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Article ; Online: Clinical implications of estrone sulfate measurement in laboratory medicine.

Rezvanpour, Atoosa / Don-Wauchope, Andrew C

Critical reviews in clinical laboratory sciences

2017 Volume 54, Issue 2, Page(s) 73–86

Abstract: Estrone sulfate ( ... ...

Abstract	Estrone sulfate (E
Language	English
Publishing date	2017-03
Publishing country	England
Document type	Journal Article
ZDB-ID	280641-1
ISSN	1549-781X ; 1040-8363 ; 0590-8191
ISSN (online)	1549-781X
ISSN	1040-8363 ; 0590-8191
DOI	10.1080/10408363.2016.1252310
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Zs.A 771: Show issues

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Article: Unique S100 target protein interactions.

Rezvanpour, Atoosa / Shaw, Gary S

General physiology and biophysics

2009 Volume 28 Spec No Focus, Page(s) F39–46

Abstract: Three-dimensional structures of S100B, S100A1, S100A6 and S100A11 have shown that calcium binding to these proteins results in a conformational change allowing them to interact with many biological targets. The structures of some S100 proteins in the ... ...

Abstract	Three-dimensional structures of S100B, S100A1, S100A6 and S100A11 have shown that calcium binding to these proteins results in a conformational change allowing them to interact with many biological targets. The structures of some S100 proteins in the presence of peptide targets from Ndr kinase, p53, CapZ, annexins A1 and A2 and the Siah-1 Interacting Protein indicate there are at least three modes of recognition that utilize two distinct surfaces in the S100 proteins. These surfaces have been hypothesized to simultaneously accommodate multiple binding partners. This review focuses on potential multiprotein complexes involving calcium-insensitive S100A10, annexin A2 and several other proteins including AHNAK, dysferlin, NS3, TASK-1 and TRPV5/6.
MeSH term(s)	Animals ; Annexin A2/metabolism ; Calcium/chemistry ; Calcium/metabolism ; Cell Membrane/metabolism ; Humans ; Models, Biological ; Models, Molecular ; Molecular Conformation ; Multiprotein Complexes/chemistry ; Protein Binding ; Protein Conformation ; Protein Structure, Tertiary ; S100 Proteins/metabolism ; Signal Transduction
Chemical Substances	Annexin A2 ; Multiprotein Complexes ; S100 Proteins ; S100 calcium binding protein A10 ; Calcium (SY7Q814VUP)
Language	English
Publishing date	2009
Publishing country	Slovakia
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	791184-1
ISSN	0231-5882
ISSN	0231-5882
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Zs.A 1874: Show issues

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Article ; Online: Analytical factors to consider when assessing a high-sensitivity cardiac troponin I assay compared to a contemporary assay in clinical studies.

Rezvanpour, Atoosa / Shortt, Colleen / Clark, Lorna / Worster, Andrew / Kavsak, Peter A

Clinica chimica acta; international journal of clinical chemistry

2014 Volume 429, Page(s) 6–7

MeSH term(s)	Blood Chemical Analysis/methods ; Humans ; Myocardium/metabolism ; Temperature ; Troponin I/blood ; Troponin I/metabolism
Chemical Substances	Troponin I
Language	English
Publishing date	2014-02-15
Publishing country	Netherlands
Document type	Comparative Study ; Letter ; Research Support, Non-U.S. Gov't
ZDB-ID	80228-1
ISSN	1873-3492 ; 0009-8981
ISSN (online)	1873-3492
ISSN	0009-8981
DOI	10.1016/j.cca.2013.11.012
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Article ; Online: The S100A10-annexin A2 complex provides a novel asymmetric platform for membrane repair.

Rezvanpour, Atoosa / Santamaria-Kisiel, Liliana / Shaw, Gary S

The Journal of biological chemistry

2011 Volume 286, Issue 46, Page(s) 40174–40183

Abstract: Membrane repair is mediated by multiprotein complexes, such as that formed between the dimeric EF-hand protein S100A10, the calcium- and phospholipid-binding protein annexin A2, the enlargeosome protein AHNAK, and members of the transmembrane ferlin ... ...

