10 research outputs found
Mutations in Protein-Binding Hot-Spots on the Hub Protein Smad3 Differentially Affect Its Protein Interactions and Smad3-Regulated Gene Expression
- Author
- A Moustakas
- A Moustakas
- A Sultana
- AA Bogan
- B Ma
- BM Chacko
- BM Zhao
- BY Qin
- Chateen Krueger
- CJ Tsai
- D Goto
- D Javelaud
- D Koinuma
- D Liu
- D Liu
- D Reichmann
- Dhyan Chandra
- E Cukuroglu
- E Piek
- E Wiercinska
- EN Olson
- F. Michael Hoffmann
- G Fibbi
- G Kennedy
- G Wu
- G Xu
- GJ Prud'homme
- GR Warnes
- H Ikushima
- HJ Lee
- II Nagy
- IM van de Laar
- IS Moreira
- IW Taylor
- J Dzwonek
- J Gupta
- J He
- J Massague
- J Massague
- J Massague
- J Rosenbloom
- J Seoane
- J Webber
- J Webber
- J Xu
- JE Lai-Cheong
- JE Lai-Cheong
- JE Lai-Cheong
- JF Rual
- JM Hernandez-Hernandez
- JW Wu
- JW Wu
- JW Wu
- K Eppert
- K Verschueren
- KA Brown
- Kenneth A. Satyshur
- L Izzi
- L Vardouli
- L Xu
- L Xu
- L Zheng
- M Barrios-Rodiles
- M Furuhashi
- M Kioulafa
- M Kondo
- M Mizuide
- M Shiroishi
- M Tyagi
- M Weinstein
- MB Sporn
- Michael A. Newton
- Michelle M. Schiro
- N Nakaya
- NJ Burgoyne
- NL Malinin
- Norman R. Drinkwater
- O Keskin
- P Bernasconi
- P ten Dijke
- P Uetz
- PA Chong
- PL Zeeuwen
- Q Cui
- R Chen
- R Derynck
- R Janknecht
- RA Randall
- RD Cohn
- RM Simpson
- S Birtalan
- S Dennler
- S Germain
- Sara E. Stauber
- SK Lim
- SM Pulukuri
- Steven J. Darnell
- SZ Zhang
- T Clackson
- T Tsukazaki
- Tami L. Peterson
- W Chen
- WC Chou
- X Lin
- Y Kang
- Y Kang
- Y Shi
- Y Shi
- Y Shi
- Y Zhang
- YG Chen
- Publication venue
- Public Library of Science
- Publication date
- 19/09/2011
- Field of study
Hub proteins are connected through binding interactions to many other proteins. Smad3, a mediator of signal transduction induced by transforming growth factor beta (TGF-β), serves as a hub protein for over 50 protein-protein interactions. Different cellular responses mediated by Smad3 are the product of cell-type and context dependent Smad3-nucleated protein complexes acting in concert. Our hypothesis is that perturbation of this spectrum of protein complexes by mutation of single protein-binding hot-spots on Smad3 will have distinct consequences on Smad3-mediated responses.We mutated 28 amino acids on the surface of the Smad3 MH2 domain and identified 22 Smad3 variants with reduced binding to subsets of 17 Smad3-binding proteins including Smad4, SARA, Ski, Smurf2 and SIP1. Mutations defective in binding to Smad4, e.g., D408H, or defective in nucleocytoplasmic shuttling, e.g., W406A, were compromised in modulating the expression levels of a Smad3-dependent reporter gene or six endogenous Smad3-responsive genes: Mmp9, IL11, Tnfaip6, Fermt1, Olfm2 and Wnt11. However, the Smad3 mutants Y226A, Y297A, W326A, K341A, and E267A had distinct differences on TGF-β signaling. For example, K341A and Y226A both reduced the Smad3-mediated activation of the reporter gene by ∼50% but K341A only reduced the TGF-β inducibilty of Olfm2 in contrast to Y226A which reduced the TGF-β inducibility of all six endogenous genes as severely as the W406A mutation. E267A had increased protein binding but reduced TGF-β inducibility because it caused higher basal levels of expression. Y297A had increased TGF-β inducibility because it caused lower Smad3-induced basal levels of gene expression.Mutations in protein binding hot-spots on Smad3 reduced the binding to different subsets of interacting proteins and caused a range of quantitative changes in the expression of genes induced by Smad3. This approach should be useful for unraveling which Smad3 protein complexes are critical for specific biological responses
Using Focus Groups for Program Planning and Evaluation
- Author
- Ansay SJ
- Ayala GX
- Cameron KA
- Debevc M
- Denham SA
- Gilbert LK
- Goodman D
- Hathout E
- Heary CM
- Horner SD
- Kennedy C
- Kubik MY
- Large A
- Mail PD
- McEwan MJ
- McLafferty I
- Owen S
- Parlove AE
- Patricia B. Krauskopf
- Patterson DL
- Peremans L
- Peterson-Sweeney K
- Rachel Davidson
- Renner CC
- Rhee H
- Rhee H
- Robinson N
- Ronen GM
- Tami H. Wyatt
- Wagenaar AC
- Webb C
- Wilson DK
- Wyatt TH
- Publication venue
- 'SAGE Publications'
- Publication date
- Field of study
Evolocumab and clinical outcomes in patients with cardiovascular disease
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- Abelson M.
