Sign In

Login

Password

Forgot Password ? Sign Up

CLPB (French Wikipedia)

Analysis of information sources in references of the Wikipedia article "CLPB" in French language version.

refsWebsite
Global rank French rank
22nih.gov
4th place
12th place
22doi.org
2nd place
3rd place
9issn.org
57th place
4th place
2ensembl.org
1,626th place
2,018th place
1uniprot.org
5,673rd place
low place
1nature.com
234th place
147th place
1cell.com
2,814th place
1,023rd place

cell.com (Global: 2,814th place; French: 1,023rd place)

doi.org (Global: 2nd place; French: 3rd place)

dx.doi.org

  • « Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs », Genome Research, vol. 11, no 3,‎ , p. 422–35 (PMID 11230166, PMCID 311072, DOI 10.1101/gr.GR1547R)
  • « Expression of a putative ATPase suppresses the growth defect of a yeast potassium transport mutant: identification of a mammalian member of the Clp/HSP104 family », Gene, vol. 152, no 2,‎ , p. 157–63 (PMID 7835694, DOI 10.1016/0378-1119(94)00697-Q)
  • « CLPB mutations cause 3-methylglutaconic aciduria, progressive brain atrophy, intellectual disability, congenital neutropenia, cataracts, movement disorder », American Journal of Human Genetics, vol. 96, no 2,‎ , p. 245–57 (PMID 25597510, PMCID 4320260, DOI 10.1016/j.ajhg.2014.12.013)
  • « CLPB variants associated with autosomal-recessive mitochondrial disorder with cataract, neutropenia, epilepsy, and methylglutaconic aciduria », American Journal of Human Genetics, vol. 96, no 2,‎ , p. 258–65 (PMID 25597511, PMCID 4320254, DOI 10.1016/j.ajhg.2014.12.020)
  • Cupo et Shorter, « Skd3 (human CLPB) is a potent mitochondrial protein disaggregase that is inactivated by 3-methylglutaconic aciduria-linked mutations », eLife, vol. 9,‎ , e55279 (ISSN 2050-084X, PMID 32573439, PMCID 7343390, DOI 10.7554/eLife.55279)
  • « Novel CLPB mutation in a patient with 3-methylglutaconic aciduria causing severe neurological involvement and congenital neutropenia », Clinical Immunology, vol. 165,‎ , p. 1–3 (PMID 26916670, DOI 10.1016/j.clim.2016.02.008)
  • Ericson, Schnell, Freeman et Haskell-Luevano, « A fragment of the Escherichia coli ClpB heat-shock protein is a micromolar melanocortin 1 receptor agonist », Bioorganic & Medicinal Chemistry Letters, vol. 25, no 22,‎ , p. 5306–5308 (ISSN 0960-894X, DOI 10.1016/j.bmcl.2015.09.046, lire en ligne)
  • Tennoune, Chan, Breton et Legrand, « Bacterial ClpB heat-shock protein, an antigen-mimetic of the anorexigenic peptide α-MSH, at the origin of eating disorders », Translational Psychiatry, vol. 4, no 10,‎ , e458–e458 (ISSN 2158-3188, DOI 10.1038/tp.2014.98, lire en ligne)
  • (en) Saita, Nolte, Fiedler et Kashkar, « PARL mediates Smac proteolytic maturation in mitochondria to promote apoptosis », Nature Cell Biology, vol. 19, no 4,‎ , p. 318–328 (ISSN 1476-4679, PMID 28288130, DOI 10.1038/ncb3488, lire en ligne)
  • « A camel passes through the eye of a needle: protein unfolding activity of Clp ATPases », Molecular Microbiology, vol. 61, no 5,‎ , p. 1094–100 (PMID 16879409, PMCID 1852505, DOI 10.1111/j.1365-2958.2006.05309.x)
