Francisco Rafael Martins Laurindo
CV Lattes
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Secretaria da Saúde (São Paulo - Estado). Hospital das Clínicas da Faculdade de Medicina da USP (HCFMUSP). Instituto do Coração Professor Euryclides de Jesus Zerbini (INCOR) (Institutional affiliation for the last research proposal) Birthplace: Brazil
Francisco R. M. Laurindo graduated in Medicine by the University of São Paulo School of Medicine, São Paulo, Brazil , in 1978 and completed his residence training in Internal Medicine and Cardiology at the Heart Institute(Incor), University of São Paulo School of Medicine. After a period (1982-84) as associate physician at the same institution, he underwent research training in Physiology and Pharmacology at the Uniformed Services University of the Health Sciences, in Bethesda, Maryland (under Dr. Robert Goldstein, 1984-87). Back to the Heart Institute, University of São Paulo School of Medicine, he started an investigative research track focused on mechanisms of redox signaling processes in the vascular system. He obtained his PhD in 1992, supervised by Dr. Protásio da Luz. Thereafter, he conducted several research projects through independent financial support from research agencies. In 2001, he started, together with Dr. Protásio da Luz, the Vascular Biology Laboratory at the Heart Institute (Incor), University of São Paulo School of Medicine and became its Director in 2008, until presently. His major research interests have focused on understanding mechanisms and regulatory processes underlying the production of oxidant species in vascular cells and tissues and their physiological implications for vessel remodeling in disease. The most important contributions of his group have been the original description of shear stress-dependent generation of superoxide radical from the endothelium, the multi-level characterization of redox response to vascular injury and, particularly, the original discovery that the endoplasmic reticulum chaperone protein disulfide isomerase interacts functionally and physically with oxidant-generating NADPH oxidase complexes. This finding had relevant implications regarding the role of endoplasmic reticulum (patho)physiology on NADPH oxidase function and how redox processes regulate cell migration and vascular remodeling. More recently, Dr. Laurindo's group showed an important role for extracellular PDI in arterial remodeling after injury. Dr. Laurindo has authored or co-authored over 145 publications in peer-reviewed journals, cited >3500 times (h-index=35 (ISI)). He supervised 18 PhD students and 17 post-doctoral fellows, in addition to several undergraduate trainees. From 2008-14, he was the vice-coordinator of the National Institute for Science and Technology of Redox Processes in Biomedicine (CNPq/Fapesp) and since 2013 (until present) the Vice-coordinator and principal investigator of Cepid-Fapesp Redoxoma. He is a member of the Brazilian Academy of Sciences since 2012 and a member of its Board of Directors since 2016, a member of Fapesp Study Committee in Health Sciences from 2008-2016 and Fapesp Advisor Committee in Life Sciences since 2016, a member of Capes Federal Agency Committee (Medicine) from 1998-2017. He served as Council Member of the Society for Free Radical Biology and Medicine from 2010-2014 and belongs to the Editorial Board of Free Radical Biology and Medicine since 2008 and of Clinical Science since 2012. He has been an ad-hoc consultant for >35 publications and research agencies from Brazil and abroad. He was elected as vice-chair (2014) and chair (2016) of the Gordon Research Conference on Nox Family NADPH Oxidases. (Source: Lattes Curriculum)
| News published in Agência FAPESP Newsletter about the researcher |
| Enzyme may indicate predisposition to cardiovascular disease |
- Endoplasmic reticulum-plasma membrane contacts as hubs for Nox NADPH oxidase dependent cellular redox signaling (FAPESP-kcl), AP.R
Abstract
Redox processes strongly regulate (patho) physiological cell signaling, yet several fundamental underlying mechanisms remain unclear, including in particular the associated subcellular compartmentalization. The Shah group at KCI investigates endoplasmic reticulum (ER) signaling mechanisms and associated cardiovascular implications of Nox NAOPH oxidases, major cellular ROS enzyme sources...
