A. C. Matin: Difference between revisions

Add links
From Wikipedia, the free encyclopedia
Browse history interactively
← Previous editNext edit →
Content deleted Content added
VisualWikitext
Setting DEFAULTSORT key to Matin, A. C. using Hot Default Sort
Filled in 21 bare reference(s) with reFill 2
Line 40: Line 40:


===Bacterial hunger response===
===Bacterial hunger response===
Matin studied the effect of nutrient deprivation in bacteria, which is often experienced by them in the human body and the environment,<ref>{{cite journal | vauthors = Matin A, Veldkamp H | title = Physiological basis of the selective advantage of a Spirillum sp. in a carbon-limited environment | journal = Journal of General Microbiology | volume = 105 | issue = 2 | pages = 187–97 | date = April 1978 | pmid = 641523 | doi = 10.1099/00221287-105-2-187 }}</ref><ref>{{cite web|url=https://pubmed.ncbi.nlm.nih.gov/950555/|title=Influence of dilution rate on enzymes of intermediary metabolism in two freshwater bacteria grown in continuous culture}}</ref><ref name=Sigma/> and worked on induction of two classes of starvation genes named as cyclic AMP-dependent and independent.<ref>{{cite web|url=https://jb.asm.org/content/168/2/486.short|title=Starvation proteins in Escherichia coli: kinetics of synthesis and role in starvation survival.}}</ref> <ref name="auto2">{{cite web|url=https://jb.asm.org/content/160/3/1041.short|title=Role of protein synthesis in the survival of carbon-starved Escherichia coli K-12.}}</ref><ref name="auto1">{{cite web|url=https://jb.asm.org/content/170/9/3903.short|title=Differential regulation by cyclic AMP of starvation protein synthesis in Escherichia coli.}}</ref> He studied the comprehensive resistant state of the bacteria. For example, hunger stress made bacteria more resistant not only to nutrient deprivation but also to oxidative stress, a major resistance mechanism in humans against pathogenic bacteria, as well as to heat and osmotic stresses.<ref name="auto2"/><ref>{{cite web|url=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC211389/|title=Starvation-induced cross protection against heat or H2O2 challenge in Escherichia coli.}}</ref><ref>{{cite web|url=https://pubmed.ncbi.nlm.nih.gov/2185233/|title=Starvation-induced cross protection against osmotic challenge in Escherichia coli}}</ref>
Matin studied the effect of nutrient deprivation in bacteria, which is often experienced by them in the human body and the environment,<ref>{{cite journal | vauthors = Matin A, Veldkamp H | title = Physiological basis of the selective advantage of a Spirillum sp. in a carbon-limited environment | journal = Journal of General Microbiology | volume = 105 | issue = 2 | pages = 187–97 | date = April 1978 | pmid = 641523 | doi = 10.1099/00221287-105-2-187 }}</ref><ref>{{cite web|url=https://pubmed.ncbi.nlm.nih.gov/950555/|title=Influence of dilution rate on enzymes of intermediary metabolism in two freshwater bacteria grown in continuous culture}}</ref><ref name=Sigma/> and worked on induction of two classes of starvation genes named as cyclic AMP-dependent and independent.<ref>{{Cite journal|url=https://jb.asm.org/content/168/2/486|title=Starvation proteins in Escherichia coli: kinetics of synthesis and role in starvation survival.|first1=R. G.|last1=Groat|first2=J. E.|last2=Schultz|first3=E.|last3=Zychlinsky|first4=A.|last4=Bockman|first5=A.|last5=Matin|date=November 1, 1986|journal=Journal of Bacteriology|volume=168|issue=2|pages=486–493|via=jb.asm.org|doi=10.1128/jb.168.2.486-493.1986|pmid=3536847}}</ref> <ref name="auto2">{{Cite journal|url=https://jb.asm.org/content/160/3/1041|title=Role of protein synthesis in the survival of carbon-starved Escherichia coli K-12.|first1=C. A.|last1=Reeve|first2=P. S.|last2=Amy|first3=A.|last3=Matin|date=December 1, 1984|journal=Journal of Bacteriology|volume=160|issue=3|pages=1041–1046|via=jb.asm.org|pmid=6389505}}</ref><ref name="auto1">{{Cite journal|url=https://jb.asm.org/content/170/9/3903|title=Differential regulation by cyclic AMP of starvation protein synthesis in Escherichia coli.|first1=J. E.|last1=Schultz|first2=G. I.|last2=Latter|first3=A.|last3=Matin|date=September 1, 1988|journal=Journal of Bacteriology|volume=170|issue=9|pages=3903–3909|via=jb.asm.org|doi=10.1128/jb.170.9.3903-3909.1988|pmid=2842291}}</ref> He studied the comprehensive resistant state of the bacteria. For example, hunger stress made bacteria more resistant not only to nutrient deprivation but also to oxidative stress, a major resistance mechanism in humans against pathogenic bacteria, as well as to heat and osmotic stresses.<ref name="auto2"/><ref>{{cite web|url=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC211389/|title=Starvation-induced cross protection against heat or H2O2 challenge in Escherichia coli.}}</ref><ref>{{cite web|url=https://pubmed.ncbi.nlm.nih.gov/2185233/|title=Starvation-induced cross protection against osmotic challenge in Escherichia coli}}</ref>


Matin pioneered the discovery that this comprehensive resistance was due to cAMP-independent class of proteins, called the Pex proteins,<ref name="auto1"/> further he showed that the Pex protein synthesis was controlled by σs (formerly called KatF) and that this sigma factor thereby controlled development of the general stress response.<ref>{{cite web|url=https://pubmed.ncbi.nlm.nih.gov/2061293/|title=The putative sigma factor KatF has a central role in development of starvation-mediated general resistance in Escherichia coli}}</ref> Hunger stress was found to trigger the expression of virulence proteins in bacteria enhancing their pathogenic prowess.<ref>{{cite web|url=https://web.stanford.edu/~amatin/MatinLabHomePage/PDF/Stress%20response_2015.pdf|title=Stress, Bacterial:General and Specific. Reference Module in Biomedical Science}}</ref><ref>{{cite journal | vauthors = Sonenshein AL | title = CodY, a global regulator of stationary phase and virulence in Gram-positive bacteria | journal = Current Opinion in Microbiology | volume = 8 | issue = 2 | pages = 203–7 | date = April 2005 | pmid = 15802253 | doi = 10.1016/j.mib.2005.01.001 }}</ref>
Matin pioneered the discovery that this comprehensive resistance was due to cAMP-independent class of proteins, called the Pex proteins,<ref name="auto1"/> further he showed that the Pex protein synthesis was controlled by σs (formerly called KatF) and that this sigma factor thereby controlled development of the general stress response.<ref>{{cite web|url=https://pubmed.ncbi.nlm.nih.gov/2061293/|title=The putative sigma factor KatF has a central role in development of starvation-mediated general resistance in Escherichia coli}}</ref> Hunger stress was found to trigger the expression of virulence proteins in bacteria enhancing their pathogenic prowess.<ref>{{Cite web|url=https://web.stanford.edu/~amatin/MatinLabHomePage/PDF/Stress%20response_2015.pdf|title=Stress, Bacterial:General and Specific. Reference Module in Biomedical Science}}</ref><ref>{{cite journal | vauthors = Sonenshein AL | title = CodY, a global regulator of stationary phase and virulence in Gram-positive bacteria | journal = Current Opinion in Microbiology | volume = 8 | issue = 2 | pages = 203–7 | date = April 2005 | pmid = 15802253 | doi = 10.1016/j.mib.2005.01.001 }}</ref>


