PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA Journal
Overview
publication venue for
- Cardiac troponin T N-domain variant destabilizes the actin interface resulting in disturbed myofilament function. 120. 2023
- The structure of the native cardiac thin filament at systolic Ca2+ levels. 118. 2021
- NF-kappa B-induced R-loop accumulation and DNA damage select for nucleotide excision repair deficiencies in adult T cell leukemia. 118. 2021
- Facebook language predicts depression in medical records.. 115:11203-11208. 2018
- Ca2+-induced movement of tropomyosin on native cardiac thin filaments revealed by cryoelectron microscopy. 114:6782-6787. 2017
- Ca<sup>2+</sup>-induced movement of tropomyosin on native cardiac thin filaments revealed by cryoelectron microscopy.. 114:6782-6787. 2017
- C0 and C1 N-terminal Ig domains of myosin binding protein C exert different effects on thin filament activation. 113:1558-1563. 2016
- C0 and C1 N-terminal Ig domains of myosin binding protein C exert different effects on thin filament activation.. 113:1558-63. 2016
- Regulation of actin-myosin interaction by conserved periodic sites of tropomyosin. 109:18425-18430. 2012
- BclAF1 restriction factor is neutralized by proteasomal degradation and microRNA repression during human cytomegalovirus infection. 109:9575-9580. 2012
- Remodeling of actin filaments by ADF/cofilin proteins. 108:20568-20572. 2011
- Influence of lever structure on myosin 5a walking. 107:2509-2514. 2010
- ParA2, a Vibrio cholerae chromosome partitioning protein, forms left-handed helical filaments on DNA. 107:4590-4595. 2010
- The SAH domain extends the functional length of the myosin lever. 106:22193-22198. 2009
- Cloning human herpes virus 6A genome into bacterial artificial chromosomes and study of DNA replication intermediates. 106:19138-19143. 2009
- Characterization of a pigment-dispersing hormone in eyestalks of the fiddler crab Uca pugilator. 82:5319-5322. 1985
- Docosahexaenoic acid ethyl esters ineffective? 2013
Identity
International Standard Serial Number (ISSN)
- 0027-8424
Electronic International Standard Serial Number (EISSN)
- 1091-6490