- Aboufakher R.
- Abrahamsen T. E.
- Accini Mendoza J. L.
- Acheatel R.
- Ackermann D.
- Adamkova V.
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- Ahsan A.
- Ainsworth P.
- Airody Govinda R.
- Akai A.
- Ako J.
- Al-Bahrani A.
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- Aldegather J.
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- Alt I.
- Alzohaili O.
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- Publication venue
- 'Massachusetts Medical Society'
- Publication date
- 01/01/2017
- Field of study
peer reviewedBACKGROUND Evolocumab is a monoclonal antibody that inhibits proprotein convertase subtilisin-kexin type 9 (PCSK9) and lowers low-density lipoprotein (LDL) cholesterol levels by approximately 60%. Whether it prevents cardiovascular events is uncertain. METHODS We conducted a randomized, double-blind, placebo-controlled trial involving 27,564 patients with atherosclerotic cardiovascular disease and LDL cholesterol levels of 70 mg per deciliter (1.8 mmol per liter) or higher who were receiving statin therapy. Patients were randomly assigned to receive evolocumab (either 140 mg every 2 weeks or 420 mg monthly) or matching placebo as subcutaneous injections. The primary efficacy end point was the composite of cardiovascular death, myocardial infarction, stroke, hospitalization for unstable angina, or coronary revascularization. The key secondary efficacy end point was the composite of cardiovascular death, myocardial infarction, or stroke. The median duration of follow-up was 2.2 years. RESULTS At 48 weeks, the least-squares mean percentage reduction in LDL cholesterol levels with evolocumab, as compared with placebo, was 59%, from a median baseline value of 92 mg per deciliter (2.4 mmol per liter) to 30 mg per deciliter (0.78 mmol per liter) (P<0.001). Relative to placebo, evolocumab treatment significantly reduced the risk of the primary end point (1344 patients [9.8%] vs. 1563 patients [11.3%]; hazard ratio, 0.85; 95% confidence interval [CI], 0.79 to 0.92; P<0.001) and the key secondary end point (816 [5.9%] vs. 1013 [7.4%]; hazard ratio, 0.80; 95% CI, 0.73 to 0.88; P<0.001). The results were consistent across key subgroups, including the subgroup of patients in the lowest quartile for baseline LDL cholesterol levels (median, 74 mg per deciliter [1.9 mmol per liter]). There was no significant difference between the study groups with regard to adverse events (including new-onset diabetes and neurocognitive events), with the exception of injection-site reactions, which were more common with evolocumab (2.1% vs. 1.6%). CONCLUSIONS In our trial, inhibition of PCSK9 with evolocumab on a background of statin therapy lowered LDL cholesterol levels to a median of 30 mg per deciliter (0.78 mmol per liter) and reduced the risk of cardiovascular events. These findings show that patients with atherosclerotic cardiovascular disease benefit from lowering of LDL cholesterol levels below current targets. © 2017 Massachusetts Medical Society
Cardiovascular Efficacy and Safety of Bococizumab in High-Risk Patients
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- Wang D.
- Wang Ellen
- Wang G.
- Wang Y.
- Wasserburger B.
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- Weber K.
- Wegner John
- Wei Caimiao
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- Welty Francine
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- Wermuth S.
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- Wetzel T.
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- William M.
- Williams D. G.
- Williams M.
- Willis J. G.
- Willits V. L.
- Winkelmann B.
- Witt N.
- Wittmann I.
- Woehrle J.
- Worner Diz F.
- Wozniak I.
- Wright R. S.
- Wronska D.
- Wuerzner G.
- Wychota K.
- Xu P.
- Xue L.
- Yakusevich V. V.
- Yang P.
- Yang X.
- Yao L. C.
- Yared Z.
- Yarows S. A.
- Yigit Z.
- Yoon J.
- Yunis C.
- Zadra R.
- Zaidman C. J.
- Zamorano Gomez J. L.
- Zannad Faiez
- Zarandon R. B. S.
- Zarich S. W.
- Zateyshchikov D.
- Zavaro S. H.
- Zebrack J. S.
- Zeig S.
- Zemek S.
- Zemour G.
- Zeng X.
- Zeno M. L.
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- Zidkova E.
- Zieba B.
- Zilahi Z.
- Zoet-Nugteren S. K.
- Zrazhevskiy K.
- Zubek V.
