Molecular Medicine - Nomenclature

AMA Manual of Style - Stacy L. Christiansen, Cheryl Iverson 2020

Molecular Medicine
Nomenclature

Molecules and their interactions underlie every area of medicine. Many classes of molecules are described according to rules or conventions, some of which are covered in other sections of this chapter. The Joint Commission on Biochemical Nomenclature formulates nomenclature policy for classes of biochemicals.1 The Joint Commission on Biochemical Nomenclature enzyme nomenclature is described in 14.10.3, Enzyme Nomenclature.2 The US National Center for Biotechnology Information is a searchable information resource on molecular biology with links to databases.3

This section provides information on various molecular terms, including expansions, derivations, typography, and usage information (but not rules for naming molecules). It is meant to assist the editor or reader encountering an unfamiliar term and to guide the author in using such terms. For terms not described herein, helpful sources include the Medical Subject Headings database of the National Library of Medicine,4 medical texts and dictionaries, and internet searches. For a review of molecular biology databases, see the 2016 Database Issue of Nucleic Acids Research.5

14.10.1 Molecular Terminology: Other Sections of Chapter 14.

The following sections of chapter 14 have subsections on molecular terms: 14.2, Cancer; 14.3, Cardiology; and 14.11, Neurology. The following sections of chapter 14 substantially deal with molecular terminology: 14.1, Blood Groups, Platelet Antigens, and Granulocyte Antigens; 14.6, Genetics; 14.7, Hemostasis; and 14.8, Immunology.

Table 14.10-1 gives molecular terms associated with subjects covered elsewhere in this chapter.

Table 14.10-1. Molecular Terms and Chapter Section Numbers

Entity

Section

amino acids

14.6.1, Nucleic Acids and Amino Acids

antitrypsins, antithrombins

14.7.4, Inhibition of Coagulation and Fibrinolysis

apolipoproteins

14.3.12, Cellular and Molecular Cardiology

bacterial strains and proteins

14.14.2, Bacteria: Additional Terminology

blood gas terminology (eg, PaO2)

14.16, Pulmonary and Respiratory Terminology

cancer molecules

14.2.5, Molecular Cancer Terminology 14.6.3, Oncogenes and Tumor Suppressor Genes

cellular adhesion molecules

14.7.2, Endothelial Factors 14.8, Immunology

chemokines

14.8, Immunology

chromosomes

14.6.4, Human Chromosomes

cloning vectors

14.6.1, Nucleic Acids and Amino Acids

clotting factors

14.7.3, Secondary Hemostasis (Amplification and Propagation)

clusters of differentiation (CDs)

14.8, Immunology 14.1.2, Platelet-Specific Antigens

codons

14.6.1, Nucleic Acids and Amino Acids

colony-stimulating factors

14.8, Immunology

complement

14.8, Immunology

creatine kinases

14.3.12, Cellular and Molecular Cardiology

cytokines

14.8, Immunology

D-dimer

14.7.4, Inhibition of Coagulation and Fibrinolysis

DNA

14.6.1, Nucleic Acids and Amino Acids

genes

14.6.2, Human Gene Nomenclature 14.6.3, Oncogenes and Tumor Suppressor Genes 14.6.5, Nonhuman Genetic Terms

glycoproteins

14.1.2, Platelet-Specific Antigens 14.7.1, Primary Hemostasis (Initiation) 14.7.2, Endothelial Factors

guanine nucleotides

14.3.12, Cellular and Molecular Cardiology 14.6.1, Nucleic Acids and Amino Acids

hemostatic molecules

14.7.1, Primary Hemostasis (Initiation)

hepatitis antigens and antibodies

14.14.3, Virus Nomenclature

histones

14.6.1, Nucleic Acids and Amino Acids

HLA antigens

14.8, Immunology

immunoglobulins

14.8, Immunology

influenza types and strains

14.14.3, Virus Nomenclature

integrins

14.7.2, Endothelial Factors

interferon

14.8, Immunology

interleukins

14.8, Immunology

ion channels

14.11.5, Molecular Neuroscience

lipoproteins

14.3.12, Cellular and Molecular Cardiology

muscle cell components

14.3.12, Cellular and Molecular Cardiology

mutations

14.6.1, Nucleic Acids and Amino Acids

myosin chains

14.7.1, Primary Hemostasis (Initiation)

