The Date
U.S. Department of Homeland Security
Bureau of Citizenship and Immigration Services
To Whom It May Concern:
I am providing this opinion letter to Dr. Li’s petition for permanent residency in the United States. In 1999 I first met Dr. Li at the XXX Research Institute, where he was conducting postdoctoral research. While never a scientific collaborator, I have become familiar with his outstanding work through his publications in the field of XXX and XXX chemistry.
I myself am an organic chemist with a Ph.D. degree from XXX University. Currently I am an assistant professor in the Department of Chemistry at XXX University. A copy of my Curriculum Vitae is attached for your benefit and illustrates my credentials and standing in the international scientific community. My research interests bridge synthetic organic, physical, and materials chemistry. A primary theme is that of the rational, molecular design of materials formed by XXX and organic synthesis lies near the heart of all that we do. Our programs are funded by the National Science Foundation. Over ## publications and ## invited lectures have detailed aspects of my research in organic chemistry. My work has been recognized with receipts of many awards including a XXX Young Professor Award, a Research Innovation Award from Research Corp., a Camille and Henry Dreyfus New Faculty Award, an NIH Fellowship, a XXX Memorial Fellowship, and a XXX Scholar Award. In addition to being elected as program chairs at numerous international scientific conferences including the National Meeting of American Chemical Society, I also served as a consultant to DuPont Central Research Department from 19XX to 20XX.
Anyone familiar with Dr. Li’s science, becomes immediately impressed with the originality of his work as well as with the special blend of skills he brings to the arena of organic chemistry. His research involved the application of modern synthetic chemistry to the elucidation of enzyme mechanisms, important to several therapeutic areas. For example, his doctoral research on enzyme 1 culminated in a research paper “paper title” published in J. Am. Chem. Soc. 19XX, XXX, XXXX. In this paper Dr. Li designed and synthesized several inhibitors to investigate the mechanism of enzyme 1. Although the enzymatic mechanism was proposed twenty years ago, it is only through Dr. Li’s efforts that the structural details of the interaction of enzyme 1 with its substrate are being unraveled. Specifically his study provided evidence that part of the substrate XYZ acts as the base that catalyzes two of the steps supposedly catalyzed by the enzyme itself. This important discovery made him well known in the international community of enzyme 1 research and thus far, has been corroborated independently by other academic groups. For instance, Adams, etc. at XXX College (Biochemistry 20XX, XX, XXXXX) described that “consistent with the involvement of XXX in intramolecular proton transfer, we have found that substrate analog XXX, with its much lower pKa, is not a substrate for the archaeal enzyme 1”. Armed with a high affinity inhibitor synthesized by Dr. Li, Roberts group (J. Biol. Chem. 20XX, XXX, XXXX) solved a crystal structure of enzyme 1 and found that “the inhibitor molecule (made by Dr. Li) is well nestled within the enzyme active site” and “either XYZ or Lys-XXX may act as the base at the XXX step” while “in the XXX step, the XYZ could transfer the proton abstracted from C# to O#”.
On the therapeutic front, the utility of inhibitors for enzyme 1 has just been recognized. DEF and DEF-containing compounds are essential in all eukaryotes where they play important roles in cell signaling, membrane trafficking, cell survival, and even DNA repair. The possibility that DEF metabolism is involved in the etiology of XXX disorder is a hot topic. In a review article entitled “enzyme1: a possible new target for anti-XXX drugs” (journal name, 20XX, XX, XX), Bob, etc. in Israel cited the discovery by Dr. Li and claimed that “clinical evidence, behavioral studies and molecular studies implicate the involvement of DEF in the therapeutic mechanism of XXX and XXX and in the etiology of XXX disorder” and “enzyme 1 is suggested to play a role in this mechanism”. In prokaryotes, DEF-containing compounds are also involved in infection and pathology of XXX tuberculosis, a member of mycobacteria. According to a study carried out by the Daniel group in U.K. (Structure 20XX, XX, XXX), “enzymes in the DEF synthesis pathway are clear targets for novel anti-XXX therapeutics”. Furthermore, based on their observation that “limited sequence variation (exists) within the active site of the eukaryotic and the archaeal/mycobacterial enzyme 1”, known inhibitors of enzyme 1 such as those developed by Dr. Li might form the basis for developing selective inhibitors for the mycobacerial enzymes. Undoubtedly, Dr. Li’s important discovery has laid the foundation for more clinically oriented research.