- Publication venue
- 'Massachusetts Medical Society'
- Publication date
- 01/01/2017
- Field of study
BACKGROUN
Evolocumab and clinical outcomes in patients with cardiovascular disease
- Author
- Abelson M
- Aboufakher R
- Abrahamsen Te
- Accini Mendoza Jl
- Acheatel R
- Ackermann D
- Adamkova V
- Adams M
- Adlam D
- Aggarwal R
- Aggarwal S
- Ahsan A
- Ainsworth P
- Airody Govinda R
- Akai A
- Ako J
- Al-Bahrani A
- Al-Joundi T
- Aldegather J
- Aldrete Velasco Ja
- Alfieri A
- Alt I
- Alzohaili O
- Amerena J
- Amin J
- Amoedo R
- Amuchastegui M
- Anderson T
- Andreka P
- Andreotti F
- Angoulvant D
- Ansell B
- Antalik L
- Antkowiak-Piatyszek K
- Appel K
- Arakawa T
- Arana Londoño C
- Ardissino D
- Ardito Wr
- Arkhipov M
- Arsenescu-Georgescu C
- Asamoah N
- Ascaso Gimilio Jf
- Atar S
- Atassi K
- Athyros V
- Auerbach E
- Awtry E
- Baass A
- Badariene J
- Badat A
- Badila E
- Bae J
- Baigent C
- Bain S
- Baird I
- Baker J
- Balbay Y
- Baldari D
- Ballantyne C
- Bammert A
- Banach M
- Bandh S
- Banerjee S
- Banik M
- Banikova A
- Barbarash O
- Barcinas R
- Barnum O
- Barroso de Souza Wk
- Bart B
- Barton J
- Bata I
- Batalla E
- Bayat J
- Bazzoni Ruiz Ae
- Bednarkiewicz Z
- Beer Hj
- Begg A
- Beltrame J
- Bendermacher P
- Benton R
- Berger C
- Bergeron J
- Bergler-Klein J
- Berglund S
- Berlacher P
- Bernstein M
- Bertolet B
- Bertolim Precoma D
- Bhagwat R
- Bhargava R
- Bhushan R
- Biasucci Lm
- Bilianou H
- Blagden M
- Blaha V
- Blasko P
- Blicharski T
- Blignaut S
- Blokhin A
- Blumberg E
- Bodanese Lc
- Bokern M
- Bolshakova O
- Bonaca Mp
- Bonnet B
- Bosiljanoff P
- Boswijk D
- Botero Lopez R
- Bourhaial H
- Bousboulas S
- Brabec T
- Brezina B
- Bronnum-Schou J
- Brotanek J
- Broughton R
- Brown C
- Brown Wv
- Bubnova M
- Budoff M
- Burgess L
- Burianova H
- Burrough B
- Butler R
- Buysschaert I
- Bystryk L
- Capps N
- Cappuccio F
- Cardona Muñoz Eg
- Carhart R
- Cariou B
- Carr K
- Case C
- Castellanos Bueno R
- Catez E
- Caulfield M
- Cayla G
- Cech V
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- Cha J
- Chandra L
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- Charng Mj
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- Chauhan A
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- Chehayeb R
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- Cheung D
- Cho Y
- Choi D
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- Christofides E
- Cifkova R
- Civeira Murillo F
- Cizinsky S
- Clardy D
- Claxton E
- Clements B
- Cobos Jl
- Coching Rm
- Coetzer Tf
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- Colombo H
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- Cuneo C
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- Dabrowski M
- Dahlén G
- Dai H
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- Darius H
- Dauber I
- Dave K
- Davila W
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- Dawood S
- de Belder M
- De Caterina R
- De Ferrari Gm
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- De los Rios Ibarra Mo
- De Meulemeester M
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- Duarte Barbosa Ec
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- Dyke C
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- Farshid A
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- Fernandes Manenti Er
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- Im K
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- Izumiya Y
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- Joffe I
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- Joshi A
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- Kakurina N
- Kanevsky E
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- Karen I
- Karpenko O
- Kashyap M
- Kassner U
- Kast P
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- Kawabata K
- Kawamitsu K
- Kawasaki T
- Kayikcioglu L
- Kazdera P
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- Keeling P
- Kellnerova I
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- Kerr Saraiva Jf
- Khalife K
- Khan A
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- Khanoyan P
- Khurana S
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- Kinasz L
- King M
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- Kinova E
- Kirma C
- Kirstein J
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- Kjaerulf Jensen H
- Klausen Ic
- Klimsa Z
- Klug E
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- Knusel B
- Kobalava Z
- Kochiadakis G
- Koga Y
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- Kooij A
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- Kopytsya M
- Koren M
- Kork A
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- Korzh O
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- Kosior D
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- Kothiwale V
- Kovar F
- Kozlowski L
- Kozuma K
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- Kraіz I
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- Kubica J
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- Kurtz Lisboa Hr
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- Landzberg J