- Redoxome - Redox Processes in Biomedicine, AP.CEPID
Abstract
The study of redox processes has high potential to elucidate integrative mechanisms, due to the ubiquity and strength of their effects. Many studies involve the role of redox mechanisms in diseases. However, the complexity of this field has increased concerning structures, structure-function relations, methods, molecular and sub-cellular pathology of redox-regulated proteins, genomics, ...
- Regulation of redox homeostasis and integrated stress response by Protein Disulfide Isomerase (PDI): mechanisms and role in the pathophysiology and therapy of vascular diseases, AP.TEM
Abstract
Redox homeostasis depends on the regulated production of reactive oxygen species (ROS) via enzymatic sources such as the Nox family NADPH oxidase complex, the main source of ROs in vascular cells. Recent studies from our laboratory disclosed an important role of PDI in the regulation of NADPH oxidase. The important functional effects of PDI in NADPH oxidase in a number of distinct cell ...
- Coupling of stress of endoplasmatic reticule with oxidative stress in vascular cells via interaction between protein disulfide isomerase and NAD(p)H oxidase: role of thiol oxidoredutases, AP.TEM
Abstract
The aim of this project is the development and implementation of Laser Induced Breakdown Spectroscopy (LIBS), an analytical technique based on sampling and excitation of atoms and molecules induced by laser. Most recently, LlBS has been considered a very promising analytical tool for in situ quantitative chemical analysis, either in industrial process as well as in the field. However, t...
- Molecular physiology of redox signaling in the vascular system and cultured cell models, AP.TEM
Abstract
Vascular endothelial dysfunction is primarily a dysfunction of redox signaling. These processes involve the effect of free radicals, redox-active metals and reducing equivalents on specific proteins that govern cell function. The enzymatic pathways underlying superoxide radical and other reactive oxygen species (ROS) production are yet unclear. A number of evidences, including work from...
(Only some records are available in English at this moment)
- Cytosolic protein disulfide isomerase-A1 (PDIA1): a novel thiol-redox mechanism in cell signaling, BP.PD
Abstract
Protein disulfide isomerase-A1 (PDIA1) is a dithiol-disulfide oxidoreductase chaperone with a major canonical function of redox protein folding (disulfide bond formation/isomerization) in nascent proteins at the endoplasmic reticulum (ER). Thus, PDIA1 exerts a central role in ER-associated proteostasis and redox balance. The quantitatively smaller PDIA1 pool at the cell surface and extr...
- Modulation of mitochondrial dynamics by isomerase-A1 dissulfide protein in vascular smooth muscle cell, BP.IC
Abstract
Protein Isomerase Disulfide (PDI) is a reticulum chaperone involved in oxidation and reduction, it is a member of thioredoxin superfamily which catalyses the isomerization and formation of disulfide bounds, an essential component in the protein synthesis and processing. PDI have an important role in the cytoskeleton organization and migration of vascular muscular smooth muscle (VSMC). R...
- Endoplasmic reticulum-plasma membrane contacts as hubs for NOx NADPH oxidase-dependent cellular redox signaling, BP.PD
Abstract
Redox processes emerged as major regulatory mechanisms of cell signaling and strongly regulate (patho)physiological processes, but several fundamental underlying mechanisms remain unclear, including in particular the associated subcellular compartmentalization. This remains a fundamental problem in cell biology, essential to clarify the implications of redox processes in health and dise...
(Only some records are available in English at this moment)
- A new PDI activity assay in human plasma, BP.IC
Abstract
Protein Disulfide Isomerase (PDI) is a dithiol disulfide oxidoreductase chaperone of thioredoxin superfamily that catalyzes the formation and isomerization of disulfide bonds as an essential functional component of protein synthesis and processing. Although localized primarily in the endoplasmic reticulum, PDI has been reported in other intracellular locations and on the cell surface. P...