Abstract	Membrane repair is mediated by multiprotein complexes, such as that formed between the dimeric EF-hand protein S100A10, the calcium- and phospholipid-binding protein annexin A2, the enlargeosome protein AHNAK, and members of the transmembrane ferlin family. Although interactions between these proteins have been shown, little is known about their structural arrangement and mechanisms of formation. In this work, we used a non-covalent complex between S100A10 and the N terminus of annexin A2 (residues 1-15) and a designed hybrid protein (A10A2), where S100A10 is linked in tandem to the N-terminal region of annexin A2, to explore the binding region, stoichiometry, and affinity with a synthetic peptide from the C terminus of AHNAK. Using multiple biophysical methods, we identified a novel asymmetric arrangement between a single AHNAK peptide and the A10A2 dimer. The AHNAK peptide was shown to require the annexin A2 N terminus, indicating that the AHNAK binding site comprises regions on both S100A10 and annexin proteins. NMR spectroscopy was used to show that the AHNAK binding surface comprised residues from helix IV in S100A10 and the C-terminal portion from the annexin A2 peptide. This novel surface maps to the exposed side of helices IV and IV' of the S100 dimeric structure, a region not identified in any previous S100 target protein structures. The results provide the first structural details of the ternary S100A10 protein complex required for membrane repair.
MeSH term(s)	Animals ; Annexin A2/chemistry ; Annexin A2/genetics ; Annexin A2/metabolism ; Cell Membrane/chemistry ; Cell Membrane/genetics ; Cell Membrane/metabolism ; Multiprotein Complexes/chemistry ; Multiprotein Complexes/genetics ; Multiprotein Complexes/metabolism ; Nuclear Magnetic Resonance, Biomolecular ; Peptides/chemistry ; Peptides/genetics ; Peptides/metabolism ; Protein Binding ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Rabbits ; S100 Proteins/chemistry ; S100 Proteins/genetics ; S100 Proteins/metabolism ; Structure-Activity Relationship
Chemical Substances	Annexin A2 ; Multiprotein Complexes ; Peptides ; S100 Proteins ; S100 calcium binding protein A10
Language	English
Publishing date	2011-09-26
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M111.244038
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Uc I Zs.108: Show issues

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Article ; Online: Design of high-affinity S100-target hybrid proteins.

Rezvanpour, Atoosa / Phillips, Jeremy M / Shaw, Gary S

Protein science : a publication of the Protein Society

2009 Volume 18, Issue 12, Page(s) 2528–2536

Abstract: S100B and S100A10 are dimeric, EF-hand proteins. S100B undergoes a calcium-dependent conformational change allowing it to interact with a short contiguous sequence from the actin-capping protein CapZ (TRTK12). S100A10 does not bind calcium but is able to ...