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- Zilahi Z
- Zrazhevskiy K
- Östergren J
- Publication venue
- 'Massachusetts Medical Society'
- Publication date
- 01/01/2017
- Field of study
BACKGROUND Evolocumab is a monoclonal antibody that inhibits proprotein convertase subtilisin-kexin type 9 (PCSK9) and lowers low-density lipoprotein (LDL) cholesterol levels by approximately 60%. Whether it prevents cardiovascular events is uncertain. METHODS We conducted a randomized, double-blind, placebo-controlled trial involving 27,564 patients with atherosclerotic cardiovascular disease and LDL cholesterol levels of 70 mg per deciliter (1.8 mmol per liter) or higher who were receiving statin therapy. Patients were randomly assigned to receive evolocumab (either 140 mg every 2 weeks or 420 mg monthly) or matching placebo as subcutaneous injections. The primary efficacy end point was the composite of cardiovascular death, myocardial infarction, stroke, hospitalization for unstable angina, or coronary revascularization. The key secondary efficacy end point was the composite of cardiovascular death, myocardial infarction, or stroke. The median duration of follow-up was 2.2 years. RESULTS At 48 weeks, the least-squares mean percentage reduction in LDL cholesterol levels with evolocumab, as compared with placebo, was 59%, from a median baseline value of 92 mg per deciliter (2.4 mmol per liter) to 30 mg per deciliter (0.78 mmol per liter) (P<0.001). Relative to placebo, evolocumab treatment significantly reduced the risk of the primary end point (1344 patients [9.8%] vs. 1563 patients [11.3%]; hazard ratio, 0.85; 95% confidence interval [CI], 0.79 to 0.92; P<0.001) and the key secondary end point (816 [5.9%] vs. 1013 [7.4%]; hazard ratio, 0.80; 95% CI, 0.73 to 0.88; P<0.001). The results were consistent across key subgroups, including the subgroup of patients in the lowest quartile for baseline LDL cholesterol levels (median, 74 mg per deciliter [1.9 mmol per liter]). There was no significant difference between the study groups with regard to adverse events (including new-onset diabetes and neurocognitive events), with the exception of injection-site reactions, which were more common with evolocumab (2.1% vs. 1.6%). CONCLUSIONS In our trial, inhibition of PCSK9 with evolocumab on a background of statin therapy lowered LDL cholesterol levels to a median of 30 mg per deciliter (0.78 mmol per liter) and reduced the risk of cardiovascular events. These findings show that patients with atherosclerotic cardiovascular disease benefit from lowering of LDL cholesterol levels below current targets
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- Author
- Abad Vanessa
- Abate Getahun
- Abbas Anum
- Ackerman Jamie
- Ackerman Ronald
- Ackermann Jeremy
- Adams Atoya
- Adams Mark S.
- Adams Michael R.
- Adelglass Jeffrey
- Afework Sarah
- Ahmad Nina
- Akamine Christine
- Ake Julie A.
- Al-Ibrahim Mohamed S.
- Albert Gary
- Alcaide Maria L.
- Alderson Nathan
- Aleman Lily
- Alemán José O.
- Allaw Mohammed
- Alva E. Javier Pretell
- Alvarado Hilario
- Amador Carmen
- Andersen James
- Anderson Corey G.
- Anderson Evan J.
- Anderson Victoria R.
- Andes David R.
- Andrasik Michele P.
- Andree Stephanie
- Andrews Jeb
- Andriesen Jessica G.
- Andriulis Victoria
- Ansel Jessica L.
- Anthony Codi M.
- Antwi Mohammed
- Arduino Roberto C.
- Aristy Florida
- Arnold Valerie K.
- Arrazcaeta Alicia
- Atmar Robert L.
- Avworo Ayoade
- Bacher Christina
- Baden Lindsey R.
- Badillo Diana
- Bainbridge Emma
- Baka Michele
- Baker Sherrie
- Balani Bindu
- Ball Brandy
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- Barranco-Santana Elizabeth
- Bartilucci Darlene
- Bashour Jennifer
- Batteiger Teresa A.
- Baudelaire Clarisse
- Bazan Jose A.
- Becerra Maria G.
- Becker Teresa
- Beckmann David
- Bedimo Roger J.
- Belhorn Linda R.
- Benavides Alfredo Gilberto Guerreros
- Beninati Genevieve
- Benitez Jorge A.
- Bennett Annette R.
- Bennett Elizabeth
- Beresnev Tatiana
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- Bermudez Maria I.
- Bernard Marcia
- Bernstein David I.
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- Billings Joanne L.
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- Rivera Juana
- Rivera María I.
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- Takizala Zudi-Mwak
- Takuva Simbarashe G.
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- Utz Gregory C.
- Vachris Timothy P.
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- Valika Insiya
- Van Der Leden Mimi
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- Viens Nicholas A.
- Villegas Marysol
- Vingerhoets Johan
- Vogler Mary
- Vowell Mandy
- Vrbicky Keith W.
- Wahlin Tami
- Wakefield Paul H.
- Wald Anna
- Walker James
- Walker Shannon
- Walsh Edward E.
- Walsh Mary C.
- Walsh Stephen R.
- Walsh Stephen R.
- Walter Emmanuel B.
- Walters Ayanna
- Wang Tina
- Warden Ashley
- Waters Michael
- Watkins Breanz
- Webb Angella
- Webster Hala
- Weidler Jessica L.
- Weiss Thomas
- Wells Margaret
- Wendell Lewis III
- Wendrow Andrea
- Werne Melody
- West Whitney
- Whatley Jordan L.
- Whitaker Jennifer A.
