Kalmodulin (Malay Wikipedia)

Analysis of information sources in references of the Wikipedia article "Kalmodulin" in Malay language version.

Last modified: 10:03:44, 14 March 2024 (UTC)

Ref.Un. Ref.Website

Global rank Malay rank

6547nih.gov

5^th place

3^rd place

5034doi.org

2^nd place

65adsabs.harvard.edu

14^th place

23^rd place

22worldcat.org

4^th place

8^th place

21uniprot.org

2,402^nd place

3,355^th place

21utoronto.ca

1,483^rd place

1,629^th place

21ebi.ac.uk

4,422^nd place

3,346^th place

21jbc.org

6,339^th place

2,603^rd place

11aspetjournals.org

8,671^st place

9,530^th place

11vanderbilt.edu

3,827^th place

2,852^nd place

adsabs.harvard.edu (Global: 14^th place; Malay: 23^rd place)

ui.adsabs.harvard.edu

"Conformational entropy in molecular recognition by proteins". Nature. 448 (7151): 325–9. July 2007. Bibcode:2007Natur.448..325F. doi:10.1038/nature05959. PMC 4156320. PMID 17637663.
"Protein recognition and selection through conformational and mutually induced fit". Proceedings of the National Academy of Sciences of the United States of America. 110 (51): 20545–50. December 2013. Bibcode:2013PNAS..11020545W. doi:10.1073/pnas.1312788110. PMC 3870683. PMID 24297894. Unknown parameter |displayauthors= ignored (bantuan)
"An allosteric model of calmodulin explains differential activation of PP2B and CaMKII". Proceedings of the National Academy of Sciences of the United States of America. 105 (31): 10768–73. August 2008. Bibcode:2008PNAS..10510768S. doi:10.1073/pnas.0804672105. PMC 2504824. PMID 18669651.
"Coordination to lanthanide ions distorts binding site conformation in calmodulin". Proceedings of the National Academy of Sciences of the United States of America. 115 (14): E3126–E3134. April 2018. Bibcode:2018PNAS..115E3126E. doi:10.1073/pnas.1722042115. PMC 5889669. PMID 29545272.
"Calcium/calmodulin-dependent kinase II and long-term potentiation enhance synaptic transmission by the same mechanism". Proceedings of the National Academy of Sciences of the United States of America. 92 (24): 11175–9. November 1995. Bibcode:1995PNAS...9211175L. doi:10.1073/pnas.92.24.11175. PMC 40594. PMID 7479960.

aspetjournals.org (Global: 8,671^st place; Malay: 9,530^th place)

molpharm.aspetjournals.org

"Activation of calmodulin by various metal cations as a function of ionic radius". Molecular Pharmacology. 26 (1): 75–82. July 1984. PMID 6087119.

doi.org (Global: 2^nd place; Malay: 2^nd place)