Abstract	S100B and S100A10 are dimeric, EF-hand proteins. S100B undergoes a calcium-dependent conformational change allowing it to interact with a short contiguous sequence from the actin-capping protein CapZ (TRTK12). S100A10 does not bind calcium but is able to recruit the N-terminus of annexin A2 important for membrane fusion events, and to form larger multiprotein complexes such as that with the cation channel proteins TRPV5/6. In this work, we have designed, expressed, purified, and characterized two S100-target peptide hybrid proteins comprised of S100A10 and S100B linked in tandem to annexin A2 (residues 1-15) and CapZ (TRTK12), respectively. Different protease cleavage sites (tobacco etch virus, PreScission) were incorporated into the linkers of the hybrid proteins. In situ proteolytic cleavage monitored by (1)H-(15)N HSQC spectra showed the linker did not perturb the structures of the S100A10-annexin A2 or S100B-TRTK12 complexes. Furthermore, the analysis of the chemical shift assignments ((1)H, (15)N, and (13)C) showed that residues T102-S108 of annexin A2 formed a well-defined alpha-helix in the S100A10 hybrid while the TRTK12 region was unstructured at the N-terminus with a single turn of alpha-helix from D108-K111 in the S100B hybrid protein. The two S100 hybrid proteins provide a simple yet extremely efficient method for obtaining high yields of intact S100 target peptides. Since cleavage of the S100 hybrid protein is not necessary for structural characterization, this approach may be useful as a scaffold for larger S100 complexes.
MeSH term(s)	Amino Acid Sequence ; Animals ; Annexin A2/chemistry ; Annexin A2/genetics ; Annexin A2/isolation & purification ; CapZ Actin Capping Protein/chemistry ; CapZ Actin Capping Protein/genetics ; CapZ Actin Capping Protein/isolation & purification ; EF Hand Motifs ; Escherichia coli/genetics ; Gene Expression ; Molecular Sequence Data ; Mutant Chimeric Proteins/chemistry ; Mutant Chimeric Proteins/genetics ; Mutant Chimeric Proteins/isolation & purification ; Nerve Growth Factors/chemistry ; Nerve Growth Factors/genetics ; Nerve Growth Factors/isolation & purification ; Nuclear Magnetic Resonance, Biomolecular ; Peptides/chemistry ; Peptides/genetics ; Protein Conformation ; Rabbits ; S100 Calcium Binding Protein beta Subunit ; S100 Proteins/chemistry ; S100 Proteins/genetics ; S100 Proteins/isolation & purification
Chemical Substances	Annexin A2 ; CapZ Actin Capping Protein ; Mutant Chimeric Proteins ; Nerve Growth Factors ; Peptides ; S100 Calcium Binding Protein beta Subunit ; S100 Proteins ; S100 calcium binding protein A10
Language	English
Publishing date	2009-10-13
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1106283-6
ISSN	1469-896X ; 0961-8368
ISSN (online)	1469-896X
ISSN	0961-8368
DOI	10.1002/pro.267
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Zs.A 3407: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
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Article ; Online: Temporal development of protein structure during S100A11 folding and dimerization probed by oxidative labeling and mass spectrometry.

Stocks, Bradley B / Rezvanpour, Atoosa / Shaw, Gary S / Konermann, Lars

Journal of molecular biology

2011 Volume 409, Issue 4, Page(s) 669–679

Abstract: Considerable progress in deciphering the mechanisms of protein folding has been made. However, most work in this area has focused on single-chain systems, whereas the majority of proteins are oligomers. The spontaneous assembly of intact multi-subunit ... ...

Abstract	Considerable progress in deciphering the mechanisms of protein folding has been made. However, most work in this area has focused on single-chain systems, whereas the majority of proteins are oligomers. The spontaneous assembly of intact multi-subunit systems from disordered building blocks encompasses the formation of intramolecular as well as intermolecular contacts. Both types of interaction affect the solvent accessibility of individual protein segments. This work employs pulsed hydroxyl radical (·OH) labeling for tracking time-dependent accessibility changes during folding and assembly of the S100A11 homodimer. ·OH induces covalent modifications at exposed residues. Structural snapshots are obtained by combining ·OH labeling with rapid mixing and mass spectrometry. The free subunits are found to possess a partially non-native hydrophobic core that prevents subunit association during the initial stages of the reaction. Instead, the protein forms an early (10 ms) monomeric intermediate that exhibits reduced solvent accessibility in regions distant from helices I and IV, which constitute the dimerization interface. Subunit association is complete after 800 ms, although the protein retains significant disorder in helices II and III at this point. Subsequent consolidation of these elements leads to the native state. The experimental strategy used here could become a general tool for deciphering kinetic mechanisms of biomolecular self-assembly processes.
MeSH term(s)	Amino Acid Sequence ; Animals ; Dimerization ; Mass Spectrometry/methods ; Models, Molecular ; Oxidation-Reduction ; Protein Conformation ; Protein Folding ; Rabbits ; S100 Proteins/chemistry ; S100 Proteins/genetics
Chemical Substances	S100 Proteins
Language	English
Publishing date	2011-06-17
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	80229-3
ISSN	1089-8638 ; 0022-2836
ISSN (online)	1089-8638
ISSN	0022-2836
DOI	10.1016/j.jmb.2011.04.028
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Zs.A 867: Show issues

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Article ; Online: S100-annexin complexes--structural insights.

