M
Manuel Rivera
Researcher at National Autonomous University of Mexico
Publications - 13
Citations - 461
Manuel Rivera is an academic researcher from National Autonomous University of Mexico. The author has contributed to research in topics: Voltage-dependent calcium channel & Patch clamp. The author has an hindex of 10, co-authored 13 publications receiving 411 citations. Previous affiliations of Manuel Rivera include Universidad Autónoma del Estado de Morelos.
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Journal ArticleDOI
Overexpression of NaV1.6 channels is associated with the invasion capacity of human cervical cancer
Everardo Hernández-Plata,Cindy Sharon Ortiz,Brenda Marquina-Castillo,Ingrid Medina-Martinez,Ana Alfaro,Jaime Berumen,Manuel Rivera,Juan Carlos Gomora +7 more
TL;DR: It is concluded that NaV1.6 is upregulated in CaC and could serve as a novel molecular marker for the metastatic behavior of this carcinoma.
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Activity of the renal Na+-K+-2Cl- cotransporter is reduced by mutagenesis of N-glycosylation sites: role for protein surface charge in Cl- transport.
Anahí Paredes,Consuelo Plata,Manuel Rivera,Erika Moreno,Norma Vázquez,Rosario A. Muñoz-Clares,Steven C. Hebert,Gerardo Gamba +7 more
TL;DR: The data demonstrate that NKCC2 is glycosylated and suggest that prevention of glycosYLation reduces its functional expression by affecting insertion into the plasma membrane and the intrinsic activity of the cotransporter.
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Selected mutations in Bacillus subtilis levansucrase semi-conserved regions affecting its biochemical properties
Maria Elena Ortiz-Soto,Manuel Rivera,Enrique Rudiño-Piñera,Clarita Olvera,Agustín López-Munguía +4 more
TL;DR: Evidence is found of the important role of Y429 in acceptor specificity: this is a key residue coordinating the sucrose position in the catalytic domain-binding pocket and the crystallographic structure of this mutant is reported and it is found that S164 is an important residue to maintain the nucleophile positions in the active site.
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Affinity-defining Domains in the Na-Cl Cotransporter: A DIFFERENT LOCATION FOR Cl- AND THIAZIDE BINDING *
Erika Moreno,Erika Moreno,Pedro San Cristobal,Manuel Rivera,Norma Vázquez,Norma A. Bobadilla,Gerardo Gamba +6 more
TL;DR: It is observed that elimination of glycosylation sites in flounder NCC did not affect the affinity of the cotransporter for metolazone, and interchanging transmembrane regions revealed that affinity-modifying residues for chloride and thiazide in NCC are different.
Journal ArticleDOI
α‐Amylase from Bacillus licheniformis mutants near to the catalytic site: effects on hydrolytic and transglycosylation activity
TL;DR: The engineered enzyme reported here may represent an attractive alternative for the starch transformation industries as it affords direct and substantial material savings and requires no process modifications.