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Biochemistry
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May 6, 1975
Subunit location of sulfhydryl groups of myosin labeled with a purine disulfide analog of adenosine triphosphate
P D Wagner, R G Yount
Biochemistry
|
November 18, 1975
The covalent modification of myosin's proteolytic fragments by a purine disulfide analog of adenosine triphosphate. Reaction at a binding site other than the active site
P D Wagner, R G Yount
Proceedings of the National Academy of Sciences of the United States of America
|
January 1, 1993
Photolabeling evidence for calcium-induced conformational changes at the ATP binding site of scallop myosin
B A Kerwin, R G Yount
Methods in Enzymology
|
January 1, 1982
Chemical modification of myosin by active-site trapping of metal-nucleotides with thiol crosslinking reagents
J A Wells, R G Yount
Annual Review of Physiology
|
January 1, 1996
The active site of myosin
I Rayment, C Smith, R G Yount
Biochemistry
|
June 22, 1971
Interaction of P--N--P and P--C--P analogs of adenosine triphosphate with heavy meromyosin, myosin, and actomyosin
R G Yount, D Ojala, D Babcock
Biophysical Journal
|
April 1, 1995
Is myosin a "back door" enzyme?
R G Yount, D Lawson, I Rayment
Biochemistry
|
May 2, 1989
Serine-324 of myosin's heavy chain is photoaffinity-labeled by 3'(2')-O-(4-benzoylbenzoyl)adenosine triphosphate
R Mahmood, M Elzinga, R G Yount
The Journal of Biological Chemistry
|
February 25, 1980
Magnesium nucleotide is stoichiometrically trapped at the active site of myosin and its active proteolytic fragments by thiol cross-linking reagents
J A Wells, M Sheldon, R G Yount
Biochemistry
|
September 27, 1983
Förster energy transfer measurements of thiol 1 to thiol 2 distances in myosin subfragment 1
R E Dalbey, J Weiel, R G Yount
Page
of 7
Search research articles
Search
Showing results (21-30 of 62) with videos related to
Sort By:
Page
of 7
Biochemistry
|
May 6, 1975
Subunit location of sulfhydryl groups of myosin labeled with a purine disulfide analog of adenosine triphosphate
P D Wagner, R G Yount
Biochemistry
|
November 18, 1975
The covalent modification of myosin's proteolytic fragments by a purine disulfide analog of adenosine triphosphate. Reaction at a binding site other than the active site
P D Wagner, R G Yount
Proceedings of the National Academy of Sciences of the United States of America
|
January 1, 1993
Photolabeling evidence for calcium-induced conformational changes at the ATP binding site of scallop myosin
B A Kerwin, R G Yount
Methods in Enzymology
|
January 1, 1982
Chemical modification of myosin by active-site trapping of metal-nucleotides with thiol crosslinking reagents
J A Wells, R G Yount
Annual Review of Physiology
|
January 1, 1996
The active site of myosin
I Rayment, C Smith, R G Yount
Biochemistry
|
June 22, 1971
Interaction of P--N--P and P--C--P analogs of adenosine triphosphate with heavy meromyosin, myosin, and actomyosin
R G Yount, D Ojala, D Babcock
Biophysical Journal
|
April 1, 1995
Is myosin a "back door" enzyme?
R G Yount, D Lawson, I Rayment
Biochemistry
|
May 2, 1989
Serine-324 of myosin's heavy chain is photoaffinity-labeled by 3'(2')-O-(4-benzoylbenzoyl)adenosine triphosphate
R Mahmood, M Elzinga, R G Yount
The Journal of Biological Chemistry
|
February 25, 1980
Magnesium nucleotide is stoichiometrically trapped at the active site of myosin and its active proteolytic fragments by thiol cross-linking reagents
J A Wells, M Sheldon, R G Yount
Biochemistry
|
September 27, 1983
Förster energy transfer measurements of thiol 1 to thiol 2 distances in myosin subfragment 1
R E Dalbey, J Weiel, R G Yount
Page
of 7