"Calmodulin: an introduction". Canadian Journal of Biochemistry and Cell Biology. 61 (8): 906–10. August 1983. doi:10.1139/o83-115. PMID 6313166.
"Calmodulin: a prototypical calcium sensor". Trends in Cell Biology. 10 (8): 322–8. August 2000. doi:10.1016/S0962-8924(00)01800-6. PMID 10884684.
"Structures and metal-ion-binding properties of the Ca2+-binding helix-loop-helix EF-hand motifs". The Biochemical Journal. 405 (2): 199–221. July 2007. doi:10.1042/BJ20070255. PMID 17590154.
"Calmodulin: a prototypical calcium sensor". Trends in Cell Biology. 10 (8): 322–8. August 2000. doi:10.1016/s0962-8924(00)01800-6. PMID 10884684.
"Solution structure of calcium-free calmodulin". Nature Structural Biology. 2 (9): 768–76. September 1995. doi:10.1038/nsb0995-768. PMID 7552748.
"Calcium-induced conformational transition revealed by the solution structure of apo calmodulin". Nature Structural Biology. 2 (9): 758–67. September 1995. doi:10.1038/nsb0995-758. PMID 7552747.
"Solution structure of Ca(2+)-calmodulin reveals flexible hand-like properties of its domains". Nature Structural Biology. 8 (11): 990–7. November 2001. doi:10.1038/nsb1101-990. PMID 11685248.
"Obtaining site-specific calcium-binding affinities of calmodulin". Protein and Peptide Letters. 10 (4): 331–45. August 2003. doi:10.2174/0929866033478852. PMID 14529487.
"Calcium binding to calmodulin and its globular domains". The Journal of Biological Chemistry. 266 (13): 8050–4. May 1991. doi:10.1016/S0021-9258(18)92938-8. PMID 1902469.
"Structures of four Ca2+-bound troponin C at 2.0 A resolution: further insights into the Ca2+-switch in the calmodulin superfamily". Structure. 5 (12): 1695–711. December 1997. doi:10.1016/s0969-2126(97)00315-8. PMID 9438870.
"Calmodulin's flexibility allows for promiscuity in its interactions with target proteins and peptides". Molecular Biotechnology. 27 (1): 33–57. May 2004. doi:10.1385/MB:27:1:33. PMID 15122046.
"Structural diversity of calmodulin binding to its target sites". The FEBS Journal. 280 (21): 5551–65. November 2013. doi:10.1111/febs.12296. PMID 23601118.
"Conformational entropy in molecular recognition by proteins". Nature. 448 (7151): 325–9. July 2007. Bibcode:2007Natur.448..325F. doi:10.1038/nature05959. PMC 4156320. PMID 17637663.
"A coupled equilibrium shift mechanism in calmodulin-mediated signal transduction". Structure. 16 (5): 736–46. May 2008. doi:10.1016/j.str.2008.02.017. PMC 2428103. PMID 18462678.
"Protein-peptide interaction studies demonstrate the versatility of calmodulin target protein binding". Protein and Peptide Letters. 13 (5): 455–65. 2006. doi:10.2174/092986606776819600. PMID 16800798.
"Protein recognition and selection through conformational and mutually induced fit". Proceedings of the National Academy of Sciences of the United States of America. 110 (51): 20545–50. December 2013. Bibcode:2013PNAS..11020545W. doi:10.1073/pnas.1312788110. PMC 3870683. PMID 24297894. Unknown parameter |displayauthors= ignored (bantuan)
"Effects of myosin light chain kinase and peptides on Ca2+ exchange with the N- and C-terminal Ca2+ binding sites of calmodulin". The Journal of Biological Chemistry. 271 (2): 761–7. January 1996. doi:10.1074/jbc.271.2.761. PMID 8557684.
"Target recognition by calmodulin: dissecting the kinetics and affinity of interaction using short peptide sequences". Protein Science. 5 (7): 1215–28. July 1996. doi:10.1002/pro.5560050701. PMC 2143466. PMID 8819155.
"The neuronal voltage-dependent sodium channel type II IQ motif lowers the calcium affinity of the C-domain of calmodulin". Biochemistry. 47 (1): 112–23. January 2008. doi:10.1021/bi7013129. PMID 18067319.