- Modulation of vascular calcification by protein disulfide isomerase: study on a new transgenic mouse model, BP.PD
Abstract
Vascular calcification is an active pathophysiological process related to trophic and inflammatory phenomena, which reduces vascular compliance and is associated with higher morbidity and mortality. However, mechanisms promoting vascular calcification are still poorly understood, which impacts in the absence of effective medical therapies. Oxidative stress and endoplasmic reticulum (ER...
- Grasp pathway involving on the protein disulfide isomerase externalization and its implication in endothelial cell response, BP.PD
Abstract
Protein disulfide isomerase (PDI AI or PDI) is an important chaperone that acts in the oxidative folding in the endoplasmic reticulum with emerging role in signaling and redox homeostasis pathways, including NADPH oxidases interaction. A specific pool PDI presents in the extracellular space of several cell types and regulates processes like thrombosis, cell adhesion, viral infection and...
(Only some records are available in English at this moment)
- Mechanisms and implications of selective cell-surface Grp94 inhibition in breast cancer cells, BE.EP.PD
Abstract
Several intracellular chaperones have been shown to be secreted by distinct cellular types, including vascular, immune and tumor cells. Protein disulfide isomerase (PDI), as well as 70 and 90kDa heat shock protein (Hsp70 and Hsp90) families play extracellular roles in pathological conditions such as thrombosis, vascular remodeling and cancer survival and metastasis generation. Inhibitio...
- Mechanisms underlying the loss of protein disulfide isomerase-dependent regulation of NADPH oxidase in colon carcinoma cells with ras overactivation, BE.EP.DR
Abstract
Protein Disulfide Isomerase (PDI) is a dithiol/disulfide oxidoreductase chaperone mainly from endoplasmic reticulum (ER), where it assists redox protein folding. Recent works indicate PDI involvement in redox cell signaling, bearing a close functional and physical interaction with the NADPH oxidase complex, the main cellular source of signaling oxidants. In Vascular smooth muscle cells ...
- Characterization and mechanisms of microRNA-mediated paracrine signaling involving protein disulfide isomerase-dependent mechano-adaptation in vascular cells, BE.EP.PD
Abstract
While vascular remodeling is a key determinant of vascular lumen in (patho)physiological situations, its mediators remain poorly understood. Recently, we showed that the endoplasmic reticulum redox chaperone protein disulfide isomerase-A1 (PDI) is markedly upregulated during vascular repair to injury, while its externalized pool (peri/epicellular PDI=pecPDI) counteracts constrictive rem...
(Only some records are available in English at this moment)
| 2 / 2 | Ongoing research grants |
| 9 / 4 | Completed research grants |
| 5 / 5 | Ongoing scholarships in Brazil |
| 43 / 10 | Completed scholarships in Brazil |
| 7 / 7 | Completed scholarships abroad |
| 66 / 28 | All research grants and scholarships |
| Associated processes | |
(References retrieved automatically from Web of Science and SciELO through information on FAPESP grants and their corresponding numbers as mentioned in the publications by the authors)
| Publications | 33 |
| Citations | 405 |
| Cit./Article | 12.3 |
| Data from Web of Science | |
BASSI, E.; LIBERMAN, M.; MARTINATTI, M. K.; BORTOLOTTO, L. A.; LAURINDO, F. R. M.. Lipoic acid, but not tempol, preserves vascular compliance and decreases medial calcification in a model of elastocalcinosis. Brazilian Journal of Medical and Biological Research, v. 47, n. 2, p. 119-127, Fev. 2014. Web of Science Citations: 3.
GODOY, LUIZ C.; MORETTI, ANA I.; JURADO, MARCIA C.; OXER, DANIELLA; JANISZEWSKI, MARIANO; CKLESS, KARINA; VELASCO, IRINEU T.; LAURINDO, FRANCISCO R. M.; SOUZA, HERALDO P.. LOSS OF CD40 ENDOGENOUS S-NITROSYLATION DURING INFLAMMATORY RESPONSE IN ENDOTOXEMIC MICE AND PATIENTS WITH SEPSIS. Shock, v. 33, n. 6, p. 626-633, JUN 2010. Web of Science Citations: 15.