neurotransmitters and receptors

14.11.5, Molecular Neuroscience

nitric oxide synthase

14.3.12, Cellular and Molecular Cardiology 14.7.2, Endothelial Factors

nodal cells

14.3.12, Cellular and Molecular Cardiology

nucleic acid technology (eg, polymerase chain reaction [PCR], single-nucleotide variations [SNVs] (formerly single-nucleotide polymorphisms [SNPs]), short tandem repeats [STRs])

14.6.1, Nucleic Acids and Amino Acids

nucleosides, nucleotides

14.6.1, Nucleic Acids and Amino Acids

phages

14.14.3, Virus Nomenclature

phospholipase

14.7.1, Primary Hemostasis (Initiation)

plasminogen activators

14.3.12, Cellular and Molecular Cardiology 14.7.2, Endothelial Factors

platelet-activating factors

14.7.1, Primary Hemostasis (Initiation)

prions

14.14.3, Virus Nomenclature

prostaglandins

14.7.1, Primary Hemostasis (Initiation)

restriction enzymes

14.6.1, Nucleic Acids and Amino Acids

retrovirus gene terms

14.6.3, Oncogenes and Tumor Suppressor Genes 14.6.5, Nonhuman Genetic Terms

RNA

14.6.1, Nucleic Acids and Amino Acids

serotonin

14.11.5, Molecular Neuroscience

thromboxanes

14.7.1, Primary Hemostasis (Initiation)

troponins

14.3.12, Cellular and Molecular Cardiology

von Willebrand factor

14.7.3, Secondary Hemostasis (Amplification and Propagation)

14.10.2 Molecular Terms: Considerations and Examples.

Molecular terms often are more familiar in unexpanded form; their expansions may be obscure. Molecular terms often mix numbers, letters, and cases. They may be abbreviations or abbreviations within abbreviations (for instance, see TAF and subsequent entries in Table 14.10-2). Molecular terms differ from standard abbreviations, which typically are uppercase initialisms (eg, PVC for premature ventricular contraction). In contrast, many molecular terms are (or incorporate) contractions of single words, using all lowercase letters or mixing capital and lowercase letters (eg, apo for apolipoprotein; Hb for hemoglobin).

Letter prefixes (including Greek letters) and numeric prefixes are linked to the main term by hyphens.

α1-antitrypsin

β-catenin

λ-tubulin

glucose 6-phosphate

However, these terms are not hyphenated:

α helix

β sheet

Hyphens are added in adjectival usages:

β-pleated sheet

glucose-6-phosphate dehydrogenase

Hyphens are used as follows in numbers that interrupt a word:

propan-1,2-diol (propanol)

flavan-3-ol

For letter or number suffixes, hyphens typically are not used with expanded terms but are handled in various ways with abbreviated terms:

interleukin 1 (IL-1)

phosphodiesterase 3A (PDE3A)

6-keto prostaglandin F (6-keto PGF)

The chemical prefixes L (levo) and D (dextro) are small capitals when referring to biomolecules, such as amino acids and carbohydrates, in the D/L system of configuration.

L-folinic acid

D-glutaraldehyde

Element symbols in chemical names, such as S (sulfur) and N (nitrogen), are italicized. Other capital letters are not italicized.

N-acetyl-D-glucosamine

cytochrome P450

N-terminal, C-terminal

D-dimer

A subscript letter indicates a modifier of the main term.

Pi (inorganic phosphate)

Plus signs and minus signs that indicate charges are set superscript. Numerals that indicate quantities of an element within a molecule are set subscript. Numerals that indicate a charge are set superscript.