"An allosteric model of calmodulin explains differential activation of PP2B and CaMKII". Proceedings of the National Academy of Sciences of the United States of America. 105 (31): 10768–73. August 2008. Bibcode:2008PNAS..10510768S. doi:10.1073/pnas.0804672105. PMC 2504824. PMID 18669651.
"Structural basis for calmodulin as a dynamic calcium sensor". Structure. 20 (5): 911–23. May 2012. doi:10.1016/j.str.2012.03.019. PMC 3372094. PMID 22579256. Unknown parameter |displayauthors= ignored (bantuan)
"Insights into modulation of calcium signaling by magnesium in calmodulin, troponin C and related EF-hand proteins". Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1813 (5): 913–21. May 2011. doi:10.1016/j.bbamcr.2011.01.017. PMC 3078997. PMID 21262274.
"Terbium (III) emission as a probe of calcium(II) binding sites in proteins". Journal of the American Chemical Society. 98 (25): 8255–60. December 1976. doi:10.1021/ja00441a060. PMID 993525.
"Terbium as luminescent probe of calmodulin calcium-binding sites; domains I and II contain the high-affinity sites". FEBS Letters. 116 (2): 269–72. July 1980. doi:10.1016/0014-5793(80)80660-0. PMID 7409149.
"Coordination to lanthanide ions distorts binding site conformation in calmodulin". Proceedings of the National Academy of Sciences of the United States of America. 115 (14): E3126–E3134. April 2018. Bibcode:2018PNAS..115E3126E. doi:10.1073/pnas.1722042115. PMC 5889669. PMID 29545272.
"Lanthanide ion luminescence probes of the structure of biological macromolecules". Accounts of Chemical Research. 14 (12): 384–392. 1981-12-01. doi:10.1021/ar00072a004. ISSN 0001-4842.
"Characterization of lanthanide (III) ion binding to calmodulin using luminescence spectroscopy". Biochemistry. 24 (23): 6639–45. November 1985. doi:10.1021/bi00344a051. PMID 4084548.
"Ca(2+)-dependent phosphorylation of myosin light chain kinase decreases the Ca2+ sensitivity of light chain phosphorylation within smooth muscle cells". The Journal of Biological Chemistry. 269 (13): 9912–20. April 1994. doi:10.1016/S0021-9258(17)36969-7. PMID 8144585.
"Calmodulin and the regulation of smooth muscle contraction". Molecular and Cellular Biochemistry. 135 (1): 21–41. June 1994. doi:10.1007/bf00925958. PMID 7816054.
"Regulation of calcium channels in smooth muscle: new insights into the role of myosin light chain kinase". Channels. 8 (5): 402–13. 2014-10-31. doi:10.4161/19336950.2014.950537. PMC 4594426. PMID 25483583.
"Calcium/calmodulin-mediated action of calcitonin on lipid metabolism in rats". The Journal of Clinical Investigation. 82 (4): 1165–72. October 1988. doi:10.1172/jci113713. PMC 442666. PMID 2844851. Unknown parameter |displayauthors= ignored (bantuan)
"Calcium/calmodulin-dependent kinase II and long-term potentiation enhance synaptic transmission by the same mechanism". Proceedings of the National Academy of Sciences of the United States of America. 92 (24): 11175–9. November 1995. Bibcode:1995PNAS...9211175L. doi:10.1073/pnas.92.24.11175. PMC 40594. PMID 7479960.
"Plant calmodulins and calmodulin-related proteins: multifaceted relays to decode calcium signals". Plant Signaling & Behavior. 1 (3): 96–104. May 2006. doi:10.4161/psb.1.3.2998. PMC 2635005. PMID 19521489.
Virdi, Amardeep S.; Singh, Supreet; Singh, Prabhjeet (2015). "Abiotic stress responses in plants: roles of calmodulin-regulated proteins". Frontiers in Plant Science. 6: 809. doi:10.3389/fpls.2015.00809. ISSN 1664-462X. PMC 4604306. PMID 26528296.