Matin’s work was instrumental in the discovery of σs and its regulation.<ref name="auto3">{{cite web|url=https://jb.asm.org/content/178/2/470.short|title=Regulation of Escherichia coli starvation sigma factor (sigma s) by ClpXP protease.}}</ref><ref>{{cite web|url=https://pubmed.ncbi.nlm.nih.gov/2014002/|title=The molecular basis of carbon-starvation-induced general resistance in Escherichia coli}}</ref> His research also resulted in the first identification of the physiological role for ClpXP protease, and showed that σs is rapidly degraded in fast growing cells by this protease; the site in the σs protein targeted by this protease was also identified.<ref name="auto3"/>
Matin’s work was instrumental in the discovery of σs and its regulation.<ref name="auto3">{{Cite journal|url=https://jb.asm.org/content/178/2/470|title=Regulation of Escherichia coli starvation sigma factor (sigma s) by ClpXP protease.|first1=T.|last1=Schweder|first2=K. H.|last2=Lee|first3=O.|last3=Lomovskaya|first4=A.|last4=Matin|date=January 1, 1996|journal=Journal of Bacteriology|volume=178|issue=2|pages=470–476|via=jb.asm.org|doi=10.1128/jb.178.2.470-476.1996|pmid=8550468}}</ref><ref>{{cite web|url=https://pubmed.ncbi.nlm.nih.gov/2014002/|title=The molecular basis of carbon-starvation-induced general resistance in Escherichia coli}}</ref> His research also resulted in the first identification of the physiological role for ClpXP protease, and showed that σs is rapidly degraded in fast growing cells by this protease; the site in the σs protein targeted by this protease was also identified.<ref name="auto3"/>


Matin used bioreactors to generate simulated microgravity (SMG) on Earth,<ref>{{cite web|url=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC532419/|title=Role and Regulation of σs in General Resistance Conferred by Low-Shear Simulated Microgravity in Escherichia coli}}</ref> and showed that uropathogenic Escherichia coli (UPEC) developed s-dependent comprehensive resistance under SMG, indicating that microgravity constitutes a stress.<ref>{{cite web|url=https://link.springer.com/chapter/10.1007/978-1-4939-3277-1_13|title=Cellular Response of Escherichia coli to Microgravity and Microgravity Analogue Culture}}</ref> He also studied protein folding and overproduced DnaK in an E. coil strain making the human growth hormone (HGH). His experiment resulted in much greater amount of normal and soluble HGH.<ref>{{cite web|url=https://www.nature.com/articles/nbt0392-301|title=DnaK-Mediated Alterations in Human Growth Hormone Protein Inclusion Bodies}}</ref>
Matin used bioreactors to generate simulated microgravity (SMG) on Earth,<ref>{{Cite journal|url=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC532419/|title=Role and Regulation of σs in General Resistance Conferred by Low-Shear Simulated Microgravity in Escherichia coli|first1=S. V.|last1=Lynch|first2=E. L.|last2=Brodie|first3=A.|last3=Matin|date=December 16, 2004|journal=Journal of Bacteriology|volume=186|issue=24|pages=8207–8212|via=PubMed Central|doi=10.1128/JB.186.24.8207-8212.2004|pmid=15576768}}</ref> and showed that uropathogenic Escherichia coli (UPEC) developed s-dependent comprehensive resistance under SMG, indicating that microgravity constitutes a stress.<ref>{{Cite book|url=https://doi.org/10.1007/978-1-4939-3277-1_13|title=Effect of Spaceflight and Spaceflight Analogue Culture on Human and Microbial Cells: Novel Insights into Disease Mechanisms|first1=Rachna|last1=Singh|first2=A. C.|last2=Matin|editor-first1=Cheryl A.|editor-last1=Nickerson|editor-first2=Neal R.|editor-last2=Pellis|editor-first3=C. Mark|editor-last3=Ott|date=April 16, 2016|publisher=Springer|pages=259–282|via=Springer Link|doi=10.1007/978-1-4939-3277-1_13}}</ref> He also studied protein folding and overproduced DnaK in an E. coil strain making the human growth hormone (HGH). His experiment resulted in much greater amount of normal and soluble HGH.<ref>{{cite web|url=https://www.nature.com/articles/nbt0392-301|title=DnaK-Mediated Alterations in Human Growth Hormone Protein Inclusion Bodies}}</ref>


===Antibiotic resistance===
===Antibiotic resistance===
Matin conducted research on the bacterial antibiotic resistance along with the threat of multidrug resistance (MDR) pumps in public health. His work indicated the regulation of the MDR pump by emrRAB operon and the EmrR protein.<ref>{{cite web|url=https://aac.asm.org/content/44/10/2905.short|title=The EmrR Protein Represses the Escherichia coli emrRAB Multidrug Resistance Operon by Directly Binding to Its Promoter Region}}</ref><ref name="auto">{{cite web|url=https://jb.asm.org/content/177/9/2328.short|title=EmrR is a negative regulator of the Escherichia coli multidrug resistance pump EmrAB.}}</ref> He found that the antibiotics alter the EmrR and prevent its binding to the promoter which leads to the synthesis of the pump and MDR.<ref name="auto"/> He also showed that EmrR induces of the mcb operon protecting bacteria against additional antibiotics (e.g., fluoroquinolones).<ref>{{cite web|url=https://pubmed.ncbi.nlm.nih.gov/8849229/|title=Differential regulation of the mcb and emr operons of Escherichia coli: role of mcb in multidrug resistance}}</ref>
Matin conducted research on the bacterial antibiotic resistance along with the threat of multidrug resistance (MDR) pumps in public health. His work indicated the regulation of the MDR pump by emrRAB operon and the EmrR protein.<ref>{{Cite journal|url=https://aac.asm.org/content/44/10/2905|title=The EmrR Protein Represses the Escherichia coli emrRAB Multidrug Resistance Operon by Directly Binding to Its Promoter Region|first1=A.|last1=Xiong|first2=A.|last2=Gottman|first3=C.|last3=Park|first4=M.|last4=Baetens|first5=S.|last5=Pandza|first6=A.|last6=Matin|date=October 1, 2000|journal=Antimicrobial Agents and Chemotherapy|volume=44|issue=10|pages=2905–2907|via=aac.asm.org|doi=10.1128/AAC.44.10.2905-2907.2000|pmid=10991887}}</ref><ref name="auto">{{Cite journal|url=https://jb.asm.org/content/177/9/2328|title=EmrR is a negative regulator of the Escherichia coli multidrug resistance pump EmrAB.|first1=O.|last1=Lomovskaya|first2=K.|last2=Lewis|first3=A.|last3=Matin|date=May 1, 1995|journal=Journal of Bacteriology|volume=177|issue=9|pages=2328–2334|via=jb.asm.org|doi=10.1128/jb.177.9.2328-2334.1995|pmid=7730261}}</ref> He found that the antibiotics alter the EmrR and prevent its binding to the promoter which leads to the synthesis of the pump and MDR.<ref name="auto"/> He also showed that EmrR induces of the mcb operon protecting bacteria against additional antibiotics (e.g., fluoroquinolones).<ref>{{cite web|url=https://pubmed.ncbi.nlm.nih.gov/8849229/|title=Differential regulation of the mcb and emr operons of Escherichia coli: role of mcb in multidrug resistance}}</ref>