- White Jewel J.
- White Julie
- White Toni
- Wijewardane Priyantha N.
- Wilkin Timothy
- Wilkinson Bethanie
- William S. Davis Jr
- Williams Barton G.
- Williams Hayes
- Williams Samantha
- Wilson Christine
- Wilson Clint
- Wilson Greg
- Wilson Natasha
- Winbigler Jennifer
- Winkle Peter J.
- Winokur Patricia L.
- Witbeck John
- Wohl David
- Woo Wayne
- Woodside Leana
- Wortman Glenn
- Wu Yi H.
- Wylie Paul E.
- Yang Fan
- Yang Kinara S.
- Yoon Anelgine C.
- York Jill
- Young Cheryl
- Yu Chenchen
- Yusin Joseph
- Zapata Luz
- Zash Rebecca
- Zegarra Eneyda Giuvanela Llerena
- Zemanek Arthur L.
- Zenlea Kate
- Zepeda Karla
- Zervos Marcus J.
- Zhai Nan
- Zhang Kevin
- Zhou James
- Zimmer Andrea
- Zingman Barry S.
- Zorrilla Carmen D.
- Áñez Germán
- Publication venue
- 'Elsevier BV'
- Publication date
- 01/10/2023
- Field of study
Background: While vaccines have established utility against COVID-19, phase 3 efficacy studies have generally not comprehensively evaluated protection provided by previous infection or hybrid immunity (previous infection plus vaccination). Individual patient data from US government-supported harmonized vaccine trials provide an unprecedented sample population to address this issue. We characterized the protective efficacy of previous SARS-CoV-2 infection and hybrid immunity against COVID-19 early in the pandemic over three-to six-month follow-up and compared with vaccine-associated protection. Methods: In this post-hoc cross-protocol analysis of the Moderna, AstraZeneca, Janssen, and Novavax COVID-19 vaccine clinical trials, we allocated participants into four groups based on previous-infection status at enrolment and treatment: no previous infection/placebo; previous infection/placebo; no previous infection/vaccine; and previous infection/vaccine. The main outcome was RT-PCR-confirmed COVID-19 >7–15 days (per original protocols) after final study injection. We calculated crude and adjusted efficacy measures. Findings: Previous infection/placebo participants had a 92% decreased risk of future COVID-19 compared to no previous infection/placebo participants (overall hazard ratio [HR] ratio: 0.08; 95% CI: 0.05–0.13). Among single-dose Janssen participants, hybrid immunity conferred greater protection than vaccine alone (HR: 0.03; 95% CI: 0.01–0.10). Too few infections were observed to draw statistical inferences comparing hybrid immunity to vaccine alone for other trials. Vaccination, previous infection, and hybrid immunity all provided near-complete protection against severe disease. Interpretation: Previous infection, any hybrid immunity, and two-dose vaccination all provided substantial protection against symptomatic and severe COVID-19 through the early Delta period. Thus, as a surrogate for natural infection, vaccination remains the safest approach to protection. Funding: National Institutes of Health
Risk of COVID-19 after natural infection or vaccinationResearch in context
- Author
- A. Lina Rosengren
- Abram Burgher
- Adam B. Brosz
- Adam Rosen
- Adam Schwartz
- Adriana Sordo Duran
- Adrienna Marquez
- Adrienne E. Shapiro
- Aeiress Duhart
- Afsoon Roberts
- Albert Liu
- Alejandro Hoberman
- Alejandro Quintín Barrat Hernández
- Alex Greninger
- Alexander Clark
- Alfredo Gilberto Guerreros Benavides
- Alice McGarry
- Alicia Arrazcaeta
- Alisha Lutat
- Alison Bondell
- Alison Pellecchia
- Allie Oplinger
- Allison Green
- Allison O'Brien
- Alpa Patel
- Alyssa-Kay Peay
- Amanda Horn
- Amanda Lilienthal
- Amanda Occhino
- Amanda Philyaw
- Amaran Moodley
- Amber Grant
- Amber Stanford
- Amesika Nyaku
- Amie Shannon
- Amina Z. Haggag
- Amit Paliwal
- Amy Caldwell
- Amy Chamberlain
- Amy Dye
- Amy Falk
- Amy Kelley
- Amy Medina
- Amy Potts
- Amy Salzl
- Amy Sherman
- Amy Starr
- Amy Thompson
- Andrea Berry
- Andrea Clement
- Andrea Wendrow
- Andrea Zimmer
- Andres Bran
- Andres Camacho-Gonzalez
- Andrew Lauria
- Andrew McConnell
- Andrew McWilliams
- Anelgine C. Yoon
- Angela Lee
- Angela R. Branche
- Angelica Kottkamp
- Angella Webb
- Ann M. Milliken
- Ann R. Falsey
- Anna S. Lok
- Anna Wald
- Anne Marit de Groot
- Anne-Marie Rick
- Annette R. Bennett
- Annie Ciambruschini
- Annie Luetkemeyer
- Anthony Kim
- Anum Abbas
- Anyela Lara
- April Pixler
- Ariana C. Stanton
- Arthur L. Zemanek
- Asha Inniss
- Ashley Kennedy
- Ashley Perez
- Ashley Warden
- Asif Noor
- Atoya Adams
- Aurelio Cruz-Valdez
- Austin Chan
- Austin Swanson
- Ayanna Walters
- Ayoade Avworo
- Bailey Jordan
- Barbara Corral
- Barbara Rizzardi
- Barbara Rizzardi
- Barbara S. Taylor
- Barry S. Zingman
- Barton G. Williams
- Beatriz Grinsztejn
- Becky Martinez
- Ben Ladner
- Benjamin Eckhardt
- Benjamin J. Luft
- Bernard Grunstra
- Beth Safirstein
- Bethanie Wilkinson
- Beverly E. Sha
- Beverly Ewing
- Bindu Balani
- Blanca Gomez
- Bo Shopsin
- Boerries Brandenburg
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- Brandy Ball
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- Brit Sovic
- Brittany Feijoo
- Brittany Stewart
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- Bruce G. Rankin
- Bruce McClenathan
- Bruno Valenti
- Bryan Gordon
- C. Mary Healy
- Caitlin J. Guiney
- Caitlin Moran
- Candace Smith
- Candice Montros
- Carina A. Rodriguez
