D000071458 - G02.111.570.820.709.275.750.500.395
└─└─└─└─

Domaines FERM

FERM Domains D000075926 - G02.111.570.820.709.275.750.500.422
└─└─└─└─

Domaines MYND

MYND Domains D000074608 - G02.111.570.820.709.275.750.500.474
└─└─└─└─

Domaines PDZ

PDZ Domains D054731 - G02.111.570.820.709.275.750.500.500
└─└─└─└─

Domaines à doigts de zinc de type RING

RING Finger Domains D054829 - G02.111.570.820.709.275.750.500.625
└─└─└─└─

Domaine d'homologie SRC

src Homology Domains D018909 - G02.111.570.820.709.275.750.500.750
└─└─└─└─

Motif stérile alpha

Sterile Alpha Motif D000071682 - G02.111.570.820.709.275.750.500.813
└─└─└─└─

Domaine Tudor

Tudor Domain D000071856 - G02.111.570.820.709.275.750.500.844
└─└─└─└─

Domaines WW

WW Domains D000074585 - G02.111.570.820.709.275.750.500.937
└─└─└─└─└─

Motif ETS

ETS Motif D000071419 - G02.111.570.820.709.275.500.360.360.500
└─└─└─└─└─

Domaine d'activation et de recrutement des caspases

Caspase Activation and Recruitment Domain D000071476 - G02.111.570.820.709.275.750.500.395.250
└─└─└─└─└─

Domaine de mort

Death Domain D000071459 - G02.111.570.820.709.275.750.500.395.500
└─└─└─└─└─

Domaine effecteur de mort

Death Effector Domain D000071461 - G02.111.570.820.709.275.750.500.395.750
└─└─└─└─└─

Domaine pyrine

Pyrin Domain D000071196 - G02.111.570.820.709.275.750.500.395.875
└─└─

Séquences répétées d'acides aminés

Repetitive Sequences, Amino Acid D020449 - G02.111.570.820.709.275.875
└─└─

Structure en hélice alpha

Protein Conformation, alpha-Helical D000072756 - G02.111.570.820.709.600.020
└─└─

Motifs d'acides aminés

Amino Acid Motifs D020816 - G02.111.570.820.709.600.500
└─└─

Structure en brin bêta

Protein Conformation, beta-Strand D000072757 - G02.111.570.820.709.600.750
└─└─

Domaines protéiques

Protein Domains D000072417 - G02.111.570.820.709.610.500

Auteurs principaux

Maria Silvina Fornasari

2 publications dans cette catégorie

Affiliations :
  • Departamento de Ciencia y Tecnología, Universidad Nacional de Quilmes, CONICET, Bernal, Argentina.
Publications dans "Conformation des protéines" :

Diego Javier Zea

2 publications dans cette catégorie

Affiliations :
  • Structural Bioinformatics Unit, Fundación Instituto Leloir, CONICET, Buenos Aires, Argentina.
Publications dans "Conformation des protéines" :

Gustavo Parisi

2 publications dans cette catégorie

Affiliations :
  • Departamento de Ciencia y Tecnología, Universidad Nacional de Quilmes, CONICET, Bernal, Argentina. gusparisi@gmail.com.
Publications dans "Conformation des protéines" :

Attila Gursoy

2 publications dans cette catégorie

Affiliations :
  • Computer Science and Engineering Department, Koc University, Istanbul, Turkey. agursoy@ku.edu.tr.

Ozlem Keskin

2 publications dans cette catégorie

Affiliations :
  • Chemical and Biological Engineering Department, Koc University, Istanbul, Turkey.

