J
John H. Collins
Researcher at University of Maryland, Baltimore
Publications - 58
Citations - 1945
John H. Collins is an academic researcher from University of Maryland, Baltimore. The author has contributed to research in topics: Troponin C & Peptide sequence. The author has an hindex of 25, co-authored 58 publications receiving 1933 citations. Previous affiliations of John H. Collins include Clarkson University & University of Montpellier.
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Journal ArticleDOI
Molecular cloning and immunological characterization of the gamma polypeptide, a small protein associated with the Na,K-ATPase.
TL;DR: Results are consistent with the notion that the gamma subunit is specifically associated with and may be an important component of the Na,K-ATPase.
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Myosin light chains and troponin C: structural and evolutionary relationships revealed by amino acid sequence comparisons.
TL;DR: It is remarkable that the key regulatory proteins (TnC, ELC, RLC, calmodulin) in the various regulatory systems have all evolved from a common ancestor and possess common structural features, including similar Ca2+-binding sites.
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Tryptic and chymotryptic cleavage sites in sequence of α-subunit of (Na+ + K+)-ATPase from outer medulla of mammalian kidney
TL;DR: The NH2-terminal sequence in renal alpha-subunit is not conserved in alpha + from rat neurolemma or in alpha- Subunit from Torpedo or brine shrimp, and may be a unique feature of the alpha- subunit in (Na+ + K+)-ATPase from mammalian kidney.
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Sarcolipin, the "proteolipid" of skeletal muscle sarcoplasmic reticulum, is a unique, amphipathic, 31-residue peptide.
Alicja Wawrzynow,Janet L. Theibert,C. M. Murphy,Istvan Jona,Anthony Martonosi,John H. Collins +5 more
TL;DR: The name sarcolipin is proposed for this small protein, to signify its lipid-like solubility and association with the sarcoplasmic reticulum of rabbit skeletal muscle, and the molecular weight calculated from the sequence agrees with that measured by fast atom bombardment mass spectrometry, showing that sarcolippin contains no attached fatty acyl or other prosthetic groups.
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Characterization of zero-length cross-links between rabbit skeletal muscle troponin C and troponin I: evidence for direct interaction between the inhibitory region of troponin I and the NH2-terminal, regulatory domain of troponin C.
TL;DR: These results yield the first evidence for an interaction between the N-terminal domain of TnC and the inhibitory region of TNI.