HCO3

Fe3+

Although proteins may often be expressed as p plus a numeral signifying the atomic weight in kilodaltons (eg, p53, a 53-kDa protein), p53 is an alias or nickname and should be replaced with the official symbol, TP53 (see Table 14.10-2 and 14.6.3.2, Tumor Suppressor Genes). Affixes, such as superscripts, further specify the protein (important because different proteins may have the same weight) (Table 14.10-2). Although the gene symbols for such proteins are often given as the same term italicized (eg, the tumor suppressor gene p53), the correct gene symbols should be used (eg, in humans TP53, in mice, Tp53). Use the search feature at the HUGO Gene Nomenclature Committee website6 (see 14.6, Genetics).

The term stem cell has the general meaning of a precursor, pluripotent, or progenitor cell. Research articles should specify the type(s) of stem cell referred to, for example, adult, bone marrow, embryonic, germline, hematopoietic, mesenchymal, neural, peripheral blood, somatic, umbilical cord—derived, unrestricted somatic, and so forth. (The preceding terms are not all mutually exclusive.)

Terms in Table 14.10-2 are included as a reference. Some context or explanation of such terms is desirable at first mention, but, in contrast to abbreviations (see 13.0, Abbreviations), first mention need not be a literal expansion and the term may be stated as an appositive rather than in parentheses:

the cyclin-dependent kinase CDK2

When an abbreviation is used in the Suggested Usage at First Mention column in Table 14.10-2, it is assumed that in the article the abbreviated term has already been introduced and defined or expanded; for example, if INK4 (an alias [not the official symbol] for CDKN2A) is defined as “inhibitors of CDK4” at first mention, it is assumed that CDK4 was previously defined or expanded. Providing more information is often helpful. For instance, at first mention, CDKN1A (alias [not the official symbol]: p21) may be referred to as “cyclin-dependent kinase (CDK) inhibitor 1A” or given additional context (see Table 14.10-2 for further explanation of these terms).

Table 14.10-2. Molecular Terms and Explanations

Official term (aliasa)

Explanation

Suggested usage at first mention

Aβ peptide, Aβ42

amyloid-β peptide

amyloid-β peptide (Aβ), Aβ42 peptide, or 42-residue form of Aβ

Aβ*56

56-kDa Aβ fragment

56-kDa Aβ fragment

Ach

acetylcholine

acetylcholine

Acrp30 (or adiponectin)

adipocyte-complement—related 30-kDa protein

the protein Acrp30 or adiponectin

acyl-CoA

acyl derivatives of coenzyme A

acyl coenzyme A

acyl-S-CoA

sulfonated acyl-CoA

sulfonated acyl—coenzyme A

ADAMTS7

a disintegrin like and metalloprotease domain (reprolysin-type) with thrombospondin type 1 motifs

ADAMTS protease

specific ADAMTS, eg, ADAMTS-13

ADAMTS-13; trivial name von Willebrand factor (VWF) protease (see 14.7, Hemostasis)

ADAMTS-13 and/or vWFc protease

adoHcy

S-adenosylhomocysteine

S-adenosylhomocysteine

ado-Met (also SAM)

S-adenosylmethionine

S-adenosylmethionine

Akt kinase

a serine-threonine kinase, also known as protein kinase B, related to akt oncogene (origin: AKT retrovirus isolated from AKR mouse thymoma)

Akt protein kinase

allo-SCT

allogeneic stem cell transplant

allogeneic stem cell transplant

ATCase

aspartate transcarbamoylase

aspartate transcarbamoylase

ATPase

adenosine triphosphatase

adenosine triphosphatase

BNP

brain (or b-type) natriuretic peptide

brain (or b-type) natriuretic peptide

1,3-BPG

1,3-bisphosphoglycerate

1,3-bisphosphoglycerate

CAK (or cyclin H/CDK7)

CDK-activating enzyme

the CDK-activating enzyme (CAK) cyclin H/CDK7

CaM

calmodulin

calmodulin

CDK2, CDK3, CDK7, etc

cyclin-dependent kinases

the cyclin-dependent kinase CDK2, etc

CDKI

CDK inhibitors (see INK4 below)