Ming Dong

2 publications dans cette catégorie

Affiliations :
  • Department of Chemistry, North Carolina Agricultural and Technical State University, Greensboro, NC, USA.
Publications dans "Conformation des protéines" :

David Baker

2 publications dans cette catégorie

Affiliations :
  • Department of Biochemistry, University of Washington, Seattle, WA 98105; dabaker@uw.edu so@fas.harvard.edu.
  • Institute for Protein Design, University of Washington, Seattle, WA 98105.
  • Howard Hughes Medical Institute, University of Washington, Seattle, WA 98105.
Publications dans "Conformation des protéines" :

Hao Tian

2 publications dans cette catégorie

Affiliations :
  • Center for Research Computing, Center for Drug Discovery, Design, and Delivery (CD4), Department of Chemistry, Southern Methodist University, Dallas, TX, United States.
Publications dans "Conformation des protéines" :

Sian Xiao

2 publications dans cette catégorie

Affiliations :
  • Center for Research Computing, Center for Drug Discovery, Design, and Delivery (CD4), Department of Chemistry, Southern Methodist University, Dallas, TX, United States.
Publications dans "Conformation des protéines" :

Peng Tao

2 publications dans cette catégorie

Affiliations :
  • Center for Research Computing, Center for Drug Discovery, Design, and Delivery (CD4), Department of Chemistry, Southern Methodist University, Dallas, TX, United States.
Publications dans "Conformation des protéines" :

Alexander Miguel Monzon

1 publication dans cette catégorie

Affiliations :
  • Departamento de Ciencia y Tecnología, Universidad Nacional de Quilmes, CONICET, Bernal, Argentina.
Publications dans "Conformation des protéines" :

H A Scheraga

1 publication dans cette catégorie

Affiliations :
  • Department of Chemistry and Chemical Biology, Baker Laboratory, Cornell University, Ithaca, New York, USA.
Publications dans "Conformation des protéines" :

S Rackovsky

1 publication dans cette catégorie

Affiliations :
  • Department of Chemistry and Chemical Biology, Baker Laboratory, Cornell University, Ithaca, New York, USA.
  • Department of Biochemistry and Biophysics, University of Rochester School of Medicine and Dentistry, Rochester, New York, USA.
Publications dans "Conformation des protéines" :

Avner Schlessinger

1 publication dans cette catégorie

Affiliations :
  • Department of Pharmacological Sciences, Icahn School of Medicine at Mount Sinai, New York, United States.
Publications dans "Conformation des protéines" :

Massimiliano Bonomi

1 publication dans cette catégorie

Affiliations :
  • Department of Structural Biology and Chemistry, Institut Pasteur, Université Paris Cité, Paris, France.
Publications dans "Conformation des protéines" :

Michael Assfalg

1 publication dans cette catégorie

Affiliations :
  • Department of Biotechnology, University of Verona, 37134 Verona, Italy.
Publications dans "Conformation des protéines" :

Diego S Vazquez

1 publication dans cette catégorie

Affiliations :
  • Departamento de Ciencia y Tecnología, Universidad Nacional de Quilmes and Grupo de Biología Estructural y Biotecnología, IMBICE, CONICET, Universidad Nacional de Quilmes, Argentina.
Publications dans "Conformation des protéines" :

Pamela L Toledo

1 publication dans cette catégorie

Affiliations :
  • Departamento de Ciencia y Tecnología, Universidad Nacional de Quilmes and Grupo de Biología Estructural y Biotecnología, IMBICE, CONICET, Universidad Nacional de Quilmes, Argentina.
Publications dans "Conformation des protéines" :

Alejo R Gianotti

1 publication dans cette catégorie

Affiliations :
  • Departamento de Ciencia y Tecnología, Universidad Nacional de Quilmes and Grupo de Biología Estructural y Biotecnología, IMBICE, CONICET, Universidad Nacional de Quilmes, Argentina.
Publications dans "Conformation des protéines" :

Mario R Ermácora

1 publication dans cette catégorie

Affiliations :
  • Departamento de Ciencia y Tecnología, Universidad Nacional de Quilmes and Grupo de Biología Estructural y Biotecnología, IMBICE, CONICET, Universidad Nacional de Quilmes, Argentina.
Publications dans "Conformation des protéines" :

Sources (537 au total)

Immunophenotyping of pulmonary sarcomatoid carcinoma.

Previous studies have suggested that patients with pulmonary sarcomatoid carcinoma (PSC)may benefit from immune checkpoint inhibitors (ICIs); however, relevant data are lacking. This study aimed to es... A retrospective analysis of pathologically confirmed PSC cases from two centers was performed from January 2009 to May 2021. According to the infiltration of CD8+ T cells in different spatial regions,... A total of 32 patients with PSC were included in the final analysis. Of these patients, 65.6% (21/32), 15.6% (5/32), and 18.8% (6/32) were classified as immune-inflamed, immune-excluded, and immune-de... Patients with PSC are characterized by immune-inflamed type and type I (PD-L1+/CD8+, adaptive immune resistance), explaining the intrinsic reasons for their high response rate to immunotherapy....