- Carl Fichtenbaum
- Carl P. Griffin
- Carlos A. Fierro
- Carlos del Rio
- Carlos Lopez
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- Carmel B. Dyer
- Carmen A. Paez
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- Carmen D. Zorrilla
- Carmen Medina
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- Carol Kauffman
- Carol L. Mitchell
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- Chen S. Tan
- Chenchen Yu
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- Chinar Desai
- Christian Tomaszewski
- Christina A. Rostad
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- Jaleh Ostovar
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- Uriel R. Felsen
- Valentine M. Ebuh
- Valeria D. Cantos
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- Vanessa Abad
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- Victoria Mosteller
- Victoria R. Anderson
- Vida Veronica Ruiz Herrera
- Vincent Huynh
- Vincent Mirkil
- Vivek Rajasekhar
- Viviana Gonzalez
- Vladimir Berthaud
- Walter Patton
- Wanda Ramon
- Waseem Chughtai
- Wayne L. Harper
- Wayne Woo
- Wendell Lewis
- Wendell Lewis III
- Wendy A. Keitel
- Wesley Campbell
- Wesley Van Ever
- Westly Keating
- Whitney West
- Will Hernandez
- William B. Davis
- William B. Smith
- William H. Jones
- William Jennings
- William Kirby
- William P. Silver
- William R. Hartman
- William S. Davis Jr.
- William Schnitz
- William Seger
- Winniberg Stephany Alvarez León
- Winston Cavert
- Xiaomi Tong
- Yaa D. Oppong
- Yi H. Wu
- Ying Huang
- Yogesh K. Paliwal
- Youyi Fong
- Yunda Huang
- Yunda Huang
- Yvonne Davis
- Zachary Bittner
- Zainab Rizvi
- Zindy Yazmín Zárate Hinojosa
- Zudi-Mwak Takizala
- Publication venue
- Elsevier
- Publication date
- 01/10/2023
- Field of study
Summary: Background: While vaccines have established utility against COVID-19, phase 3 efficacy studies have generally not comprehensively evaluated protection provided by previous infection or hybrid immunity (previous infection plus vaccination). Individual patient data from US government-supported harmonized vaccine trials provide an unprecedented sample population to address this issue. We characterized the protective efficacy of previous SARS-CoV-2 infection and hybrid immunity against COVID-19 early in the pandemic over three-to six-month follow-up and compared with vaccine-associated protection. Methods: In this post-hoc cross-protocol analysis of the Moderna, AstraZeneca, Janssen, and Novavax COVID-19 vaccine clinical trials, we allocated participants into four groups based on previous-infection status at enrolment and treatment: no previous infection/placebo; previous infection/placebo; no previous infection/vaccine; and previous infection/vaccine. The main outcome was RT-PCR-confirmed COVID-19 >7–15 days (per original protocols) after final study injection. We calculated crude and adjusted efficacy measures. Findings: Previous infection/placebo participants had a 92% decreased risk of future COVID-19 compared to no previous infection/placebo participants (overall hazard ratio [HR] ratio: 0.08; 95% CI: 0.05–0.13). Among single-dose Janssen participants, hybrid immunity conferred greater protection than vaccine alone (HR: 0.03; 95% CI: 0.01–0.10). Too few infections were observed to draw statistical inferences comparing hybrid immunity to vaccine alone for other trials. Vaccination, previous infection, and hybrid immunity all provided near-complete protection against severe disease. Interpretation: Previous infection, any hybrid immunity, and two-dose vaccination all provided substantial protection against symptomatic and severe COVID-19 through the early Delta period. Thus, as a surrogate for natural infection, vaccination remains the safest approach to protection. Funding: National Institutes of Health
Cardiovascular Efficacy and Safety of Bococizumab in High-Risk Patients
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- Gorog Da
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- Gottlieb Dw
- Gottsater A
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- Graff A
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- Madu Ij
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- Maggioni A
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- Makam Sk
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- Malik A
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- Mangili Oc
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- Manoj A
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- Markovic Tp
- Marshall A
- Marten I
- Martens Fm
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- Motylev I
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- Muniz Grijalvo O
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- Murcia A
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- Nikolaev Ky
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- Pei D
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- Pinto Sala X
- Pinto D
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- Plaza Perez I
- Plazas Ja
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- Plowchalk D
- Pluto Tm
- Pock J
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- Polanczyk Ca
- Ponikowski P.
