Localization of the reactive trinitrophenylated lysyl residue of myosin ATPase site in the NH2-terminal (27 k domain) of S1 heavy chain

scientific article published on 01 August 1980

Localization of the reactive trinitrophenylated lysyl residue of myosin ATPase site in the NH2-terminal (27 k domain) of S1 heavy chain is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1016/0014-5793(80)80941-0
P698PubMed publication ID6447623

P2093author name stringBertrand R
Mornet D
Audemard E
Kassab R
Pantel P
P2860cites workA new protein of the thick filaments of vertebrate skeletal myofibrils. Extractions, purification and characterizationQ28238463
Preparation and properties of 2'(or 3')-O-(2,4,6-trinitrophenyl) adenosine 5'-triphosphate, an analog of adenosine triphosphate.Q34205219
Involvement of an Arginyl Residue in the Catalytic Activity of Myosin HeadsQ39287104
Separation of subfragment-1 isoenzymes from rabbit skeletal muscle myosinQ39741645
Myosin structure. Proximity measurements by fluorescence energy transferQ39751250
Studies on the amino groups of myosin ATPase IV. Effect of ATP and its analogs on the spectral properties of trinitrophenylated myosin and its active fragmentsQ39820735
Photoaffinity labelling with an ATP analog of the N-terminal peptide of myosinQ39886937
The limited tryptic cleavage of chymotryptic S-1 : An approach to the characterization of the actin site in myosin headsQ39895347
Effect of trinitrophenylation on myosin ATPaseQ44418871
On the active site of myosin A-adenosine triphosphatase. VI. Existence of asparaginyl-prolyl-prolyl-lysine near the active siteQ68399698
ON THE ACTIVE SITE OF MYOSIN A-ADENOSINE TRIPHOSPHATASE. V. PARTIAL SOLUTION OF THE CHEMICAL STRUCTURE AROUND THE BINDING SITE OF TRINITROBENZENESULFONATEQ78563533
P433issue1
P407language of work or nameEnglishQ1860
P1104number of pages6
P304page(s)183-188
P577publication date1980-08-01
P1433published inFEBS LettersQ1388051
P1476titleLocalization of the reactive trinitrophenylated lysyl residue of myosin ATPase site in the NH2-terminal (27 k domain) of S1 heavy chain
P478volume117

Reverse relations

cites work (P2860)
Q72758006Cardiac myosin subfragment 1 modification by carbodiimide in the presence of a nucleophile
Q34180415Chemical decoupling of ATPase activation and force production from the contractile cycle in myosin by steric hindrance of lever-arm movement
Q53853480Cosolvent-Induced Aggregation Inhibits Myosin ATPase Activity by Stabilizing the Predominant Transition Intermediate
Q35185384Definite differences between in vitro actin-myosin sliding and muscle contraction as revealed using antibodies to myosin head
Q71712108Differential scanning calorimetric study of the complexes of modified myosin subfragment 1 with ADP and vanadate or beryllium fluoride
Q28344538Effect of ionic strength on the conformation of myosin subfragment 1-nucleotide complexes
Q36206008Electron microscopic recording of myosin head power stroke in hydrated myosin filaments
Q39487371Pathway for the communication between the ATPase and actin sites in myosin
Q70274917Selective cleavage of the connector segments within the myosin‐S1 heavy chain by staphylococcal protease
Q70269117Structural and actin‐binding properties of the trypsin‐produced HMM and S1 from gizzard smooth muscle myosin
Q40218299Structural aspects of actomyosin interaction
Q69837188The effect of pyrophosphate on the reaction of myosin with 2,4,6-trinitrobenzene sulphonate
Q72585881The interaction of skeletal myosin subfragment 1 with the polyanion, heparin
Q39752036The role of tropomyosin-troponin in the regulation of skeletal muscle contraction

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