Immunophenotypic characterization of acute leukemias in Bahia, Brazil.

To characterize the immunophenotypic profile of acute leukemias in the population of the state of Bahia, Brazil.... This is a descriptive, retrospective study. From 2014 to 2018, 796 new cases of acute leukemia were evaluated. The data were obtained from analysis of reports and records of tests performed by flow cy... Most cases were diagnosed as acute myeloid leukemia and 42.7% as acute lymphoblastic leukemia. Significant differences were found in expression of markers in acute leukemias when age groups were compa... Significant differences were found as to several antigens when comparing adults and children, and these findings may contribute to future studies correlating the phenotypic profile to genetic characte...

Cellular immunophenotype of major spine surgery in adults.

ASD reconstructions are a major, sterile traumatic insult, likely causing perturbations to the immune systems. The immune response to surgery is associated with outcomes. The purpose of this study was... Consecutive patients undergoing ASD surgery were approached and enrolled. Peripheral blood was drawn before incision, 4 h after, and 24 h after incision. Blood was stabilized and comprehensive flow cy... Thirteen patients were enrolled; 11(85%) F, 65.4 years (± 7.5), surgical duration 418 ± 83 min, EBL 1928 ± 1253 mL. Hierarchical clustering and PCA found consistent time from incision-dependent change... Despite surgery and patient heterogeneity, we identified an immune signature associated with the sterile trauma of ASD surgery. Circulating leukocyte populations change in composition and signaling pr...

A novel signature of autophagy-related immunophenotyping biomarkers in osteoarthritis.

We aimed to provide an autophagy-related signature to seek immunophenotyping biomarkers in osteoarthritis (OA).... Microarray expression profiling of OA subchondral bone samples and screening of an autophagy database for autophagy-related differentially expressed genes (au-DEGs) between OA and normal samples were ... We screened 754 au-DEGs between OA and control samples, and co-expression networks were constructed using au-DEGs. Three OA-related autophagy hub genes (HSPA5, HSP90AA1, and ITPKB) were identified. Ba... Three autophagy-related markers of OA were identified using bioinformatics methods, and these markers may be useful for the autophagy-related immunophenotyping of OA. The present data may facilitate t...

Acute promyelocytic leukemia: Immunophenotype and differential diagnosis by flow cytometry.

Prompt diagnosis of acute promyelocytic leukemia (APL) is critical for patient care. In this study, we aimed to characterize the immunophenotype of APL and explore immunophenotypic difference between ... Eighty-five cases were collected, including 47 APL, 26 NPM1-mutated acute myeloid leukemia (AML) and 12 KMT2A-rearranged AML with an APL-like immunophenotype. Immunophenotypes were analyzed using flow... APL showed four distinct patterns (designated a-d) based on CD45/SSC plots. Blasts in patterns a-c showed high side scatter, whereas blasts in pattern d had low side scatter and were located in the tr... APL and its immunophenotypic mimics share some immunophenotypic similarities but can be distinguished by CD2, CD13, CD34, CD64, and MPO....

Acute myeloid leukemia with RAM immunophenotype: A new underdiagnosed entity.

Acute myeloid leukemia (AML) with RAM immunophenotype is a distinct subtype of AML, as described by the Children's Oncology Group (COG), with characteristic morphological and immunophenotypic properti... Seven cases with the characteristic RAM immunophenotype were identified in this retrospective analysis of newly diagnosed pediatric AML cases from January 2019 to December 2021. Herein, we have critic... Of 302 cases of pediatric AML (age <18 years), seven cases (2.3%) with the distinct RAM phenotype were observed, with age ranging from 9 months to 5 years. Two patients were misdiagnosed earlier as sm... AML with RAM immunophenotype, a distinct form of pediatric AML with a poor prognosis, may pose a diagnostic challenge if presented as a soft tissue mass. A comprehensive immunophenotypic evaluation, i...