ebi.ac.uk (Global: 4,422^nd place; Malay: 3,346^th place)

"Calmodulin". InterPro Protein Archive. Dicapai pada 23 February 2016.

jbc.org (Global: 6,339^th place; Malay: 2,603^rd place)

"Ca(2+)-dependent phosphorylation of myosin light chain kinase decreases the Ca2+ sensitivity of light chain phosphorylation within smooth muscle cells". The Journal of Biological Chemistry. 269 (13): 9912–20. April 1994. doi:10.1016/S0021-9258(17)36969-7. PMID 8144585.

nih.gov (Global: 5^th place; Malay: 3^rd place)

pubmed.ncbi.nlm.nih.gov

"Calmodulin: an introduction". Canadian Journal of Biochemistry and Cell Biology. 61 (8): 906–10. August 1983. doi:10.1139/o83-115. PMID 6313166.
"Calmodulin: a prototypical calcium sensor". Trends in Cell Biology. 10 (8): 322–8. August 2000. doi:10.1016/S0962-8924(00)01800-6. PMID 10884684.
"Structures and metal-ion-binding properties of the Ca2+-binding helix-loop-helix EF-hand motifs". The Biochemical Journal. 405 (2): 199–221. July 2007. doi:10.1042/BJ20070255. PMID 17590154.
"Calmodulin: a prototypical calcium sensor". Trends in Cell Biology. 10 (8): 322–8. August 2000. doi:10.1016/s0962-8924(00)01800-6. PMID 10884684.
"Solution structure of calcium-free calmodulin". Nature Structural Biology. 2 (9): 768–76. September 1995. doi:10.1038/nsb0995-768. PMID 7552748.
"Calcium-induced conformational transition revealed by the solution structure of apo calmodulin". Nature Structural Biology. 2 (9): 758–67. September 1995. doi:10.1038/nsb0995-758. PMID 7552747.
"Solution structure of Ca(2+)-calmodulin reveals flexible hand-like properties of its domains". Nature Structural Biology. 8 (11): 990–7. November 2001. doi:10.1038/nsb1101-990. PMID 11685248.
"Obtaining site-specific calcium-binding affinities of calmodulin". Protein and Peptide Letters. 10 (4): 331–45. August 2003. doi:10.2174/0929866033478852. PMID 14529487.
"Calcium binding to calmodulin and its globular domains". The Journal of Biological Chemistry. 266 (13): 8050–4. May 1991. doi:10.1016/S0021-9258(18)92938-8. PMID 1902469.
"Structures of four Ca2+-bound troponin C at 2.0 A resolution: further insights into the Ca2+-switch in the calmodulin superfamily". Structure. 5 (12): 1695–711. December 1997. doi:10.1016/s0969-2126(97)00315-8. PMID 9438870.
"Calmodulin's flexibility allows for promiscuity in its interactions with target proteins and peptides". Molecular Biotechnology. 27 (1): 33–57. May 2004. doi:10.1385/MB:27:1:33. PMID 15122046.
"Structural diversity of calmodulin binding to its target sites". The FEBS Journal. 280 (21): 5551–65. November 2013. doi:10.1111/febs.12296. PMID 23601118.
"Conformational entropy in molecular recognition by proteins". Nature. 448 (7151): 325–9. July 2007. Bibcode:2007Natur.448..325F. doi:10.1038/nature05959. PMC 4156320. PMID 17637663.
"A coupled equilibrium shift mechanism in calmodulin-mediated signal transduction". Structure. 16 (5): 736–46. May 2008. doi:10.1016/j.str.2008.02.017. PMC 2428103. PMID 18462678.
"Protein-peptide interaction studies demonstrate the versatility of calmodulin target protein binding". Protein and Peptide Letters. 13 (5): 455–65. 2006. doi:10.2174/092986606776819600. PMID 16800798.
"Protein recognition and selection through conformational and mutually induced fit". Proceedings of the National Academy of Sciences of the United States of America. 110 (51): 20545–50. December 2013. Bibcode:2013PNAS..11020545W. doi:10.1073/pnas.1312788110. PMC 3870683. PMID 24297894. Unknown parameter |displayauthors= ignored (bantuan)
"Effects of myosin light chain kinase and peptides on Ca2+ exchange with the N- and C-terminal Ca2+ binding sites of calmodulin". The Journal of Biological Chemistry. 271 (2): 761–7. January 1996. doi:10.1074/jbc.271.2.761. PMID 8557684.