Matin discovered the mechanism of bactericidal antibiotics for generating oxidative stress.<ref name=Sigma>{{cite web|url=https://aac.asm.org/content/58/10/5964|title=Sigma S-Dependent Antioxidant Defense Protects Stationary-Phase Escherichia coli against the Bactericidal Antibiotic Gentamicin}}</ref> His research indicated that suppressing UPEC antioxidant defense can bolster gentamicin (Gm) effectiveness In treating cystitis. He also studied the effects of σs-mediated enhanced resistance and SMG.<ref>{{cite web|url=https://aem.asm.org/content/72/12/7701.short|title=Escherichia coli Biofilms Formed under Low-Shear Modeled Microgravity in a Ground-Based System}}</ref><ref>{{cite web|url=https://www.sciencedirect.com/science/article/abs/pii/S2214552417300251|title=Payload hardware and experimental protocol development to enable future testing of the effect of space microgravity on the resistance to gentamicin of uropathogenic Escherichia coli and its σs-deficient mutant}}</ref> Based on these studies, Matin in collaboration with NASA, designed a payload system for testing the effect of space microgravity on UPEC Gm resistance and confirmed that silencing of σs will make Gm more effective against bacterial infections also in space flight,<ref>{{cite web|url=https://www.sciencedirect.com/science/article/pii/S2214552419301257|title=EcAMSat spaceflight measurements of the role of σs in antibiotic resistance of stationary phase Escherichia coli in microgravity}}</ref><ref>{{cite web|url=https://web.stanford.edu/~amatin/MatinLabHomePage/PDF/EcAmSat.pdf|title=Payload hardware and experimental protocol development to enable future testing of the effect of space microgravity on the resistance to gentamicin of uropathogenic Escherichia coli and its σs-deficient mutant }}</ref> providing the means of increasing Gm effectiveness both on Earth and space.
Matin discovered the mechanism of bactericidal antibiotics for generating oxidative stress.<ref name=Sigma>{{Cite journal|url=https://aac.asm.org/content/58/10/5964|title=Sigma S-Dependent Antioxidant Defense Protects Stationary-Phase Escherichia coli against the Bactericidal Antibiotic Gentamicin|first1=Jing-Hung|last1=Wang|first2=Rachna|last2=Singh|first3=Michael|last3=Benoit|first4=Mimi|last4=Keyhan|first5=Matthew|last5=Sylvester|first6=Michael|last6=Hsieh|first7=Anuradha|last7=Thathireddy|first8=Yi-Ju|last8=Hsieh|first9=A. C.|last9=Matin|date=October 1, 2014|journal=Antimicrobial Agents and Chemotherapy|volume=58|issue=10|pages=5964–5975|via=aac.asm.org|doi=10.1128/AAC.03683-14|pmid=25070093}}</ref> His research indicated that suppressing UPEC antioxidant defense can bolster gentamicin (Gm) effectiveness In treating cystitis. He also studied the effects of σs-mediated enhanced resistance and SMG.<ref>{{Cite journal|url=https://aem.asm.org/content/72/12/7701|title=Escherichia coli Biofilms Formed under Low-Shear Modeled Microgravity in a Ground-Based System|first1=S. V.|last1=Lynch|first2=K.|last2=Mukundakrishnan|first3=M. R.|last3=Benoit|first4=P. S.|last4=Ayyaswamy|first5=A.|last5=Matin|date=December 1, 2006|journal=Applied and Environmental Microbiology|volume=72|issue=12|pages=7701–7710|via=aem.asm.org|doi=10.1128/AEM.01294-06|pmid=17028231}}</ref><ref>{{Cite journal|url=https://www.sciencedirect.com/science/article/abs/pii/S2214552417300251|title=Payload hardware and experimental protocol development to enable future testing of the effect of space microgravity on the resistance to gentamicin of uropathogenic Escherichia coli and its σs-deficient mutant|date=November 1, 2017|journal=Life Sciences in Space Research|volume=15|pages=1–10|via=www.sciencedirect.com|doi=10.1016/j.lssr.2017.05.001}}</ref> Based on these studies, Matin in collaboration with NASA, designed a payload system for testing the effect of space microgravity on UPEC Gm resistance and confirmed that silencing of σs will make Gm more effective against bacterial infections also in space flight,<ref>{{Cite journal|url=https://www.sciencedirect.com/science/article/pii/S2214552419301257|title=EcAMSat spaceflight measurements of the role of σs in antibiotic resistance of stationary phase Escherichia coli in microgravity|date=February 1, 2020|journal=Life Sciences in Space Research|volume=24|pages=18–24|via=www.sciencedirect.com|doi=10.1016/j.lssr.2019.10.007}}</ref><ref>{{Cite web|url=https://web.stanford.edu/~amatin/MatinLabHomePage/PDF/EcAmSat.pdf|title=Payload hardware and experimental protocol development to enable future testing of the effect of space microgravity on the resistance to gentamicin of uropathogenic Escherichia coli and its σs-deficient mutant}}</ref> providing the means of increasing Gm effectiveness both on Earth and space.