Dr. Li also played a significant role in the sturdy of anti-microbial agents, aiming at diversification for the therapies available to fight pathogenic bacteria. The specific goal of his work was to find potent inhibitors of enzyme 2, an enzyme of the XXX pathway that is necessary for the survival of microbes. Once again, Dr. Li was successful, demonstrating that XXX inhibitors were as potent as the known, but therapeutically challenged, XXX inhibitors. This work was published in 199X in J. Org. Chem. and has been cited in a review article (Chem. Rev. 200X, 10X, XXX).
At XXX Research Institute Dr. Li worked on inhibition studies of enzyme 3, which is involved in the biosynthesis of XXX-conjugates associated with metastasis and inflammation in human. Inhibitors of enzyme 3 have potential applications in anti-inflammation or anti-cancer research. Dr. Li employed a unique strategy to identify inhibitors of enzyme 3 by using a novel scaffold to mimic the conformation of the transition state of the enzymatic reaction. His research showed that XXX and XXX of the transition state seem to contribute equally to the enzyme-catalyzed reaction. This study was published in 200X in Angew. Chem. Int. Ed. and received international attention immediately. It has already been cited by ## other international research groups for its significance to their own independent studies.
In summary, Dr. Li has distinguished himself as an outstanding scientist in the field of XXX and medicinal chemistry. There are few in the world who can match his expertise and talent in the technically demanding field of XXX and medicinal research targeting multiple enzymatic systems. Given his proven track record and unique qualifications, I fully expect him to make significant contributions to the very important and globally competitive area of pharmaceutical and biomedical research.
Sincerely,
John Doe, Ph.D.
Assistant professor of Chemistry
johnd@XXX.edu
U.S. Department of Homeland Security
Bureau of Citizenship and Immigration Services
To Whom It May Concern:
I am providing this opinion letter to Dr. Li’s petition for permanent residency in the United States. In 1999 I first met Dr. Li at the XXX Research Institute, where he was conducting postdoctoral research. While never a scientific collaborator, I have become familiar with his outstanding work through his publications in the field of XXX and XXX chemistry.
I myself am an organic chemist with a Ph.D. degree from XXX University. Currently I am an assistant professor in the Department of Chemistry at XXX University. A copy of my Curriculum Vitae is attached for your benefit and illustrates my credentials and standing in the international scientific community. My research interests bridge synthetic organic, physical, and materials chemistry. A primary theme is that of the rational, molecular design of materials formed by XXX and organic synthesis lies near the heart of all that we do. Our programs are funded by the National Science Foundation. Over ## publications and ## invited lectures have detailed aspects of my research in organic chemistry. My work has been recognized with receipts of many awards including a XXX Young Professor Award, a Research Innovation Award from Research Corp., a Camille and Henry Dreyfus New Faculty Award, an NIH Fellowship, a XXX Memorial Fellowship, and a XXX Scholar Award. In addition to being elected as program chairs at numerous international scientific conferences including the National Meeting of American Chemical Society, I also served as a consultant to DuPont Central Research Department from 19XX to 20XX.