MONTEIRO‚ H.P.; ROCHA OLIVEIRA‚ C.J.; CURCIO‚ M.F.; MORAES‚ M.S.; ARAI‚ R.J.. Tyrosine Phosphorylation in Nitric Oxide-Mediated Signaling Events. Methods in Enzymology, v. 396, p. 350-358, 2005. (00/12154-2)
TREVELIN, SILVIA C.; CARLOS, DANIELA; BERETTA, MATTEO; DA SILVA, JOAO S.; CUNHA, FERNANDO Q.. Diabetes Mellitus and Sepsis: A Challenging Association. Shock, v. 47, n. 3, p. 276-287, MAR 2017. Web of Science Citations: 12. (13/08216-2, 11/03293-3, 11/19670-0, 09/54764-6)
SOARES MORETTI, ANA IOCHABEL; MARTINS LAURINDO, FRANCISCO RAFAEL. Protein disulfide isomerases: Redox connections in and out of the endoplasmic reticulum. Archives of Biochemistry and Biophysics, v. 617, n. SI, p. 106-119, MAR 1 2017. Web of Science Citations: 29. (13/07937-8, 14/23657-8, 09/54764-6)
GIMENEZ, MARCELA; SCHICKLING, BRANDON M.; LOPES, LUCIA R.; MILLER, JR., FRANCIS J.. Nox1 in cardiovascular diseases: regulation and pathophysiology. Clinical Science, v. 130, n. 3, p. 151-165, FEB 1 2016. Web of Science Citations: 17. (13/18300-0, 13/03520-5, 13/07937-8, 09/54764-6)
ARAUJO, THAIS L. S.; ZEIDLERA, JULIANNA D.; OLIVEIRA, PERCILLIA V. S.; DIAS, MATHEUS H.; ARMELIN, HUGO A.; LAURINDO, FRANCISCO R. M.. Protein disulfide isomerase externalization in endothelial cells follows classical and unconventional routes. Free Radical Biology and Medicine, v. 103, p. 199-208, FEB 2017. Web of Science Citations: 11. (12/02372-0, 13/07937-8, 14/20595-1, 09/54764-6)
ARAUJO, THAIS L. S.; FERNANDES, CAROLINA G.; LAURINDO, FRANCISCO R. M.. Golgi-independent routes support protein disulfide isomerase externalization in vascular smooth muscle cells. REDOX BIOLOGY, v. 12, p. 1004-1010, AUG 2017. Web of Science Citations: 5. (13/07937-8, 15/06210-2, 12/02372-0)
TANAKA, LEONARDO Y.; LAURINDO, FRANCISCO R. M.. Vascular remodeling: A redox-modulated mechanism of vessel caliber regulation. Free Radical Biology and Medicine, v. 109, n. SI, p. 11-21, AUG 2017. Web of Science Citations: 0. (13/17115-5, 13/07937-8, 09/54764-6)
TREVELIN, SILVIA CELLONE; DOS SANTOS, CELIO XAVIER; FERREIRA, RAPHAEL GOMES; LIMA, LARISSA DE SA; SILVA, RANGEL LEAL; SCAVONE, CRISTOFORO; CURI, RUI; CARLOS ALVES-FILHO, JOSE; CUNHA, THIAGO MATTAR; ROXO-JUNIOR, PERSIO; et al. Apocynin and Nox2 regulate NF-kappa B by modifying thioredoxin-1 redox-state. SCIENTIFIC REPORTS, v. 6, OCT 4 2016. Web of Science Citations: 14. (11/03293-3, 11/19670-0, 13/08216-2, 13/03520-5, 13/07937-8, 12/24677-7, 09/54764-6)
TANAKA, LEONARDO YUJI; GRASSMANN BECHARA, LUIZ ROBERTO; DOS SANTOS, ADRIANA MARQUES; JORDAO, CAMILA PAIXAO; OLIVEIRA DE SOUSA, LUIS GUSTAVO; BARTHOLOMEU, TERESA; VENTURA, LAURA INES; MARTINS LAURINDO, FRANCISCO RAFAEL; RAMIRES, PAULO RIZZO. Exercise improves endothelial function: A local analysis of production of nitric oxide and reactive oxygen species. NITRIC OXIDE-BIOLOGY AND CHEMISTRY, v. 45, p. 7-14, FEB 15 2015. Web of Science Citations: 21.