Matin focused on bacterial biofilms as a challenge in disease treatment. He used his discovery that E. coli strains fluoresce upon tetracycline treatment to test if biofilm penetration barrier accounted for their enhanced resistance. Tetracycline caused cells to fluoresce throughout the biofilms indicating no role for the penetration barrier.<ref>{{cite web|url=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC127323/|title=Tetracycline Rapidly Reaches All the Constituent Cells of Uropathogenic Escherichia coli Biofilms}}</ref> However, a UPEC mutant missing the rapA gene, generated by Matin, showed that impaired penetration had a role in biofilm resistance to penicillin, norfloxacin, chloramphenicol, and Gm, and that, in addition, the yhcQ gene, which encoded a putative MDR pump was also involved.<ref>{{cite web|url=https://aac.asm.org/content/51/10/3650.short|title=Role of the rapA Gene in Controlling Antibiotic Resistance of Escherichia coli Biofilms}}</ref> That biofilm resistance differ for different antibiotics and different bacteria is now widely accepted.
Matin focused on bacterial biofilms as a challenge in disease treatment. He used his discovery that E. coli strains fluoresce upon tetracycline treatment to test if biofilm penetration barrier accounted for their enhanced resistance. Tetracycline caused cells to fluoresce throughout the biofilms indicating no role for the penetration barrier.<ref>{{Cite journal|url=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC127323/|title=Tetracycline Rapidly Reaches All the Constituent Cells of Uropathogenic Escherichia coli Biofilms|first1=G.|last1=Stone|first2=P.|last2=Wood|first3=L.|last3=Dixon|first4=M.|last4=Keyhan|first5=A.|last5=Matin|date=August 16, 2002|journal=Antimicrobial Agents and Chemotherapy|volume=46|issue=8|pages=2458–2461|via=PubMed Central|doi=10.1128/AAC.46.8.2458-2461.2002|pmid=12121918}}</ref> However, a UPEC mutant missing the rapA gene, generated by Matin, showed that impaired penetration had a role in biofilm resistance to penicillin, norfloxacin, chloramphenicol, and Gm, and that, in addition, the yhcQ gene, which encoded a putative MDR pump was also involved.<ref>{{Cite journal|url=https://aac.asm.org/content/51/10/3650|title=Role of the rapA Gene in Controlling Antibiotic Resistance of Escherichia coli Biofilms|first1=S. V.|last1=Lynch|first2=L.|last2=Dixon|first3=M. R.|last3=Benoit|first4=E. L.|last4=Brodie|first5=M.|last5=Keyhan|first6=P.|last6=Hu|first7=D. F.|last7=Ackerley|first8=G. L.|last8=Andersen|first9=A.|last9=Matin|date=October 1, 2007|journal=Antimicrobial Agents and Chemotherapy|volume=51|issue=10|pages=3650–3658|via=aac.asm.org|doi=10.1128/AAC.00601-07|pmid=17664315}}</ref> That biofilm resistance differ for different antibiotics and different bacteria is now widely accepted.


===Molecular bioremediation===
===Molecular bioremediation===
Matin has also studied bacterial bioremediation of the carcinogens chromate Cr(VI) and uranyl U(VI), which are wide-spread environmental pollutants, especially in the Department of Energy waste sites,<ref>{{cite web|url=https://web.stanford.edu/~amatin/MatinLabHomePage/PDF/Targets-Keyhan2003.pdf|title=TARGETS OF IMPROVEMENT IN BACTERIAL CHROMATE BIOREMEDIATION}}</ref> and worked on their bioremediation to the insoluble and nontoxic Cr(III) and U(IV). He studied various consequences after the bacterial exposure to chromate and uranyl, and found that the post-exposure effects resulted in one electron reduction of these carcinogens, generating the radicals Cr and U(V) by flavoproteins with various essential metabolic functions. These radicals interacted with oxygen, and generated large quantities of ROS by redox cycling, poisoning the bacteria.<ref>{{cite web|url=https://sfamjournals.onlinelibrary.wiley.com/doi/abs/10.1111/j.1462-2920.2004.00639.x|title=Mechanism of chromate reduction by the Escherichia coli protein, NfsA, and the role of different chromate reductases in minimizing oxidative stress during chromate reduction}}</ref><ref>{{cite web|url=https://pubmed.ncbi.nlm.nih.gov/16621832/#:~:text=The%20nature%20of%20the%20stress,withstand%20this%20stress%2C%20were%20examined.&text=Chromate%20exposure%20depleted%20cellular%20levels,in%20nonadapted%20than%20preadapted%20cells|title=Effect of chromate stress on Escherichia coli K-12}}</ref>
Matin has also studied bacterial bioremediation of the carcinogens chromate Cr(VI) and uranyl U(VI), which are wide-spread environmental pollutants, especially in the Department of Energy waste sites,<ref>{{Cite web|url=https://web.stanford.edu/~amatin/MatinLabHomePage/PDF/Targets-Keyhan2003.pdf|title=TARGETS OF IMPROVEMENT IN BACTERIAL CHROMATE BIOREMEDIATION}}</ref> and worked on their bioremediation to the insoluble and nontoxic Cr(III) and U(IV). He studied various consequences after the bacterial exposure to chromate and uranyl, and found that the post-exposure effects resulted in one electron reduction of these carcinogens, generating the radicals Cr and U(V) by flavoproteins with various essential metabolic functions. These radicals interacted with oxygen, and generated large quantities of ROS by redox cycling, poisoning the bacteria.<ref>{{cite web|url=https://sfamjournals.onlinelibrary.wiley.com/doi/abs/10.1111/j.1462-2920.2004.00639.x|title=Mechanism of chromate reduction by the Escherichia coli protein, NfsA, and the role of different chromate reductases in minimizing oxidative stress during chromate reduction}}</ref><ref>{{Cite journal|url=https://pubmed.ncbi.nlm.nih.gov/16621832/#:~:text=The+nature+of+the+stress,withstand+this+stress,+were+examined.&text=Chromate+exposure+depleted+cellular+levels,in+nonadapted+than+preadapted+cells|title=Effect of chromate stress on Escherichia coli K-12|first1=D. F.|last1=Ackerley|first2=Y.|last2=Barak|first3=S. V.|last3=Lynch|first4=J.|last4=Curtin|first5=A.|last5=Matin|date=May 16, 2006|journal=Journal of Bacteriology|volume=188|issue=9|pages=3371–3381|via=PubMed|doi=10.1128/JB.188.9.3371-3381.2006|pmid=16621832|pmc=1447458}}</ref>