Rintala-Dempsey, Anne C / Rezvanpour, Atoosa / Shaw, Gary S

The FEBS journal

2008 Volume 275, Issue 20, Page(s) 4956–4966

Abstract: Annexins and S100 proteins represent two large, but distinct, calcium-binding protein families. Annexins are made up of a highly alpha-helical core domain that binds calcium ions, allowing them to interact with phospholipid membranes. Furthermore, some ... ...

Abstract	Annexins and S100 proteins represent two large, but distinct, calcium-binding protein families. Annexins are made up of a highly alpha-helical core domain that binds calcium ions, allowing them to interact with phospholipid membranes. Furthermore, some annexins, such as annexins A1 and A2, contain an N-terminal region that is expelled from the core domain on calcium binding. These events allow for the interaction of the annexin N-terminus with target proteins, such as S100. In addition, when an S100 protein binds calcium ions, it undergoes a structural reorientation of its helices, exposing a hydrophobic patch capable of interacting with its targets, including the N-terminal sequences of annexins. Structural studies of the complexes between members of these two families have revealed valuable details regarding the mechanisms of the interactions, including the binding surfaces and conformation of the annexin N-terminus. However, other S100-annexin interactions, such as those between S100A11 and annexin A6, or between dicalcin and annexins A1, A2 and A5, appear to be more complicated, involving the annexin core region, perhaps in concert with the N-terminus. The diversity of these interactions indicates that multiple forms of recognition exist between S100 proteins and annexins. S100-annexin interactions have been suggested to play a role in membrane fusion events by the bridging together of two annexin proteins, bound to phospholipid membranes, by an S100 protein. The structures and differential interactions of S100-annexin complexes may indicate that this process has several possible modes of protein-protein recognition.
MeSH term(s)	Animals ; Annexins/chemistry ; Annexins/metabolism ; Humans ; Membrane Proteins/metabolism ; Multiprotein Complexes ; Protein Binding ; S100 Proteins/chemistry ; S100 Proteins/metabolism
Chemical Substances	Annexins ; Membrane Proteins ; Multiprotein Complexes ; S100 Proteins
Language	English
Publishing date	2008-10
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2173655-8
ISSN	1742-4658 ; 1742-464X
ISSN (online)	1742-4658
ISSN	1742-464X
DOI	10.1111/j.1742-4658.2008.06654.x
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Zs.A 260: Show issues

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Article ; Online: The effects of oligomerization on Saccharomyces cerevisiae Mcm4/6/7 function.

Ma, Xiaoli / Stead, Brent E / Rezvanpour, Atoosa / Davey, Megan J

BMC biochemistry

2010 Volume 11, Page(s) 37

Abstract: Background: Minichromosome maintenance proteins (Mcm) 2, 3, 4, 5, 6 and 7 are related by sequence and form a variety of complexes that unwind DNA, including Mcm4/6/7. A Mcm4/6/7 trimer forms one half of the Mcm2-7 hexameric ring and can be thought of as ...