CHIGNALIA, ANDREIA Z.; OLIVEIRA, MARIA APARECIDA; DEBBAS, VICTOR; DULL, RANDAL O.; LAURINDO, FRANCISCO R. M.; TOUYZ, RHIAN M.; CARVALHO, MARIA HELENA C.; FORTES, ZULEICA B.; TOSTES, RITA C.. Testosterone induces leucocyte migration by NADPH oxidase-driven ROS- and COX2-dependent mechanisms. Clinical Science, v. 129, n. 1, p. 39-48, JUL 2015. Web of Science Citations: 17.
LAURINDO, FRANCISCO R. M.; ARAUJO, THAIS L. S.; ABRAHAO, THALITA B.. Nox NADPH Oxidases and the Endoplasmic Reticulum. Antioxidants & Redox Signaling, v. 20, n. 17, p. 2755-2775, JUN 10 2014. Web of Science Citations: 68. (09/54764-6)
DEMASI, MARILENE; SIMOES, VANESSA; BONATTO, DIEGO. Cross-talk between redox regulation and the ubiquitin-proteasome system in mammalian cell differentiation. BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS, v. 1850, n. 8, SI, p. 1594-1606, AUG 2015. Web of Science Citations: 7. (11/23268-3, 09/54764-6)
TREVELIN, SILVIA CELLONE; LOPES, LUCIA ROSSETTI. Protein Disulfide Isomerase and Nox: New Partners in Redox Signaling. CURRENT PHARMACEUTICAL DESIGN, v. 21, n. 41, p. 5951-5963, 2015. Web of Science Citations: 18. (13/07937-8, 13/03520-5, 09/54764-6)
NOGUEIRA, ADRIANO BARRETO; SOGAYAR, MARI CLEIDE; COLQUHOUN, ALISON; SIQUEIRA, SHEILA APARECIDA; NOGUEIRA, ARIEL BARRETO; MARCHIORI, PAULO EURIPEDES; TEIXEIRA, MANOEL JACOBSEN. Existence of a potential neurogenic system in the adult human brain. JOURNAL OF TRANSLATIONAL MEDICINE, v. 12, MAR 22 2014. Web of Science Citations: 25.
TANAKA, LEONARDO Y.; LAURINDO, FRANCISCO R. M.. Vascular remodeling: A redox-modulated mechanism of vessel caliber regulation. Free Radical Biology and Medicine, v. 109, n. SI, p. 11-21, AUG 2017. Web of Science Citations: 13. (13/17115-5, 13/07937-8, 09/54764-6)
GUIDO, MARIA C.; DEBBAS, VICTOR; SALEMI, VERA M.; TAVARES, ELAINE R.; MEIRELLES, THAYNA; ARAUJO, THAIS L. S.; NOLASCO, PATRICIA; FERREIRA-FILHO, JULIO C. A.; TAKIMURA, CELSO K.; PEREIRA, LYGIA V.; et al. Effect of the Antioxidant Lipoic Acid in Aortic Phenotype in a Marfan Syndrome Mouse Model. OXIDATIVE MEDICINE AND CELLULAR LONGEVITY, 2018. Web of Science Citations: 0. (13/07937-8, 09/54764-6)
TANAKA, LEONARDO Y.; ARAUJO, HANIEL A.; HIRONAKA, GUSTAVO K.; ARAUJO, THAIS L. S.; TAKIMURA, CELSO K.; RODRIGUEZ, ANDRES I.; CASAGRANDE, ANNELISE S.; GUTIERREZ, PAULO S.; LEMOS-NETO, PEDRO ALVES; LAURINDO, FRANCISCO R. M.. Peri/Epicellular Protein Disulfide Isomerase Sustains Vascular Lumen Caliber Through an Anticonstrictive Remodeling Effect. Hypertension, v. 67, n. 3, p. 613-622, MAR 2016. Web of Science Citations: 14. (13/07937-8, 10/06360-0, 09/54764-6)