- Pons Amate Jm
- Pop Cf
- Popa Ar
- Popescu A
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- Popoviciu Ms
- Porcu M
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- Potthoff S
- Pouzar Je
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- Prasada S
- Precoma Db
- Pretorius Ce
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- Pride Y
- Probst V
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- Proietto J
- Promisloff Sd
- Pryke Jr
- Przekwas-Jaruchowska M
- Pudi Kk
- Puhakka M
- Purdy Da
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- Quyyumi Aa
- Rabahi F
- Radin Dm
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- Rai A
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- Ramstad Ds
- Randall Wj
- Randhawa Pm
- Range G
- Ranjith N
- Raoof Tj
- Raslova K
- Rasmanis G
- Rasmussen Tk
- Rech Rl
- Reddy Rd
- Redifer P
- Reed R
- Reedy Ma
- Reiber I
- Reis G
- Remmen Jj
- Rendell Ms
- Rensing Bj
- Resende Es
- Reshetko O
- Resk Jh
- Revkin J.
- Reyes Rg
- Reyna Ls
- Reynolds Rd
- Rhee My
- Rhudy Jm
- Rice S
- Rickers H
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- Rictor Kw
- Ridker P. M.
- Riesenberg Ra
- Rigolosi R
- Rihani R
- Riksen Np
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- Rinke A
- Riojas Charles Cm
- Ripoll Vera Tv
- Risser Ja
- Ritt Le
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- Robinson Jg
- Robinson Mf
- Robles Iniesta A
- Rocco Mb
- Rodriguez Ij
- Rodriguez Wr
- Rodriguez-Briones I
- Roman G
- Roman O
- Romer Tj
- Romero Hinojosa Ja
- Roncon L
- Ronner E
- Roos Js
- Roosen J
- Roquer Gonzalez J
- Rosenfeld Jc
- Rosenstock J
- Roskova E
- Ross S
- Rossi Pr
- Roubille F
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- Rozpondek P
- Rubenfire M
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- Ruoff Ge
- Rusculleda Mm
- Rusicka T
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- Saini S
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- Schroe Hh
- Schuchard Tn
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- Solodky A
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- Somogyi A
- Soosova I
- Soran H.
- Soroka E
- Sosa-Padilla Ma
- Soto Gonzalez A
- Soto Jr
- Sotolongo R
- Sotolongo Rp
- Soufflet V
- Sparks J
- Spence Jd
- Srimahachota S
- Sritara P
- Sritara P
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- St-Amour E
- Staab Pk
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- Stawowy P
- Steffensen R
- Steinberg Aa
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- Stellbrink C
- Sternieri Mv
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- Strain Je
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- Stringam So
- Strobl Dj
- Strzinek Ra
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- Styczkiewicz M
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- Suarez-Fernandez C
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- Sullivan B
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- Sultan S
- Sumbal J
- Suomi J
- Supronik J
- Suryanarayana Pg
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- Sydo T
- Sykulski R
- Szilagyi I
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- Teitelbaum I
- Tellier G
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- Tengmark Bo
- Ternouth If
- Terns Riera M
- Terrelonge Ae
- The Sh
- Thoeng J
- Thom S
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- Thouvenot E
- Ti Z
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- Tinahones Madueno Fj
- Tivadar S
- Tofe Povedano S
- Toldy-Schedel E
- Tolkacheva V
- Torre Amione G
- Tortensson I
- Toth K
- Toth L
- Townsend Jc
- Traboulssi Ma
- Treasure Cb
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- Trenk D
- Triana Eh
- Trimarco B
- Trippett Jm
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- Tökgozoğlu L
- Ueng Kc
- Uhliar R
- Ulla Mr
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- Updegrove Jd
- Uresin Ay
- Urhammer S
- Urina M
- Urina-Triana Ma
- Uusinarkaus Kt
- Vaca Ce
- Vahed Ya
- Valdez Lopez Hg
- Valtonen M
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- van Beek E
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- van de Wal Rm
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- van de Wiel A
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- van der Zwaan Ct
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- van Hal Jm
- Van het Hof-Wiersma Jj
- van Kempen Ww
- Van Koningsbruggen P
- van Landegem P
- van Leendert Rj
- van Nieuwenhuizen E
- van Rossum P
- van Royen N
- van Zyl Lj
- Vannatta B
- Vanttinen E
- Varleta P
- Vazan A
- Vazquez-Tanus Jb
- Veenendaal A
- Vejar M
- Venereo Jm
- Venter Dj
- Verdeza C
- Vertes A
- Vervoort G
- Verwerft J
- Vesely J
- Vico Ml
- Viergever Ep
- Viklund J
- Vila Belmonte A
- Villaman-Bencosme Y
- Vinanska D
- Vincent J.