"Target recognition by calmodulin: dissecting the kinetics and affinity of interaction using short peptide sequences". Protein Science. 5 (7): 1215–28. July 1996. doi:10.1002/pro.5560050701. PMC 2143466. PMID 8819155.
"The neuronal voltage-dependent sodium channel type II IQ motif lowers the calcium affinity of the C-domain of calmodulin". Biochemistry. 47 (1): 112–23. January 2008. doi:10.1021/bi7013129. PMID 18067319.
"An allosteric model of calmodulin explains differential activation of PP2B and CaMKII". Proceedings of the National Academy of Sciences of the United States of America. 105 (31): 10768–73. August 2008. Bibcode:2008PNAS..10510768S. doi:10.1073/pnas.0804672105. PMC 2504824. PMID 18669651.
"Structural basis for calmodulin as a dynamic calcium sensor". Structure. 20 (5): 911–23. May 2012. doi:10.1016/j.str.2012.03.019. PMC 3372094. PMID 22579256. Unknown parameter |displayauthors= ignored (bantuan)
"Insights into modulation of calcium signaling by magnesium in calmodulin, troponin C and related EF-hand proteins". Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1813 (5): 913–21. May 2011. doi:10.1016/j.bbamcr.2011.01.017. PMC 3078997. PMID 21262274.
"Terbium (III) emission as a probe of calcium(II) binding sites in proteins". Journal of the American Chemical Society. 98 (25): 8255–60. December 1976. doi:10.1021/ja00441a060. PMID 993525.
"Terbium as luminescent probe of calmodulin calcium-binding sites; domains I and II contain the high-affinity sites". FEBS Letters. 116 (2): 269–72. July 1980. doi:10.1016/0014-5793(80)80660-0. PMID 7409149.
"Coordination to lanthanide ions distorts binding site conformation in calmodulin". Proceedings of the National Academy of Sciences of the United States of America. 115 (14): E3126–E3134. April 2018. Bibcode:2018PNAS..115E3126E. doi:10.1073/pnas.1722042115. PMC 5889669. PMID 29545272.
"Activation of calmodulin by various metal cations as a function of ionic radius". Molecular Pharmacology. 26 (1): 75–82. July 1984. PMID 6087119.
"Characterization of lanthanide (III) ion binding to calmodulin using luminescence spectroscopy". Biochemistry. 24 (23): 6639–45. November 1985. doi:10.1021/bi00344a051. PMID 4084548.
"Ca(2+)-dependent phosphorylation of myosin light chain kinase decreases the Ca2+ sensitivity of light chain phosphorylation within smooth muscle cells". The Journal of Biological Chemistry. 269 (13): 9912–20. April 1994. doi:10.1016/S0021-9258(17)36969-7. PMID 8144585.
"Calmodulin and the regulation of smooth muscle contraction". Molecular and Cellular Biochemistry. 135 (1): 21–41. June 1994. doi:10.1007/bf00925958. PMID 7816054.
"Regulation of calcium channels in smooth muscle: new insights into the role of myosin light chain kinase". Channels. 8 (5): 402–13. 2014-10-31. doi:10.4161/19336950.2014.950537. PMC 4594426. PMID 25483583.
"Calcium/calmodulin-mediated action of calcitonin on lipid metabolism in rats". The Journal of Clinical Investigation. 82 (4): 1165–72. October 1988. doi:10.1172/jci113713. PMC 442666. PMID 2844851. Unknown parameter |displayauthors= ignored (bantuan)
"Calcium/calmodulin-dependent kinase II and long-term potentiation enhance synaptic transmission by the same mechanism". Proceedings of the National Academy of Sciences of the United States of America. 92 (24): 11175–9. November 1995. Bibcode:1995PNAS...9211175L. doi:10.1073/pnas.92.24.11175. PMC 40594. PMID 7479960.
"Plant calmodulins and calmodulin-related proteins: multifaceted relays to decode calcium signals". Plant Signaling & Behavior. 1 (3): 96–104. May 2006. doi:10.4161/psb.1.3.2998. PMC 2635005. PMID 19521489.
Virdi, Amardeep S.; Singh, Supreet; Singh, Prabhjeet (2015). "Abiotic stress responses in plants: roles of calmodulin-regulated proteins". Frontiers in Plant Science. 6: 809. doi:10.3389/fpls.2015.00809. ISSN 1664-462X. PMC 4604306. PMID 26528296.