MEIRELLES, THAYNA; ARAUJO, THAIS L. S.; NOLASCO, PATRICIA; MORETTI, ANA I. S.; GUIDO, MARIA C.; DEBBAS, VICTOR; PEREIRA, LYGIA V.; LAURINDO, FRANCISCO R.. Fibrillin-1 mg Delta(lPn) Marfan syndrome mutation associates with preserved proteostasis and bypass of a protein disulfide isomerase-dependent quality checkpoint. INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY, v. 71, p. 81-91, FEB 2016. Web of Science Citations: 5. (12/23490-0, 13/07937-8, 09/54764-6)
WATANABE, MONICA M.; LAURINDO, FRANCISCO R. M.; FERNANDES, DENISE C.. Methods of measuring protein disulfide isomerase activity: a critical overview. FRONTIERS IN CHEMISTRY, v. 2, 2014. Web of Science Citations: 15. (13/07937-8, 09/54764-6)
MORETTI, ANA I. S.; PAVANELLI, JESSYCA C.; NOLASCO, PATRICIA; LEISEGANG, MATTHIAS S.; TANAKA, LEONARDO Y.; FERNANDES, CAROLINA G.; WOSNIAK, JR., JOAO; KAJIHARA, DANIELA; DIAS, MATHEUS H.; FERNANDES, DENISE C.; et al. Conserved Gene Microsynteny Unveils Functional Interaction Between Protein Disulfide Isomerase and Rho Guanine-Dissociation Inhibitor Families. SCIENTIFIC REPORTS, v. 7, DEC 8 2017. Web of Science Citations: 5. (13/07937-8, 14/24511-7, 12/10203-3, 09/54764-6, 15/15281-0)
OLIVEIRA, PERCILLIA V. S.; LAURINDO, FRANCISCO R. M.. Implications of plasma thiol redox in disease. Clinical Science, v. 132, n. 12, p. 1257-1280, JUN 29 2018. Web of Science Citations: 10. (13/07937-8, 14/20595-1)
AMANSO, ANGELICA M.; DEBBAS, VICTOR; LAURINDO, FRANCISCO R. M.. Proteasome Inhibition Represses Unfolded Protein Response and Nox4, Sensitizing Vascular Cells to Endoplasmic Reticulum Stress-Induced Death. PLoS One, v. 6, n. 1, JAN 26 2011. Web of Science Citations: 26. (04/13683-0, 09/54764-6)
MONTEIRO, H. P.; SILVA, E. F.; STERN, A.. Nitric oxide: a potential inducer of adhesion-related apoptosis-anoikis. NITRIC OXIDE-BIOLOGY AND CHEMISTRY, v. 10, n. 1, p. 1-10, Feb. 2004. (00/12154-2)
KRIEGER, M. H.; SANTOS, K. F. R.; SHISHIDO, S. M.; WANSCHEL, A. C. B. A.; ESTRELA, H. F. G.; SANTOS, L.; OLIVEIRA, M. G. DE; FRANCHINI, K. G.; SPADARI-BRATFISCH, R. C.; LAURINDO, F. R. M.. Antiatherogenic effects of S-nitroso-N-acetylcysteine in hypercholesterolemic LDL receptor knockout mice. NITRIC OXIDE-BIOLOGY AND CHEMISTRY, v. 14, n. 1, p. 12-20, Feb. 2006. (00/12154-2)
SAN MARTIN, ALEJANDRA; FONCEA, ROCIO; LAURINDO, FRANCISCO R.; EBENSPERGER, ROBERTO; GRIENDLING, KATHY K.; LEIGHTON, FEDERICO. Nox1-based NADPH oxidase-derived superoxide is required for VSMC activation by advanced glycation end-products. Free Radical Biology and Medicine, v. 42, n. 11, p. 1671-1679, June 2007. (00/12154-2)