Abstract	Background: Minichromosome maintenance proteins (Mcm) 2, 3, 4, 5, 6 and 7 are related by sequence and form a variety of complexes that unwind DNA, including Mcm4/6/7. A Mcm4/6/7 trimer forms one half of the Mcm2-7 hexameric ring and can be thought of as the catalytic core of Mcm2-7, the replicative helicase in eukaryotic cells. Oligomeric analysis of Mcm4/6/7 suggests that it forms a hexamer containing two Mcm4/6/7 trimers, however, under certain conditions trimeric Mcm4/6/7 has also been observed. The functional significance of the different Mcm4/6/7 oligomeric states has not been assessed. The results of such an assessment would have implications for studies of both Mcm4/6/7 and Mcm2-7. Results: Here, we show that Saccharomyces cerevisiae Mcm4/6/7 reconstituted from individual subunits exists in an equilibrium of oligomeric forms in which smaller oligomers predominate in the absence of ATP. In addition, we found that ATP, which is required for Mcm4/6/7 activity, shifts the equilibrium towards larger oligomers, likely hexamers of Mcm4/6/7. ATPγS and to a lesser extent ADP also shift the equilibrium towards hexamers. Study of Mcm4/6/7 complexes containing mutations that interfere with the formation of inter-subunit ATP sites (arginine finger mutants) indicates that full activity of Mcm4/6/7 requires all of its ATP sites, which are formed in a hexamer and not a trimer. In keeping with this observation, Mcm4/6/7 binds DNA as a hexamer. Conclusions: The minimal functional unit of Mcm4/6/7 is a hexamer. One of the roles of ATP binding by Mcm4/6/7 may be to stabilize formation of hexamers.
MeSH term(s)	Adenosine Triphosphate/chemistry ; Cell Cycle Proteins/chemistry ; Cell Cycle Proteins/metabolism ; Chromosomal Proteins, Non-Histone/chemistry ; Chromosomal Proteins, Non-Histone/metabolism ; Cross-Linking Reagents/chemistry ; DNA-Binding Proteins/chemistry ; DNA-Binding Proteins/metabolism ; Minichromosome Maintenance Complex Component 4 ; Minichromosome Maintenance Complex Component 6 ; Minichromosome Maintenance Complex Component 7 ; Nuclear Proteins/chemistry ; Nuclear Proteins/metabolism ; Protein Binding ; Protein Multimerization ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/chemistry ; Saccharomyces cerevisiae Proteins/metabolism
Chemical Substances	Cell Cycle Proteins ; Chromosomal Proteins, Non-Histone ; Cross-Linking Reagents ; DNA-Binding Proteins ; Nuclear Proteins ; Saccharomyces cerevisiae Proteins ; Adenosine Triphosphate (8L70Q75FXE) ; MCM4 protein, S cerevisiae (EC 3.6.4.12) ; MCM6 protein, S cerevisiae (EC 3.6.4.12) ; MCM7 protein, S cerevisiae (EC 3.6.4.12) ; Minichromosome Maintenance Complex Component 4 (EC 3.6.4.12) ; Minichromosome Maintenance Complex Component 6 (EC 3.6.4.12) ; Minichromosome Maintenance Complex Component 7 (EC 3.6.4.12)
Language	English
Publishing date	2010-09-22
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2041216-2
ISSN	1471-2091 ; 1471-2091
ISSN (online)	1471-2091
ISSN	1471-2091
DOI	10.1186/1471-2091-11-37
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Article ; Online: The effects of oligomerization on Saccharomyces cerevisiae Mcm4/6/7 function

Davey Megan J / Rezvanpour Atoosa / Stead Brent E / Ma Xiaoli

BMC Biochemistry, Vol 11, Iss 1, p

2010 Volume 37

Abstract: Abstract Background Minichromosome maintenance proteins (Mcm) 2, 3, 4, 5, 6 and 7 are related by sequence and form a variety of complexes that unwind DNA, including Mcm4/6/7. A Mcm4/6/7 trimer forms one half of the Mcm2-7 hexameric ring and can be ... ...

