Zobrazeno 1 - 10
of 23
pro vyhledávání: '"Virtudes Villegas"'
Autor:
Manuel Rico, Jorge Santoro, Francesc X. Avilés, Josep Vendrell, M. Angeles Jiménez, Luis Serrano, Virtudes Villegas
Publikováno v:
Protein Science. 12:296-305
The activation domain of human procarboxypeptidase A2, ADA2h, is an 81-residue globular domain released during the proteolytic activation of the proenzyme. The role of this and other similar domains as assistants of the correct folding of the enzyme
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f569e6c81829a9d7a78215105c30b383
https://doi.org/10.1110/ps.0227303
https://doi.org/10.1110/ps.0227303
Publikováno v:
Journal of Mass Spectrometry. 37:974-984
In the post-genomic era, several projects focused on the massive experimental resolution of the three-dimensional structures of all the proteins of different organisms have been initiated. Simultaneously, significant progress has been made in the ab
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3bea4cfea34c53a8127c3fc978d5975e
https://doi.org/10.1002/jms.356
https://doi.org/10.1002/jms.356
Autor:
Jui-Yoa Chang, Virtudes Villegas, Silvia Salamanca, Josep Vendrell, Li Li, Francesc X. Avilés
Publikováno v:
Journal of Biological Chemistry. 277:17538-17543
The unfolding and denaturation curves of leech carboxypeptidase inhibitor (LCI) were elucidated using the technique of disulfide scrambling. In the presence of thiol initiator and denaturant, the native LCI denatures by shuffling its native disulfide
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0728009794a63a9e9997b48ec19e3d3c
https://doi.org/10.1074/jbc.m200040200
https://doi.org/10.1074/jbc.m200040200
Autor:
Francesc X. Avilés, Vladimir V. Filimonov, Luis Serrano, Jose C. Martinez, Virtudes Villegas, Ana María González Fernández, Francisco Conejero-Lara, Nico A. J. van Nuland, Pedro L. Mateo
Publikováno v:
European Journal of Biochemistry. 267:5891-5899
Thermodynamic characterization of the activation domain of human procarboxypeptidase A2, ADA2h, and its helix-engineered mutants was carried out by differential scanning calorimetry. The mutants were engineered by changing residues in the exposed fac
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::248a93d45cd080f50f4e5b7532a5265d
https://doi.org/10.1046/j.1432-1327.2000.01638.x
https://doi.org/10.1046/j.1432-1327.2000.01638.x
Publikováno v:
FEBS Letters. 472:27-33
Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS) has been used to monitor hydrogen exchange on entire proteins. Two alternative methods have been used to carry out the hydrogen exchange studies, exchanging d
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::123a3092fcfd900458cf6c827288c58a
https://doi.org/10.1016/s0014-5793(00)01418-6
https://doi.org/10.1016/s0014-5793(00)01418-6
Autor:
Jane Larowe Sterner, Salvador Ventura, Jeffrey Lynn Larson, Josep Vendrell, Charles Lee Hershberger, Francesc X. Avilés, Virtudes Villegas
Publikováno v:
Journal of Biological Chemistry. 274:19925-19933
The proteolytic processing of pancreatic procarboxypeptidase B to a mature and functional enzyme is much faster than that of procarboxypeptidase A1. This different behavior has been proposed to depend on specific conformational features at the region
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::41c795e6e4871b6af9c0c746e97585d2
https://doi.org/10.1074/jbc.274.28.19925
https://doi.org/10.1074/jbc.274.28.19925
Stabilization of proteins by rational design of α-helix stability using helix/coil transition theory
Publikováno v:
Scopus-Elsevier
Backgound: Increasing protein stability is a major goal of protein engineering because of its potential industrial and pharmacological applications. Several different rule-of-thumb strategies have been employed for such a purpose, but a general ratio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4b9f1a866ba721b3e94a46e93dc138af
https://doi.org/10.1016/s1359-0278(96)00009-0
https://doi.org/10.1016/s1359-0278(96)00009-0
Autor:
Virtudes Villegas, Fernando Soriano, Enrique Méndez, Francesc X. Avilés, Miquel Salva, Francisco J. Burgos
Publikováno v:
Scopus-Elsevier
The molecular events which lead to the proteolytic transformation of porcine procarboxypeptidase B (PCPB) in carboxypeptidase B (CPB) have been determined. Among pancreatic and other tested proteinases, trypsin is the only one capable of generating c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d9ec1fe3e5e5d1cc09f4aaa50ba1312d
https://doi.org/10.1021/bi00230a038
https://doi.org/10.1021/bi00230a038
Publikováno v:
Current Microbiology. 20:83-90
The expression of the linkedtoxA andtoxB genes coding for the A and B subunits of the heat-labile enterotoxin ofEscherichia coli, respectively, has been studied. For this reason,toxA-lacZ andtoxB-lacZ fusions were constructed through a promoter-probe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ed8c7da8521b9ab6a7e12b2b9f31884f
https://doi.org/10.1007/bf02092878
https://doi.org/10.1007/bf02092878
Publikováno v:
Journal of molecular biology. 366(4)
Understanding the initial steps of protein aggregation leading to the formation of amyloid fibrils remains a challenge. Here, the kinetics of such a process is determined for a misfolding protein model, ADA2h. The double nature of the very early kine
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ab7979831ed0f52bd1f895d7784bf4cb
https://pubmed.ncbi.nlm.nih.gov/17204287
https://pubmed.ncbi.nlm.nih.gov/17204287