DE ANDRADE, C. R.; LEITE, P. F.; MONTEZANO, A. C.; CASOLARI, D. A.; YOGI, A.; TOSTES, R. C.; HADDAD, R.; EBERLIN, M. N.; LAURINDO, F. R. M.; DE SOUZA, H. P.; et al. Increased endothelin-1 reactivity and endothelial dysfunction in carotid arteries from rats with hyperhomocysteinemia. British Journal of Pharmacology, v. 157, n. 4, p. 568-580, JUN 2009. Web of Science Citations: 11. (04/13683-0)
DE BESSA, TIPHANY CORALIE; PAGANO, ALESSANDRA; SOARES MORETTI, ANA IOCHABEL; SANTOS OLIVEIRA, PERCILLIA VICTORIA; MENDONCA, SAMIR ANDRADE; KOVACIC, HERVE; MARTINS LAURINDO, FRANCISCO RAFAEL. Subverted regulation of Nox1 NADPH oxidase-dependent oxidant generation by protein disulfide isomerase A1 in colon carcinoma cells with overactivated KRas. CELL DEATH & DISEASE, v. 10, FEB 13 2019. Web of Science Citations: 1. (13/07937-8, 13/02070-6, 14/20595-1, 09/54764-6, 16/00686-8)
TANAKA, LEONARDO Y.; ARAUJO, THAIS L. S.; RODRIGUEZ, I, ANDRES; FERRAZ, MARIANA S.; PELEGATI, VITOR B.; MORAIS, MAURO C. C.; DOS SANTOS, ALINE M.; CESAR, CARLOS L.; RAMOS, ALEXANDRE F.; ALENCAR, ADRIANO M.; et al. Peri/epicellular protein disulfide isomerase-A1 acts as an upstream organizer of cytoskeletal mechanoadaptation in vascular smooth muscle cells. AMERICAN JOURNAL OF PHYSIOLOGY-HEART AND CIRCULATORY PHYSIOLOGY, v. 316, n. 3, p. H566-H579, MAR 2019. Web of Science Citations: 1. (13/07937-8, 13/17115-5, 15/06210-2)
CARMO, LUCIANA S.; BURDMANN, EMMANUEL A.; FESSEL, MELISSA R.; ALMEIDA, YOURI E.; PESCATORE, LUCIANA A.; FARIAS-SILVA, ELISANGELA; GAMARRA, LIONEL F.; LOPES, GABRIEL H.; ALOIA, THIAGO P. A.; LIBERMAN, MARCEL. Expansive Vascular Remodeling and Increased Vascular Calcification Response to Cholecalciferol in a Murine Model of Obesity and Insulin Resistance. ARTERIOSCLEROSIS THROMBOSIS AND VASCULAR BIOLOGY, v. 39, n. 2, p. 200-211, FEB 2019. Web of Science Citations: 3. (13/09652-0, 13/09611-2, 15/25923-0)
GIMENEZ, MARCELA; VERISSIMO-FILHO, SIDNEY; WITTIG, ILKA; SCHICKLING, BRANDON M.; HAHNER, FABIAN; SCHUERMANN, CHRISTOPH; NETTO, LUIS E. S.; ROSA, JOSE CESAR; BRANDES, RALF P.; SARTORETTO, SIMONE; et al. Redox Activation of Nox1 (NADPH Oxidase 1) Involves an Intermolecular Disulfide Bond Between Protein Disulfide Isomerase and p47(phox) in Vascular Smooth Muscle Cells. ARTERIOSCLEROSIS THROMBOSIS AND VASCULAR BIOLOGY, v. 39, n. 2, p. 224-236, FEB 2019. Web of Science Citations: 0. (13/07937-8, 13/03520-5, 09/54764-6)
JOSHI, SUHASINI; WANG, TAI; ARAUJO, THAIS L. S.; SHARMA, SAHIL; BRODSKY, JEFFREY L.; CHIOSIS, GABRIELA. Adapting to stress - chaperome networks in cancer. NATURE REVIEWS CANCER, v. 18, n. 9, p. 562-575, SEP 2018. Web of Science Citations: 15. (17/01130-6)