ncbi.nlm.nih.gov

"Conformational entropy in molecular recognition by proteins". Nature. 448 (7151): 325–9. July 2007. Bibcode:2007Natur.448..325F. doi:10.1038/nature05959. PMC 4156320. PMID 17637663.
"A coupled equilibrium shift mechanism in calmodulin-mediated signal transduction". Structure. 16 (5): 736–46. May 2008. doi:10.1016/j.str.2008.02.017. PMC 2428103. PMID 18462678.
"Protein recognition and selection through conformational and mutually induced fit". Proceedings of the National Academy of Sciences of the United States of America. 110 (51): 20545–50. December 2013. Bibcode:2013PNAS..11020545W. doi:10.1073/pnas.1312788110. PMC 3870683. PMID 24297894. Unknown parameter |displayauthors= ignored (bantuan)
"Target recognition by calmodulin: dissecting the kinetics and affinity of interaction using short peptide sequences". Protein Science. 5 (7): 1215–28. July 1996. doi:10.1002/pro.5560050701. PMC 2143466. PMID 8819155.
"An allosteric model of calmodulin explains differential activation of PP2B and CaMKII". Proceedings of the National Academy of Sciences of the United States of America. 105 (31): 10768–73. August 2008. Bibcode:2008PNAS..10510768S. doi:10.1073/pnas.0804672105. PMC 2504824. PMID 18669651.
"Structural basis for calmodulin as a dynamic calcium sensor". Structure. 20 (5): 911–23. May 2012. doi:10.1016/j.str.2012.03.019. PMC 3372094. PMID 22579256. Unknown parameter |displayauthors= ignored (bantuan)
"Insights into modulation of calcium signaling by magnesium in calmodulin, troponin C and related EF-hand proteins". Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1813 (5): 913–21. May 2011. doi:10.1016/j.bbamcr.2011.01.017. PMC 3078997. PMID 21262274.
"Coordination to lanthanide ions distorts binding site conformation in calmodulin". Proceedings of the National Academy of Sciences of the United States of America. 115 (14): E3126–E3134. April 2018. Bibcode:2018PNAS..115E3126E. doi:10.1073/pnas.1722042115. PMC 5889669. PMID 29545272.
"Regulation of calcium channels in smooth muscle: new insights into the role of myosin light chain kinase". Channels. 8 (5): 402–13. 2014-10-31. doi:10.4161/19336950.2014.950537. PMC 4594426. PMID 25483583.
"Calcium/calmodulin-mediated action of calcitonin on lipid metabolism in rats". The Journal of Clinical Investigation. 82 (4): 1165–72. October 1988. doi:10.1172/jci113713. PMC 442666. PMID 2844851. Unknown parameter |displayauthors= ignored (bantuan)
"Calcium/calmodulin-dependent kinase II and long-term potentiation enhance synaptic transmission by the same mechanism". Proceedings of the National Academy of Sciences of the United States of America. 92 (24): 11175–9. November 1995. Bibcode:1995PNAS...9211175L. doi:10.1073/pnas.92.24.11175. PMC 40594. PMID 7479960.
"Plant calmodulins and calmodulin-related proteins: multifaceted relays to decode calcium signals". Plant Signaling & Behavior. 1 (3): 96–104. May 2006. doi:10.4161/psb.1.3.2998. PMC 2635005. PMID 19521489.
Virdi, Amardeep S.; Singh, Supreet; Singh, Prabhjeet (2015). "Abiotic stress responses in plants: roles of calmodulin-regulated proteins". Frontiers in Plant Science. 6: 809. doi:10.3389/fpls.2015.00809. ISSN 1664-462X. PMC 4604306. PMID 26528296.

uniprot.org (Global: 2,402^nd place; Malay: 3,355^th place)

"CALM1 – Calmodulin – Homo sapiens (Human) – CALM1 gene & protein". www.uniprot.org. Dicapai pada 2016-02-23.

utoronto.ca (Global: 1,483^rd place; Malay: 1,629^th place)

calcium.uhnres.utoronto.ca

"Calmodulin Target Database". Dicapai pada 27 July 2020.

vanderbilt.edu (Global: 3,827^th place; Malay: 2,852^nd place)

structbio.vanderbilt.edu

"Home Page for Calmodulin". structbio.vanderbilt.edu. Dicapai pada 2016-02-23.

worldcat.org (Global: 4^th place; Malay: 8^th place)

"Lanthanide ion luminescence probes of the structure of biological macromolecules". Accounts of Chemical Research. 14 (12): 384–392. 1981-12-01. doi:10.1021/ar00072a004. ISSN 0001-4842.
Virdi, Amardeep S.; Singh, Supreet; Singh, Prabhjeet (2015). "Abiotic stress responses in plants: roles of calmodulin-regulated proteins". Frontiers in Plant Science. 6: 809. doi:10.3389/fpls.2015.00809. ISSN 1664-462X. PMC 4604306. PMID 26528296.

Kalmodulin (Malay Wikipedia)

adsabs.harvard.edu (Global: 14th place; Malay: 23rd place)

ui.adsabs.harvard.edu

aspetjournals.org (Global: 8,671st place; Malay: 9,530th place)

molpharm.aspetjournals.org

doi.org (Global: 2nd place; Malay: 2nd place)

ebi.ac.uk (Global: 4,422nd place; Malay: 3,346th place)

jbc.org (Global: 6,339th place; Malay: 2,603rd place)

nih.gov (Global: 5th place; Malay: 3rd place)