CDK inhibitors

CoA

coenzyme A

coenzyme A

COX-1, COX-2

cyclooxygenases 1 and 2

cyclooxygenase 1 (COX-1), cyclooxygenase 2 (COX-2)

C-reactive protein

protein reactive to pneumococcal cell wall C polysaccharide

C-reactive protein (CRP)

cyclin D/CDK4/CDK6, cyclin E/CDK2

cyclin-CDK complexes

the cyclin D/CDK4/CDK6 complex; the cyclin E/CDK2 complex

CYP1A2, CYP2C9, CYP2C19, CYP2D6, CYP3A4

isoforms of cytochrome P450 enzymes (also cytochrome P450 isozymes) (P: pigment; 450: 450-nm absorbance)

various, eg, cytochrome P450 1A2 isozyme (CYP1A2); cytochrome P450 3A4 isozyme (CYP3A4 or P450 3A4 or 3A4)

Dkk-1

dickkopf-1

the inhibitor protein Dkk-1

F0 (subscript is zero, not capital O)

portion of mitochondrial ATP synthase (F: energy-coupling factor)

context, eg, F0 portion of mitochondrial ATP synthase, proton channel portion of ATP synthase, etc

F0F1

complex portion of mitochondrial ATP synthase

context, eg, F0F1 mitochondrial ATP synthase, F0F1 complex, etc

F1

portion of mitochondrial ATP synthase

context, eg, F1 portion of mitochondrial ATP synthase, catalytic portion of ATP synthase

F1P, F6P

fructose 1-phosphate, fructose 6-phosphate

fructose 1-phosphate, fructose 6-phosphate

FAD

flavin adenine dinucleotide

flavin adenine dinucleotide

FADH2

reduced (hydrogenated) FAD

FADH2or reduced (or hydrogenated) FAD

FBPase-1, FBPase-2

fructose 1,6-bisphosphatase, fructose 2,6-bisphosphatase

fructose 1,6-bisphosphatase, fructose 2,6-bisphosphatase

Fd

ferredoxin

ferredoxin

Fhit

fragile histidine triad protein

fragile histidine triad protein

FMN

flavin mononucleotide

flavin mononucleotide

FMNH2

reduced (hydrogenated) FMN

FMNH2or reduced (or hydrogenated) FMN

Fp

flavoprotein

flavoprotein (Fp)

G0

quiescent state of cell cycle

G0 phase

G1

growth or gap 1 phase of cell cycle

G1 phase

G2

growth or gap 2 phase of cell cycle

G2 phase

G protein

guanine triphosphate (GTP)—binding protein

G protein

Gα, Gβ, Gγ

G protein families

Gα, Gβ, Gγ protein or family

Gα12, Gα13

members of Gα

Gα12, Gα13 protein

Gβγ, βγ

Gβ subunit or complex

Gβγ, βγ subunit or complex

G1P, G6P

glucose 1-phosphate, glucose 6-phosphate

glucose 1-phosphate, glucose 6-phosphate

GalN

D-galactosamine

D-galactosamine

GalNAc

N-acetyl-D-galactosamine

N-acetyl-d-galactosamine

Gi

inhibitory G protein

inhibitory G protein

Glc or D-Glc

D-glucose

glucose orD-glucose

Gq, Gq/11

classes of G protein

Gq, Gq/11 protein

Gs

stimulatory G protein

stimulatory G protein

GlcA

D-gluconic acid

gluconic acid orD-gluconic acid

GlcNAc (also NAG)

N-acetyl-D-glucosamine

N-acetyl-D-glucosamine GlcNAc

GlcUA

D-glucuronic acid

D-glucuronic acid

Grb2

growth factor receptor—bound protein 2

the protein Grb2

H2F (also DHF)

dihydrofolate or 7,8-dihydrofolate

dihydrofolate (H2F or DHF) or 7,8-dihydrofolate (H2F or DHF)