Anyone familiar with Dr. Li’s science, becomes immediately impressed with the originality of his work as well as with the special blend of skills he brings to the arena of organic chemistry. His research involved the application of modern synthetic chemistry to the elucidation of enzyme mechanisms, important to several therapeutic areas. For example, his doctoral research on enzyme 1 culminated in a research paper “paper title” published in J. Am. Chem. Soc. 19XX, XXX, XXXX. In this paper Dr. Li designed and synthesized several inhibitors to investigate the mechanism of enzyme 1. Although the enzymatic mechanism was proposed twenty years ago, it is only through Dr. Li’s efforts that the structural details of the interaction of enzyme 1 with its substrate are being unraveled. Specifically his study provided evidence that part of the substrate XYZ acts as the base that catalyzes two of the steps supposedly catalyzed by the enzyme itself. This important discovery made him well known in the international community of enzyme 1 research and thus far, has been corroborated independently by other academic groups. For instance, Adams, etc. at XXX College (Biochemistry 20XX, XX, XXXXX) described that “consistent with the involvement of XXX in intramolecular proton transfer, we have found that substrate analog XXX, with its much lower pKa, is not a substrate for the archaeal enzyme 1”. Armed with a high affinity inhibitor synthesized by Dr. Li, Roberts group (J. Biol. Chem. 20XX, XXX, XXXX) solved a crystal structure of enzyme 1 and found that “the inhibitor molecule (made by Dr. Li) is well nestled within the enzyme active site” and “either XYZ or Lys-XXX may act as the base at the XXX step” while “in the XXX step, the XYZ could transfer the proton abstracted from C# to O#”.
On the therapeutic front, the utility of inhibitors for enzyme 1 has just been recognized. DEF and DEF-containing compounds are essential in all eukaryotes where they play important roles in cell signaling, membrane trafficking, cell survival, and even DNA repair. The possibility that DEF metabolism is involved in the etiology of XXX disorder is a hot topic. In a review article entitled “enzyme1: a possible new target for anti-XXX drugs” (journal name, 20XX, XX, XX), Bob, etc. in Israel cited the discovery by Dr. Li and claimed that “clinical evidence, behavioral studies and molecular studies implicate the involvement of DEF in the therapeutic mechanism of XXX and XXX and in the etiology of XXX disorder” and “enzyme 1 is suggested to play a role in this mechanism”. In prokaryotes, DEF-containing compounds are also involved in infection and pathology of XXX tuberculosis, a member of mycobacteria. According to a study carried out by the Daniel group in U.K. (Structure 20XX, XX, XXX), “enzymes in the DEF synthesis pathway are clear targets for novel anti-XXX therapeutics”. Furthermore, based on their observation that “limited sequence variation (exists) within the active site of the eukaryotic and the archaeal/mycobacterial enzyme 1”, known inhibitors of enzyme 1 such as those developed by Dr. Li might form the basis for developing selective inhibitors for the mycobacerial enzymes. Undoubtedly, Dr. Li’s important discovery has laid the foundation for more clinically oriented research.
Dr. Li also played a significant role in the sturdy of anti-microbial agents, aiming at diversification for the therapies available to fight pathogenic bacteria. The specific goal of his work was to find potent inhibitors of enzyme 2, an enzyme of the XXX pathway that is necessary for the survival of microbes. Once again, Dr. Li was successful, demonstrating that XXX inhibitors were as potent as the known, but therapeutically challenged, XXX inhibitors. This work was published in 199X in J. Org. Chem. and has been cited in a review article (Chem. Rev. 200X, 10X, XXX).
At XXX Research Institute Dr. Li worked on inhibition studies of enzyme 3, which is involved in the biosynthesis of XXX-conjugates associated with metastasis and inflammation in human. Inhibitors of enzyme 3 have potential applications in anti-inflammation or anti-cancer research. Dr. Li employed a unique strategy to identify inhibitors of enzyme 3 by using a novel scaffold to mimic the conformation of the transition state of the enzymatic reaction. His research showed that XXX and XXX of the transition state seem to contribute equally to the enzyme-catalyzed reaction. This study was published in 200X in Angew. Chem. Int. Ed. and received international attention immediately. It has already been cited by ## other international research groups for its significance to their own independent studies.
In summary, Dr. Li has distinguished himself as an outstanding scientist in the field of XXX and medicinal chemistry. There are few in the world who can match his expertise and talent in the technically demanding field of XXX and medicinal research targeting multiple enzymatic systems. Given his proven track record and unique qualifications, I fully expect him to make significant contributions to the very important and globally competitive area of pharmaceutical and biomedical research.
Sincerely,
John Doe, Ph.D.
Assistant professor of Chemistry
johnd@XXX.edu
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