Matin discovered a new class of enzymes, such as ChrR of E. coli, which are obligatory two-/four-electron reducers; these pre-empted the generation of the radicals. He then improved these enzymes and engineered bacteria more effective in remediating these carcinogens.<ref>{{cite web|url=https://www.jbc.org/content/280/24/22590.short|title=ChrR, a Soluble Quinone Reductase of Pseudomonas putida That Defends against H2O2}}</ref> He also studied the physiological role of ChrR, which is to convert quinones to hydroxyquinones in one step, thus preventing the formation of semiquinones, which also redox cycle. In addition, this enzyme prevents redox cycling of numerous compounds generated during metabolism within the bacteria, and those present in the environment that have the proclivity for one-electron reduction.
Matin discovered a new class of enzymes, such as ChrR of E. coli, which are obligatory two-/four-electron reducers; these pre-empted the generation of the radicals. He then improved these enzymes and engineered bacteria more effective in remediating these carcinogens.<ref>{{Cite journal|url=https://www.jbc.org/article/S0021-9258(20)61424-7/abstract|title=ChrR, a Soluble Quinone Reductase of Pseudomonas putida That Defends against H2O2*|first1=Claudio F.|last1=Gonzalez|first2=David F.|last2=Ackerley|first3=Susan V.|last3=Lynch|first4=A.|last4=Matin|date=June 17, 2005|journal=Journal of Biological Chemistry|volume=280|issue=24|pages=22590–22595|via=www.jbc.org|doi=10.1074/jbc.M501654200|pmid=15840577}}</ref> He also studied the physiological role of ChrR, which is to convert quinones to hydroxyquinones in one step, thus preventing the formation of semiquinones, which also redox cycle. In addition, this enzyme prevents redox cycling of numerous compounds generated during metabolism within the bacteria, and those present in the environment that have the proclivity for one-electron reduction.


==Awards/Honors==
==Awards/Honors==
Line 66: Line 66:
*1995 - Elected Fellow, American Academy of Microbiology
*1995 - Elected Fellow, American Academy of Microbiology
*2011 - Elected Associate Fellow, American Aerospace Medical Association
*2011 - Elected Associate Fellow, American Aerospace Medical Association
*Honorary Editorial Board Member, London Journals Press<ref>{{cite web|url=https://journalspress.com/research/editorial-board|title=EDITORIAL BOARD}}</ref>
*Honorary Editorial Board Member, London Journals Press<ref>{{Cite web|url=https://journalspress.com/editorial-board/|title=Editorial Board|website=London Journals Press}}</ref>
*1992-1994 - Review Committee of the Accreditation Board for Engineering and Technology (ABET)
*1992-1994 - Review Committee of the Accreditation Board for Engineering and Technology (ABET)


Revision as of 06:59, 16 April 2021

A. C. Matin
Born1941
Delhi, India
NationalityIndian-American
Occupation(s)Microbiologist, immunologist, and academician
AwardsElected Fellow, American Academy of Microbiology
Elected Associate Fellow, Aerospace Medical Association
Recipient of NASA honor award for the ECAMSAT Project
Review Committee of the Accreditation Board for Engineering and Technology (ABET)
Academic background
EducationB.S., Microbiology
M.S., Microbiology
Ph.D., Microbiology
Alma materUniversity of Karachi, Pakistan
University of California, Los Angeles
Academic work
InstitutionsStanford University School of Medicine

A. C. Matin is an Indian-American microbiologist, immunologist, academician and researcher. He is a Professor of Microbiology & Immunology at Stanford University School of Medicine.[1]

Matin has published over 100 research papers plus several reviews and has many patents registered in his name. His research is focused on bio-molecular engineering, cellular resistance and virulence, drug discovery, biology of microgravity, bioremediation, stress promoters, stress sensing, and biotechnology. He has made pioneering research contributions in biology and physiology of mixotrophy, starvation responses at the cellular and genetic levels, bacterial multidrug and biofilm resistance, role of G proteins in starvation and motility, discovery of an imageable cancer prodrug, specific drug targeting and the development of heritable contrast agent for molecular resonance imaging. Matin’s work on antibiotic resistance along with his work as a Principal Investigator on E. coli AntiMicrobial Satellite (EcAMSat) system resulted in NASA sending E. coli to space for astronaut health protection in 2017.[2] He is the recipient of NASA honor award for the ECAMSAT Project.

Matin was the Editor-in-Chief of Open Access Journal of Applied Sciences.

Education

Matin studied Microbiology at University of Karachi and received his Bachelor and Master’s degrees in 1960 and 1962, respectively, followed by college-level teaching for two years. He was awarded a Fulbright Fellowship, moved to USA and earned his Ph.D. degree in Microbiology from University of California, Los Angeles in 1969. He completed his postdoctoral research from University of California in 1971.[1]

Career

Following his postdoctoral studies, Matin joined University of Groningen in the Netherlands as a First Class Scientific Officer from 1971 till 1975 before moving back to USA and being appointed by Stanford University. He is a Professor in Department of Microbiology and Immunology and is associated with Cancer Institute, Program in Genetic and Molecular Medicine, Woods Environmental Institute,[3]Cardiovascular Institute, Institute for Immunity, and BioX Program[4] at Stanford University. From 1989 till 1998 (when the program ended), he served as a Professor at Western Region Hazardous Substance Research Center at the University.[1]

Research

Matin’s work is focused on various microbiology and biotechnology related topics including antibiotic resistance, cancer research, bio-molecular engineering, biofilms, cellular resistance and virulence, biology of microgravity, bioremediation, stress promoters, stress sensing, and systems biology. His work in bioenergetics provided fundamental insights into how acidophilic bacteria, which grow at a pH of 3 or lower, keep a neutral cytoplasm.[5]

Enzyme improvement and targeted therapy for cancer research

Matin discovered a new gene delivered enzyme prodrug therapy consisting of CNOB,[6] and the enzyme ChrR which activates the CNOB. He then improved and humanized the enzyme to HChrR6[7] by using non structure-based approaches like DNA shuffling;[8] a novel statistical method for protein improvement,[9] as well as analyzing HChrR structure.[10]

Matin found that the activated toxic product of CNOB, MCHB, is highly fluorescent[11] and used this discovery for the development of a method using mRNA for targeting the HChrR6 gene specifically to cancer.[12] He generated exosomes loaded with the HChrR6 mRNA that displayed high affinity anti-HER2 scFv, and named them EXODEPTs; the EXODEPTs specifically targeted the HER2 receptor and delivered the HChrR6 mRNA only to HER2-positive cells.[13] Matin applied systemic EXODEPT injection along with CNOB or tretazicar (CB1954), and found complete growth arrest of orthotopic HER2 positive breast cancer xenografts in mice without injuring other tissues or organs, indicating no off-target prodrug activation. This work was high-lighted in Science Translational Medicine.[14] He was the pioneer in using exosomes to deliver exogenous mRNA.[13][12] Matin also showed that magentotactic bacteria can specifically target tumors in mice and generate both positive and negative magnetic resonance imaging signals, and thus provide a potential tool for improved MRI visualization; this was the first use of these bacteria for this purpose.[15]