Abstract	Abstract Background Minichromosome maintenance proteins (Mcm) 2, 3, 4, 5, 6 and 7 are related by sequence and form a variety of complexes that unwind DNA, including Mcm4/6/7. A Mcm4/6/7 trimer forms one half of the Mcm2-7 hexameric ring and can be thought of as the catalytic core of Mcm2-7, the replicative helicase in eukaryotic cells. Oligomeric analysis of Mcm4/6/7 suggests that it forms a hexamer containing two Mcm4/6/7 trimers, however, under certain conditions trimeric Mcm4/6/7 has also been observed. The functional significance of the different Mcm4/6/7 oligomeric states has not been assessed. The results of such an assessment would have implications for studies of both Mcm4/6/7 and Mcm2-7. Results Here, we show that Saccharomyces cerevisiae Mcm4/6/7 reconstituted from individual subunits exists in an equilibrium of oligomeric forms in which smaller oligomers predominate in the absence of ATP. In addition, we found that ATP, which is required for Mcm4/6/7 activity, shifts the equilibrium towards larger oligomers, likely hexamers of Mcm4/6/7. ATPγS and to a lesser extent ADP also shift the equilibrium towards hexamers. Study of Mcm4/6/7 complexes containing mutations that interfere with the formation of inter-subunit ATP sites (arginine finger mutants) indicates that full activity of Mcm4/6/7 requires all of its ATP sites, which are formed in a hexamer and not a trimer. In keeping with this observation, Mcm4/6/7 binds DNA as a hexamer. Conclusions The minimal functional unit of Mcm4/6/7 is a hexamer. One of the roles of ATP binding by Mcm4/6/7 may be to stabilize formation of hexamers.
Keywords	Biochemistry ; QD415-436 ; Organic chemistry ; QD241-441 ; Chemistry ; QD1-999 ; Science ; Q ; DOAJ:Biochemistry ; DOAJ:Life Sciences ; DOAJ:Biology and Life Sciences
Language	English
Publishing date	2010-09-01T00:00:00Z
Publisher	BioMed Central
Document type	Article ; Online
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Article ; Online: Structure of an asymmetric ternary protein complex provides insight for membrane interaction.

Dempsey, Brian R / Rezvanpour, Atoosa / Lee, Ting-Wai / Barber, Kathryn R / Junop, Murray S / Shaw, Gary S

Structure (London, England : 1993)

2012 Volume 20, Issue 10, Page(s) 1737–1745

Abstract: Plasma membrane repair involves the coordinated effort of proteins and the inner phospholipid surface to mend the rupture and return the cell back to homeostasis. Here, we present the three-dimensional structure of a multiprotein complex that includes ... ...

Abstract	Plasma membrane repair involves the coordinated effort of proteins and the inner phospholipid surface to mend the rupture and return the cell back to homeostasis. Here, we present the three-dimensional structure of a multiprotein complex that includes S100A10, annexin A2, and AHNAK, which along with dysferlin, functions in muscle and cardiac tissue repair. The 3.5 Å resolution X-ray structure shows that a single region from the AHNAK C terminus is recruited by an S100A10-annexin A2 heterotetramer, forming an asymmetric ternary complex. The AHNAK peptide adopts a coil conformation that arches across the heterotetramer contacting both annexin A2 and S100A10 protomers with tight affinity (∼30 nM) and establishing a structural rationale whereby both S100A10 and annexin proteins are needed in AHNAK recruitment. The structure evokes a model whereby AHNAK is targeted to the membrane surface through sandwiching of the binding region between the S100A10/annexin A2 complex and the phospholipid membrane.
MeSH term(s)	Amino Acid Motifs ; Animals ; Annexin A2/chemistry ; Cell Membrane/chemistry ; Crystallography, X-Ray ; Membrane Proteins/chemistry ; Models, Molecular ; Neoplasm Proteins/chemistry ; Nuclear Magnetic Resonance, Biomolecular ; Peptide Fragments/chemistry ; Protein Binding ; Protein Interaction Domains and Motifs ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Rabbits ; Recombinant Fusion Proteins/chemistry ; S100 Proteins/chemistry
Chemical Substances	AHNAK protein, human ; ANXA2 protein, human ; Annexin A2 ; Membrane Proteins ; Neoplasm Proteins ; Peptide Fragments ; Recombinant Fusion Proteins ; S100 Proteins ; S100 calcium binding protein A10
Language	English
Publishing date	2012-10-10
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	1213087-4
ISSN	1878-4186 ; 0969-2126
ISSN (online)	1878-4186
ISSN	0969-2126
DOI	10.1016/j.str.2012.08.004
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