  • (en) Erives et Fassler, « Metabolic and Chaperone Gene Loss Marks the Origin of Animals: Evidence for Hsp104 and Hsp78 Chaperones Sharing Mitochondrial Enzymes as Clients », PLOS ONE, vol. 10, no 2,‎ , e0117192 (ISSN 1932-6203, PMID 25710177, PMCID 4339202, DOI 10.1371/journal.pone.0117192)
  • « The ankyrin repeat as molecular architecture for protein recognition », Protein Science, vol. 13, no 6,‎ , p. 1435–48 (PMID 15152081, PMCID 2279977, DOI 10.1110/ps.03554604)
  • « Ankyrin repeat: a unique motif mediating protein-protein interactions », Biochemistry, vol. 45, no 51,‎ , p. 15168–78 (PMID 17176038, DOI 10.1021/bi062188q)
  • Erzberger et Berger, « Evolutionary relationships and structural mechanisms of aaa+ proteins », Annual Review of Biophysics and Biomolecular Structure, vol. 35, no 1,‎ , p. 93–114 (ISSN 1056-8700, PMID 16689629, DOI 10.1146/annurev.biophys.35.040405.101933)
  • « Disruption of CLPB is associated with congenital microcephaly, severe encephalopathy and 3-methylglutaconic aciduria », Journal of Medical Genetics, vol. 52, no 5,‎ , p. 303–11 (PMID 25650066, DOI 10.1136/jmedgenet-2014-102952)
  • « The AAA+ superfamily of functionally diverse proteins », Genome Biology, vol. 9, no 4,‎ , p. 216 (PMID 18466635, PMCID 2643927, DOI 10.1186/gb-2008-9-4-216)
  • (en) Mróz, Wyszkowski, Szablewski et Zawieracz, « CLPB (caseinolytic peptidase B homolog), the first mitochondrial protein refoldase associated with human disease », Biochimica et Biophysica Acta (BBA) - General Subjects, vol. 1864, no 4,‎ , p. 129512 (PMID 31917998, DOI 10.1016/j.bbagen.2020.129512)
  • « Roles of the Escherichia coli small heat shock proteins IbpA and IbpB in thermal stress management: comparison with ClpA, ClpB, and HtpG In vivo », Journal of Bacteriology, vol. 180, no 19,‎ , p. 5165–72 (PMID 9748451, PMCID 107554, DOI 10.1128/JB.180.19.5165-5172.1998)
  • (en) Chen, Glytsou, Zhou et Narang, « Targeting Mitochondrial Structure Sensitizes Acute Myeloid Leukemia to Venetoclax Treatment », Cancer Discovery, vol. 9, no 7,‎ , p. 890–909 (ISSN 2159-8274, PMID 31048321, PMCID 6606342, DOI 10.1158/2159-8290.CD-19-0117)
  • « New perspective in diagnostics of mitochondrial disorders: two years' experience with whole-exome sequencing at a national paediatric centre », Journal of Translational Medicine, vol. 14, no 1,‎ , p. 174 (PMID 27290639, PMCID 4903158, DOI 10.1186/s12967-016-0930-9)
  • Fetissov, « Role of the gut microbiota in host appetite control: bacterial growth to animal feeding behaviour », Nature Reviews Endocrinology, vol. 13, no 1,‎ , p. 11–25 (ISSN 1759-5029, DOI 10.1038/nrendo.2016.150, lire en ligne)
  • (en) Yoshinaka, Kosako, Yoshizumi et Furukawa, « Structural Basis of Mitochondrial Scaffolds by Prohibitin Complexes: Insight into a Role of the Coiled-Coil Region », iScience, vol. 19,‎ , p. 1065–1078 (ISSN 2589-0042, PMID 31522117, PMCID 6745515, DOI 10.1016/j.isci.2019.08.056, lire en ligne)

ensembl.org (Global: 1,626th place; French: 2,018th place)

May2017.archive.ensembl.org

issn.org (Global: 57th place; French: 4th place)

portal.issn.org

nature.com (Global: 234th place; French: 147th place)

nih.gov (Global: 4th place; French: 12th place)

ncbi.nlm.nih.gov

uniprot.org (Global: 5,673rd place; French: low place)