Bacterial hunger response

Matin studied the effect of nutrient deprivation in bacteria, which is often experienced by them in the human body and the environment,[16][17][18] and worked on induction of two classes of starvation genes named as cyclic AMP-dependent and independent.[19] [20][21] He studied the comprehensive resistant state of the bacteria. For example, hunger stress made bacteria more resistant not only to nutrient deprivation but also to oxidative stress, a major resistance mechanism in humans against pathogenic bacteria, as well as to heat and osmotic stresses.[20][22][23]

Matin pioneered the discovery that this comprehensive resistance was due to cAMP-independent class of proteins, called the Pex proteins,[21] further he showed that the Pex protein synthesis was controlled by σs (formerly called KatF) and that this sigma factor thereby controlled development of the general stress response.[24] Hunger stress was found to trigger the expression of virulence proteins in bacteria enhancing their pathogenic prowess.[25][26]

Matin’s work was instrumental in the discovery of σs and its regulation.[27][28] His research also resulted in the first identification of the physiological role for ClpXP protease, and showed that σs is rapidly degraded in fast growing cells by this protease; the site in the σs protein targeted by this protease was also identified.[27]

Matin used bioreactors to generate simulated microgravity (SMG) on Earth,[29] and showed that uropathogenic Escherichia coli (UPEC) developed s-dependent comprehensive resistance under SMG, indicating that microgravity constitutes a stress.[30] He also studied protein folding and overproduced DnaK in an E. coil strain making the human growth hormone (HGH). His experiment resulted in much greater amount of normal and soluble HGH.[31]

Antibiotic resistance

Matin conducted research on the bacterial antibiotic resistance along with the threat of multidrug resistance (MDR) pumps in public health. His work indicated the regulation of the MDR pump by emrRAB operon and the EmrR protein.[32][33] He found that the antibiotics alter the EmrR and prevent its binding to the promoter which leads to the synthesis of the pump and MDR.[33] He also showed that EmrR induces of the mcb operon protecting bacteria against additional antibiotics (e.g., fluoroquinolones).[34]

Matin discovered the mechanism of bactericidal antibiotics for generating oxidative stress.[18] His research indicated that suppressing UPEC antioxidant defense can bolster gentamicin (Gm) effectiveness In treating cystitis. He also studied the effects of σs-mediated enhanced resistance and SMG.[35][36] Based on these studies, Matin in collaboration with NASA, designed a payload system for testing the effect of space microgravity on UPEC Gm resistance and confirmed that silencing of σs will make Gm more effective against bacterial infections also in space flight,[37][38] providing the means of increasing Gm effectiveness both on Earth and space.

Matin focused on bacterial biofilms as a challenge in disease treatment. He used his discovery that E. coli strains fluoresce upon tetracycline treatment to test if biofilm penetration barrier accounted for their enhanced resistance. Tetracycline caused cells to fluoresce throughout the biofilms indicating no role for the penetration barrier.[39] However, a UPEC mutant missing the rapA gene, generated by Matin, showed that impaired penetration had a role in biofilm resistance to penicillin, norfloxacin, chloramphenicol, and Gm, and that, in addition, the yhcQ gene, which encoded a putative MDR pump was also involved.[40] That biofilm resistance differ for different antibiotics and different bacteria is now widely accepted.

Molecular bioremediation

Matin has also studied bacterial bioremediation of the carcinogens chromate Cr(VI) and uranyl U(VI), which are wide-spread environmental pollutants, especially in the Department of Energy waste sites,[41] and worked on their bioremediation to the insoluble and nontoxic Cr(III) and U(IV). He studied various consequences after the bacterial exposure to chromate and uranyl, and found that the post-exposure effects resulted in one electron reduction of these carcinogens, generating the radicals Cr and U(V) by flavoproteins with various essential metabolic functions. These radicals interacted with oxygen, and generated large quantities of ROS by redox cycling, poisoning the bacteria.[42][43]

Matin discovered a new class of enzymes, such as ChrR of E. coli, which are obligatory two-/four-electron reducers; these pre-empted the generation of the radicals. He then improved these enzymes and engineered bacteria more effective in remediating these carcinogens.[44] He also studied the physiological role of ChrR, which is to convert quinones to hydroxyquinones in one step, thus preventing the formation of semiquinones, which also redox cycle. In addition, this enzyme prevents redox cycling of numerous compounds generated during metabolism within the bacteria, and those present in the environment that have the proclivity for one-electron reduction.

Awards/Honors

  • 1964-1971 - Fulbright Fellowship
  • 1991, 1995 - Star Award, Environmental Protection Agency
  • 1991-1993 - ASM Foundation for Microbiology Lecturer
  • 1995 - Elected Fellow, American Academy of Microbiology
  • 2011 - Elected Associate Fellow, American Aerospace Medical Association
  • Honorary Editorial Board Member, London Journals Press[45]
  • 1992-1994 - Review Committee of the Accreditation Board for Engineering and Technology (ABET)

Bibliography

  • Alexis V. Forterre, Jing-Hung Wang, Alain Delcayre, Kyuri Kim, Carol Green, Mark D. Pegram, Stefanie S. Jeffrey, A. C. Matin. EV-mediated in vitro transcribed mRNA-based gene delivery for targeted treatment of HER2+ breast cancer xenografts in mice by CB1954 without general toxicity. Molecular Cancer Therapeutics, Published Online, January 15, 2020; DOI: 10.1158/1535-7163.MCT-19-0928
  • Michael R. Padgen, Matthew P. Lera, Macarena P. Parra, Antonio J. Ricco, Matthew Chin, Tori N. Chinn, Aaron Cohen, Charlie R. Friedericks, Michael B. Henschke, Timothy V. Snyder, Stevan M. Spremo, Jing-Hung Wang, AC Matin. EcAMSat spaceflight measurements of the role of σS in antibiotic resistance of stationary phase Escherichia coli in microgravity. Life Sciences in Space Research 24 (2020) 18-24
  • Kanada, M., Bachmann, M. H., Hardy, J. W., Frimannson, D. O., Bronsart, L., Wang, A., Matin, A. C. ... & Contag, C. H. (2015). Differential fates of biomolecules delivered to target cells via extracellular vesicles. Proceedings of the National Academy of Sciences, 112(12), E1433-E1442.
  • Wang, J. H., Singh, R., Benoit, M., Keyhan, M., Sylvester, M., Hsieh, M., ... & Matin, A. C. (2014). Sigma S-dependent antioxidant defense protects stationary-phase Escherichia coli against the bactericidal antibiotic gentamicin. Antimicrobial agents and chemotherapy, 58(10), 5964-5975.
  • Zhang H., Cohen A.L., Krishnakumar S., Wapnir I.L., Veeriah S., Deng G., Coram M.A., Piskun C.M., Longacre T.A., Herrler M., Frimannsson D.O., Telli M.L., Dirbas F.M., Matin A.C. … & Jeffrey S.S. 2014. Patient-derived xenografts of triple-negative breast cancer reproduce molecular features of patient tumors and respond to mTOR inhibition. Breast Cancer Res. 2014 Apr 7;16(2)
  • Gonzalez, C.F., D.F. Ackerley, S.V. Lynch, and A. Matin. 2005. ChrR, a soluble quinone reductase of Pseudomonas putida that defends against H2O2. The Journal of Biological Chemistry. 280: 22590-22595.
  • Schweder, T., K. Lee, O. Lomovskaya, and A. Matin. 1996. Regulation of Escherichia coli starvation sigma factor (s) by ClpXP protease. Journal of Bacteriology 178: 470-476.
  • Schultz, J., and A. Matin. 1991. Molecular and functional characterization of a carbon starvation gene of Escherichia coli. Journal of Molecular Biology, 218:129-140.
  • Reeve, C. A., Amy, P. S., & Matin, A. (1984). Role of protein synthesis in the survival of carbon-starved Escherichia coli K-12. Journal of Bacteriology, 160(3), 1041-1046.