C.M. PERTRINI; A.A. MIYAKAWA; F.R.M. LAURINDO; J.E. KRIEGER. Nitric oxide regulates angiotensin-I converting enzyme under static conditions but not under shear stress. Brazilian Journal of Medical and Biological Research, v. 36, n. 9, p. 1175-1178, Set. 2003. (00/12154-2, 01/00009-0)
SANTOS DE OLIVEIRA, PERCILLIA VICTORIA; GARCIA-ROSA, SHEILA; AZEVEDO SACHETTO, ANA TERESA; SOARES MORETTI, ANA IOCHABEL; DEBBAS, VICTOR; DE BESSA, TIPHANY CORALIE; SILVA, NATHALIA TENGUAN; PEREIRA, ALEXANDRE DA COSTA; MARTINS-DE-SOUZA, DANIEL; SANTORO, MARCELO LARAMI; et al. Protein disulfide isomerase plasma levels in healthy humans reveal proteomic signatures involved in contrasting endothelial phenotypes. REDOX BIOLOGY, v. 22, APR 2019. Web of Science Citations: 0. (13/07937-8, 13/25177-0, 18/07511-4, 13/08711-3, 17/19866-9, 17/25588-1, 14/10068-4, 14/20595-1)
ARAUJO, THAIS L. S.; VENTURINI, GABRIELA; MORETTI, ANA I. S.; TANAKA, LEONARDO Y.; PEREIRA, ALEXANDRE COSTA; LAURINDO, FRANCISCO R. M.. Cell-surface HSP70 associates with thrombomodulin in endothelial cells. CELL STRESS & CHAPERONES, v. 24, n. 1, p. 273-282, JAN 2019. Web of Science Citations: 1. (13/07937-8, 15/06210-2)
AMANSO‚ A.M.; DEBBAS‚ V.; LAURINDO‚ F.R.M.. Proteasome Inhibition Represses Unfolded Protein Response and Nox4‚ Sensitizing Vascular Cells to Endoplasmic Reticulum Stress-Induced Death. PLoS One, v. 6, n. 1, p. e14591, 2011. (04/13683-0, 09/54764-6)
ARAI, ROBERTO J.; OGATA, FERNANDO T.; BATISTA, WAGNER L.; MASUTANI, HIROSHI; YODOI, JUNJI; DEBBAS, VICTOR; AUGUSTO, OHARA; STERN, ARNOLD; MONTEIRO, HUGO P.. Thioredoxin-1 promotes survival in cells exposed to S-nitrosoglutathione: Correlation with reduction of intracellular levels of nitrosothiols and up-regulation of the ERK1/2 MAP Kinases. Toxicology and Applied Pharmacology, v. 233, n. 2, p. 227-237, DEC 1 2008. Web of Science Citations: 23. (00/12154-2)
PESCATORE, LUCIANA A.; GAMARRA, LIONEL F.; LIBERMAN, MARCEL. Multifaceted Mechanisms of Vascular Calcification in Aging. ARTERIOSCLEROSIS THROMBOSIS AND VASCULAR BIOLOGY, v. 39, n. 7, p. 1307-1316, JUL 2019. Web of Science Citations: 0. (16/17961-1, 16/21470-3, 15/25923-0)
(References retrieved automatically from State of São Paulo Research Institutions)
ALVES, Luciana Pescatore. Papel da dissulfeto isomerase proteica (PDI) na migração de células musculares lisas vasculares: possível envolvimento de Nox1 NADPH oxidase e RhoGTPases. 2012. Tese (Doutorado) – Faculdade de Medicina. Universidade de São Paulo (USP). São Paulo. (07/53171-6)