Willingham T, Kim Y, Lindberg E, Bleck C, Glancy B
Nat Commun. 2020; 11(1):3722.
PMID: 32709902
PMC: 7381600.
DOI: 10.1038/s41467-020-17579-6.
Squire J
Glob Cardiol Sci Pract. 2017; 2016(2):e201611.
PMID: 29043260
PMC: 5642817.
DOI: 10.21542/gcsp.2016.11.
Szent-Gyorgyi A
J Gen Physiol. 2004; 123(6):631-41.
PMID: 15173217
PMC: 2234565.
DOI: 10.1085/jgp.200409091.
REYNOLDS S
Proc R Soc Med. 1951; 44(8):695-702.
PMID: 14864579
PMC: 2081855.
Needham D, Williams J
Biochem J. 1959; 73:171-81.
PMID: 14426314
PMC: 1197029.
DOI: 10.1042/bj0730171.
THE ACTION OF THIOL REAGENTS ON THE ADENOSINE-TRIPHOSPHATASE ACTIVITIES OF HEAVY MEROMYOSIN AND L-MYOSIN.
PERRY S, Cotterill J
Biochem J. 1965; 96:224-30.
PMID: 14343136
PMC: 1206926.
DOI: 10.1042/bj0960224.
STUDIES ON THE MICRO-INJECTION OF VARIOUS SUBSTANCES INTO CRAB MUSCLE FIBRES.
CALDWELL P, WALSTER G
J Physiol. 1963; 169:353-72.
PMID: 14079672
PMC: 1368758.
DOI: 10.1113/jphysiol.1963.sp007261.
Fine structural localization of adenosinetriphosphatase activity in heart muscle myofibrils.
Tice L, Barrnett R
J Cell Biol. 1962; 15:401-16.
PMID: 13981351
PMC: 2106161.
DOI: 10.1083/jcb.15.3.401.
The degradation of heavy meromyosin by trypsin.
Mueller H, PERRY S
Biochem J. 1962; 85:431-9.
PMID: 13936493
PMC: 1243761.
DOI: 10.1042/bj0850431.
The effect of actin on the magnesium-activated adenosine triphosphatase of heavy meromyosin.
LEADBEATER L, PERRY S
Biochem J. 1963; 87:233-9.
PMID: 13928816
PMC: 1201880.
DOI: 10.1042/bj0870233.
Influence of ionic strength and phosphate concentration on tension responses of glycerol-extracted muscle fibres.
Newbold R, Rose D
J Physiol. 1957; 135(1):30-44.
PMID: 13398962
PMC: 1358909.
DOI: 10.1113/jphysiol.1957.sp005691.
A study of the effects of substrate concentration and certain relaxing factors on the magnesium-activated myofibrillar adenosine triphosphatase.
Grey T, PERRY S
Biochem J. 1956; 64(1):184-92.
PMID: 13363825
PMC: 1199709.
DOI: 10.1042/bj0640184.
Studies on the structure of muscle. III. Phase contrast and electron microscopy of dipteran flight muscle.
Hodge A
J Biophys Biochem Cytol. 1955; 1(4):361-80.
PMID: 13242599
PMC: 2223819.
DOI: 10.1083/jcb.1.4.361.
Creatine phosphokinase and the enzymic and contractile properties of the isolated myofibril.
PERRY S
Biochem J. 1954; 57(3):427-34.
PMID: 13181853
PMC: 1269775.
DOI: 10.1042/bj0570427.
The relation of energy-rich phosphate in muscle to myoglobin and to cytochrome-oxidase activity.
Lawrie R
Biochem J. 1953; 55(2):305-9.
PMID: 13093682
PMC: 1269238.
DOI: 10.1042/bj0550305.
The protein components of the isolated myofibril.
PERRY S
Biochem J. 1953; 55(1):114-22.
PMID: 13093625
PMC: 1269143.
DOI: 10.1042/bj0550114.
Further observations on a factor (The `Marsh' factor) effecting relaxation of ATP-shortened muscle-fibre models and the effect of Ca and Mg ions upon it.
Bendall J
J Physiol. 1953; 121(2):232-54.
PMID: 13085333
PMC: 1366073.
DOI: 10.1113/jphysiol.1953.sp004944.
Respiratory granules of heart muscle.
CLELAND K, SLATER E
Biochem J. 1953; 53(4):547-56.
PMID: 13032108
PMC: 1198191.
DOI: 10.1042/bj0530547.
The bound nucleotide of the isolated myofibril.
PERRY S
Biochem J. 1952; 51(4):495-9.
PMID: 13018111
PMC: 1197879.
DOI: 10.1042/bj0510495.
Proteolytic enzyme preparation from Pseudomonas fragi: its action on pig muscle.
Tarrant P, Jenkins N, Pearson A, Dutson T
Appl Microbiol. 1973; 25(6):996-1005.
PMID: 4716726
PMC: 380953.
DOI: 10.1128/am.25.6.996-1005.1973.