References

  1. ^ a b c "AC Matin".
  2. ^ Tabor, Abigail (November 16, 2017). "NASA Is Sending E. coli to Space for Astronaut Health". NASA.
  3. ^ "AC Matin". Stanford Woods Institute for the Environment. June 21, 2018.
  4. ^ "A. C. Matin - Professor of Microbiology and Immunology". Welcome to Bio-X. March 7, 2014.
  5. ^ "Ion Transport in Acidophiles" (PDF).
  6. ^ "Europe PMC". europepmc.org.
  7. ^ Barak Y, Thorne SH, Ackerley DF, Lynch SV, Contag CH, Matin A (January 2006). "New enzyme for reductive cancer chemotherapy, YieF, and its improvement by directed evolution". Molecular Cancer Therapeutics. 5 (1): 97–103. doi:10.1158/1535-7163.MCT-05-0365. PMID 16432167.
  8. ^ Barak Y, Ackerley DF, Dodge CJ, Banwari L, Alex C, Francis AJ, Matin A (November 2006). "Analysis of novel soluble chromate and uranyl reductases and generation of an improved enzyme by directed evolution". Applied and Environmental Microbiology. 72 (11): 7074–82. doi:10.1128/AEM.01334-06. PMC 1636143. PMID 17088379.
  9. ^ Barak Y, Nov Y, Ackerley DF, Matin A (February 2008). "Enzyme improvement in the absence of structural knowledge: a novel statistical approach". The ISME Journal. 2 (2): 171–9. doi:10.1038/ismej.2007.100. PMID 18253133.
  10. ^ Eswaramoorthy S, Poulain S, Hienerwadel R, Bremond N, Sylvester MD, Zhang YB, et al. (April 27, 2012). "Crystal structure of ChrR--a quinone reductase with the capacity to reduce chromate". PloS One. 7 (4): e36017. doi:10.1371/journal.pone.0036017. PMC 3338774. PMID 22558308.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  11. ^ Wang JH, Endsley AN, Green CE, Matin AC (July 2016). "Utilizing native fluorescence imaging, modeling and simulation to examine pharmacokinetics and therapeutic regimen of a novel anticancer prodrug". BMC Cancer. 16 (1): 524. doi:10.1186/s12885-016-2508-6. PMC 4960810. PMID 27457630.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  12. ^ a b Forterre AV, Wang JH, Delcayre A, Kim K, Green C, Pegram MD, et al. (March 2020). "Extracellular Vesicle-Mediated In Vitro Transcribed mRNA Delivery for Treatment of HER2+ Breast Cancer Xenografts in Mice by Prodrug CB1954 without General Toxicity". Molecular Cancer Therapeutics. 19 (3): 858–867. doi:10.1158/1535-7163.MCT-19-0928. PMID 31941722.
  13. ^ a b Wang JH, Forterre AV, Zhao J, Frimannsson DO, Delcayre A, Antes TJ, et al. (May 2018). "Anti-HER2 scFv-Directed Extracellular Vesicle-Mediated mRNA-Based Gene Delivery Inhibits Growth of HER2-Positive Human Breast Tumor Xenografts by Prodrug Activation". Molecular Cancer Therapeutics. 17 (5): 1133–1142. doi:10.1158/1535-7163.MCT-17-0827. PMID 29483213.
  14. ^ Jay, Steven M. (March 21, 2018). "An EVolving approach to directed enzyme prodrug therapy for cancer". Science Translational Medicine. 10 (433). doi:10.1126/scitranslmed.aat1642 – via stm.sciencemag.org.
  15. ^ Benoit MR, Mayer D, Barak Y, Chen IY, Hu W, Cheng Z, et al. (August 2009). "Visualizing implanted tumors in mice with magnetic resonance imaging using magnetotactic bacteria". Clinical Cancer Research. 15 (16): 5170–7. doi:10.1158/1078-0432.CCR-08-3206. PMID 19671860.
  16. ^ Matin A, Veldkamp H (April 1978). "Physiological basis of the selective advantage of a Spirillum sp. in a carbon-limited environment". Journal of General Microbiology. 105 (2): 187–97. doi:10.1099/00221287-105-2-187. PMID 641523.
  17. ^ "Influence of dilution rate on enzymes of intermediary metabolism in two freshwater bacteria grown in continuous culture".
  18. ^ a b Wang, Jing-Hung; Singh, Rachna; Benoit, Michael; Keyhan, Mimi; Sylvester, Matthew; Hsieh, Michael; Thathireddy, Anuradha; Hsieh, Yi-Ju; Matin, A. C. (October 1, 2014). "Sigma S-Dependent Antioxidant Defense Protects Stationary-Phase Escherichia coli against the Bactericidal Antibiotic Gentamicin". Antimicrobial Agents and Chemotherapy. 58 (10): 5964–5975. doi:10.1128/AAC.03683-14. PMID 25070093 – via aac.asm.org.
  19. ^ Groat, R. G.; Schultz, J. E.; Zychlinsky, E.; Bockman, A.; Matin, A. (November 1, 1986). "Starvation proteins in Escherichia coli: kinetics of synthesis and role in starvation survival". Journal of Bacteriology. 168 (2): 486–493. doi:10.1128/jb.168.2.486-493.1986. PMID 3536847 – via jb.asm.org.
  20. ^ a b Reeve, C. A.; Amy, P. S.; Matin, A. (December 1, 1984). "Role of protein synthesis in the survival of carbon-starved Escherichia coli K-12". Journal of Bacteriology. 160 (3): 1041–1046. PMID 6389505 – via jb.asm.org.
  21. ^ a b Schultz, J. E.; Latter, G. I.; Matin, A. (September 1, 1988). "Differential regulation by cyclic AMP of starvation protein synthesis in Escherichia coli". Journal of Bacteriology. 170 (9): 3903–3909. doi:10.1128/jb.170.9.3903-3909.1988. PMID 2842291 – via jb.asm.org.
  22. ^ "Starvation-induced cross protection against heat or H2O2 challenge in Escherichia coli".
  23. ^ "Starvation-induced cross protection against osmotic challenge in Escherichia coli".
  24. ^ "The putative sigma factor KatF has a central role in development of starvation-mediated general resistance in Escherichia coli".