- Vincent S
- Vinyoles Bargallo E
- Violante Ortiz R
- Vishlitzky V
- Vishneva E
- Visser Rp
- Visseren F
- Vivekananthan K
- Vizel S
- Vlach Jj
- Vodnansky P
- Voehringer Hf
- Vogel Dr
- Vohnout B
- Vojacek J
- Volkova A
- Voller H
- von Engelhardt Cb
- von Hodenberg Ef
- Vora Kn
- Vora Sk
- Voros P
- Vrablik M.
- Vrkoc J
- Vukotic G
- Wadud K
- Wainstein J
- Wakefield Ph
- Wakeling J
- Walczak M
- Walczewska J
- Walukiewica P
- Wang D
- Wang E
- Wang G
- Wang Y
- Wasserburger B
- Waxler Ar
- Wayne Jd
- Weber D
- Weber K
- Wegner J
- Wei C
- Weigmann I
- Weinstein Dl
- Weiss R
- Welker Ja
- Welty F
- Wenetz Lm
- Wermuth S
- Wesson T
- West Sh
- Westerndorp I
- Wetzel T
- White H.
- Whitlock L
- Whitney Rt
- Wiggers H
- William M
- Williams Dg
- Williams M
- Willis Jg
- Willits Vl
- Winkelmann B
- Witt N
- Wittmann I
- Woehrle J
- Worner Diz F
- Wozniak I
- Wright R. S.
- Wronska D
- Wuerzner G
- Wychota K
- Xu P
- Xue L
- Yakusevich Vv
- Yang P
- Yang X
- Yao Lc
- Yared Z
- Yarows Sa
- Yigit Z
- Yoon J
- Yunis C.
- Zadra R
- Zaidman Cj
- Zamorano Gomez Jl
- Zannad F
- Zarandon Rb
- Zarich Sw
- Zateyshchikov D
- Zavaro Sh
- Zebrack Js
- Zeig S
- Zemek S
- Zemour G
- Zeng X
- Zeno Ml
- Zhang L
- Zhang X
- Zhang Y
- Zhao Y
- Zhou C
- Zhou Y
- Zhu Y
- Zidkova E
- Zieba B
- Zilahi Z
- Zoet-Nugteren Sk
- Zrazhevskiy K
- Zubek V
- Publication venue
- 'Massachusetts Medical Society'
- Publication date
- 01/01/2017
- Field of study
Bococizumab is a humanized monoclonal antibody that inhibits proprotein convertase subtilisin- kexin type 9 (PCSK9) and reduces levels of low-density lipoprotein (LDL) cholesterol. We sought to evaluate the efficacy of bococizumab in patients at high cardiovascular risk. METHODS In two parallel, multinational trials with different entry criteria for LDL cholesterol levels, we randomly assigned the 27,438 patients in the combined trials to receive bococizumab (at a dose of 150 mg) subcutaneously every 2 weeks or placebo. The primary end point was nonfatal myocardial infarction, nonfatal stroke, hospitalization for unstable angina requiring urgent revascularization, or cardiovascular death; 93% of the patients were receiving statin therapy at baseline. The trials were stopped early after the sponsor elected to discontinue the development of bococizumab owing in part to the development of high rates of antidrug antibodies, as seen in data from other studies in the program. The median follow-up was 10 months. RESULTS At 14 weeks, patients in the combined trials had a mean change from baseline in LDL cholesterol levels of -56.0% in the bococizumab group and +2.9% in the placebo group, for a between-group difference of -59.0 percentage points (P<0.001) and a median reduction from baseline of 64.2% (P<0.001). In the lower-risk, shorter-duration trial (in which the patients had a baseline LDL cholesterol level of ≥70 mg per deciliter [1.8 mmol per liter] and the median follow-up was 7 months), major cardiovascular events occurred in 173 patients each in the bococizumab group and the placebo group (hazard ratio, 0.99; 95% confidence interval [CI], 0.80 to 1.22; P = 0.94). In the higher-risk, longer-duration trial (in which the patients had a baseline LDL cholesterol level of ≥100 mg per deciliter [2.6 mmol per liter] and the median follow-up was 12 months), major cardiovascular events occurred in 179 and 224 patients, respectively (hazard ratio, 0.79; 95% CI, 0.65 to 0.97; P = 0.02). The hazard ratio for the primary end point in the combined trials was 0.88 (95% CI, 0.76 to 1.02; P = 0.08). Injection-site reactions were more common in the bococizumab group than in the placebo group (10.4% vs. 1.3%, P<0.001). CONCLUSIONS In two randomized trials comparing the PCSK9 inhibitor bococizumab with placebo, bococizumab had no benefit with respect to major adverse cardiovascular events in the trial involving lower-risk patients but did have a significant benefit in the trial involving higher-risk patients
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