  25. ^ "Stress, Bacterial:General and Specific. Reference Module in Biomedical Science" (PDF).
  26. ^ Sonenshein AL (April 2005). "CodY, a global regulator of stationary phase and virulence in Gram-positive bacteria". Current Opinion in Microbiology. 8 (2): 203–7. doi:10.1016/j.mib.2005.01.001. PMID 15802253.
  27. ^ a b Schweder, T.; Lee, K. H.; Lomovskaya, O.; Matin, A. (January 1, 1996). "Regulation of Escherichia coli starvation sigma factor (sigma s) by ClpXP protease". Journal of Bacteriology. 178 (2): 470–476. doi:10.1128/jb.178.2.470-476.1996. PMID 8550468 – via jb.asm.org.
  28. ^ "The molecular basis of carbon-starvation-induced general resistance in Escherichia coli".
  29. ^ Lynch, S. V.; Brodie, E. L.; Matin, A. (December 16, 2004). "Role and Regulation of σs in General Resistance Conferred by Low-Shear Simulated Microgravity in Escherichia coli". Journal of Bacteriology. 186 (24): 8207–8212. doi:10.1128/JB.186.24.8207-8212.2004. PMID 15576768 – via PubMed Central.
  30. ^ Singh, Rachna; Matin, A. C. (April 16, 2016). Nickerson, Cheryl A.; Pellis, Neal R.; Ott, C. Mark (eds.). Effect of Spaceflight and Spaceflight Analogue Culture on Human and Microbial Cells: Novel Insights into Disease Mechanisms. Springer. pp. 259–282. doi:10.1007/978-1-4939-3277-1_13 – via Springer Link.
  31. ^ "DnaK-Mediated Alterations in Human Growth Hormone Protein Inclusion Bodies".
  32. ^ Xiong, A.; Gottman, A.; Park, C.; Baetens, M.; Pandza, S.; Matin, A. (October 1, 2000). "The EmrR Protein Represses the Escherichia coli emrRAB Multidrug Resistance Operon by Directly Binding to Its Promoter Region". Antimicrobial Agents and Chemotherapy. 44 (10): 2905–2907. doi:10.1128/AAC.44.10.2905-2907.2000. PMID 10991887 – via aac.asm.org.
  33. ^ a b Lomovskaya, O.; Lewis, K.; Matin, A. (May 1, 1995). "EmrR is a negative regulator of the Escherichia coli multidrug resistance pump EmrAB". Journal of Bacteriology. 177 (9): 2328–2334. doi:10.1128/jb.177.9.2328-2334.1995. PMID 7730261 – via jb.asm.org.
  34. ^ "Differential regulation of the mcb and emr operons of Escherichia coli: role of mcb in multidrug resistance".
  35. ^ Lynch, S. V.; Mukundakrishnan, K.; Benoit, M. R.; Ayyaswamy, P. S.; Matin, A. (December 1, 2006). "Escherichia coli Biofilms Formed under Low-Shear Modeled Microgravity in a Ground-Based System". Applied and Environmental Microbiology. 72 (12): 7701–7710. doi:10.1128/AEM.01294-06. PMID 17028231 – via aem.asm.org.
  36. ^ "Payload hardware and experimental protocol development to enable future testing of the effect of space microgravity on the resistance to gentamicin of uropathogenic Escherichia coli and its σs-deficient mutant". Life Sciences in Space Research. 15: 1–10. November 1, 2017. doi:10.1016/j.lssr.2017.05.001 – via www.sciencedirect.com.
  37. ^ "EcAMSat spaceflight measurements of the role of σs in antibiotic resistance of stationary phase Escherichia coli in microgravity". Life Sciences in Space Research. 24: 18–24. February 1, 2020. doi:10.1016/j.lssr.2019.10.007 – via www.sciencedirect.com.
  38. ^ "Payload hardware and experimental protocol development to enable future testing of the effect of space microgravity on the resistance to gentamicin of uropathogenic Escherichia coli and its σs-deficient mutant" (PDF).
  39. ^ Stone, G.; Wood, P.; Dixon, L.; Keyhan, M.; Matin, A. (August 16, 2002). "Tetracycline Rapidly Reaches All the Constituent Cells of Uropathogenic Escherichia coli Biofilms". Antimicrobial Agents and Chemotherapy. 46 (8): 2458–2461. doi:10.1128/AAC.46.8.2458-2461.2002. PMID 12121918 – via PubMed Central.
  40. ^ Lynch, S. V.; Dixon, L.; Benoit, M. R.; Brodie, E. L.; Keyhan, M.; Hu, P.; Ackerley, D. F.; Andersen, G. L.; Matin, A. (October 1, 2007). "Role of the rapA Gene in Controlling Antibiotic Resistance of Escherichia coli Biofilms". Antimicrobial Agents and Chemotherapy. 51 (10): 3650–3658. doi:10.1128/AAC.00601-07. PMID 17664315 – via aac.asm.org.
  41. ^ "TARGETS OF IMPROVEMENT IN BACTERIAL CHROMATE BIOREMEDIATION" (PDF).
  42. ^ "Mechanism of chromate reduction by the Escherichia coli protein, NfsA, and the role of different chromate reductases in minimizing oxidative stress during chromate reduction".
  43. ^ Ackerley, D. F.; Barak, Y.; Lynch, S. V.; Curtin, J.; Matin, A. (May 16, 2006). "Effect of chromate stress on Escherichia coli K-12". Journal of Bacteriology. 188 (9): 3371–3381. doi:10.1128/JB.188.9.3371-3381.2006. PMC 1447458. PMID 16621832 – via PubMed.
  44. ^ Gonzalez, Claudio F.; Ackerley, David F.; Lynch, Susan V.; Matin, A. (June 17, 2005). "ChrR, a Soluble Quinone Reductase of Pseudomonas putida That Defends against H2O2*". Journal of Biological Chemistry. 280 (24): 22590–22595. doi:10.1074/jbc.M501654200. PMID 15840577 – via www.jbc.org.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  45. ^ "Editorial Board". London Journals Press.
Retrieved from "https://en.wikipedia.org/w/index.php?title=A._C._Matin&oldid=1018092734"