H4F (also THF)

tetrahydrofolate or 5,6,7,8-tetrahydrofolate

tetrahydrofolate or 5,6,7,8-tetrahydrofolate

Hb

hemoglobin

hemoglobin

HbA1a, HbA1b, HbA1c

glycated (not glycosylated; Lyn Reynolds, editorial office director, Diabetes, email communication, May 21, 2013) hemoglobin fractions

preferred: glycated hemoglobin A1c (HbA1c), etc (also: glycohemoglobin A1c)

HbCO

carbon monoxyhemoglobin, carboxyhemoglobin

carbon monoxyhemoglobin

HbO2

oxyhemoglobin

oxyhemoglobin

HER2/neu

from human epidermal growth factor receptor 2; preferred term is now ERBB2; see 14.6.3, Oncogenes and Tumor Suppressor Genes

ERBB2 (formerly HER2 or HER2/neu)

HMG-CoA

β-hydroxy-β-methylglutaryl-CoA

β-hydroxy-β-methylglutaryl-CoA (but statins, not HMG-CoA inhibitors)

IKKβ

IκB kinase β (I: inhibitor)

IκB kinase β

CDKN2A (INK4)

inhibitors of CDK4 (see CDKI above and p16Ink4, etc, below)

inhibitors of CDK4

IGF-1, IGF-2

insulinlike growth factor, type 1 and type 2

insulinlike growth factor 1, insulinlike growth factor 2

IGF-1R, IGF-22

IGF-1 receptor, IGF-2 receptor

IGF-1 receptor, IGF-2 receptor

IP3

inositol 1,4,5-triphosphate

inositol 1,4,5-triphosphate

α-KG

α-ketoglutarate

α-ketoglutarate

lac

lactose

lactose

M

mitosis (phase of cell cycle)

M phase

Man

D-mannose

D-mannose

Mb

myoglobin (do not confuse with Mb, megabase, or MB, megabyte)

myoglobin

MbO2

oxymyoglobin

oxymyoglobin

M-CDK

M-cyclin—CDK complex

M-phase CDK

Mcm proteins

minichromosome maintenance proteins

Mcm proteins

M-cyclin

M-kinase—cyclin complex

M-cyclin

M-kinase

mitosis-phase kinase

M-kinase

Mur

muramic acid

muramic acid

Mur2Ac (also NAM)

N-acetylmuramic acid

N-acetylmuramic acid

NAD

nicotinamide adenine dinucleotide

nicotinamide adenine dinucleotide (NAD) or the nicotinamide coenzyme NAD

NAD+

oxidized NAD

NAD+

NADH

reduced (hydrogenated) NAD

reduced (or hydrogenated) NAD or NADH

NADH hydrogenase

NADH hydrogenase

NADH hydrogenase

NADP

NAD phosphate

NAD phosphate or NADP

NADPH

reduced (hydrogenated) NADP

reduced (or hydrogenated) NADP or NADPH

NAG

(see GlcNAc above)


Neu5Ac

N-acetylneuraminic acid (sialic acid)

N-acetylneuraminic acid

NFκB

nuclear factor—κB

nuclear factor—κB (NF-κB or NF-B)

NMDA

N-methyl-D-aspartate

N-methyl-D-aspartate

NMN

nicotinamide mononucleotide

nicotinamide mononucleotide

NMN+

oxidized NMN

NMN+

NMNH

reduced (hydrogenated) NMN

reduced or hydrogenated NMN

NMP

nucleoside monophosphate

nucleoside monophosphate

NOx

nitrogen oxides, such as nitrate, nitrite, and nitrosothiols; nitric oxide (NO) metabolites

nitrogen oxides

NPY

neuropeptide Y

neuropeptide Y

NT-proBNP

N-terminal fragment of the prohormone brain natriuretic peptide (see 14.6.1.5, Amino Acids)

N-terminal fragment of the prohormone brain natriuretic peptide

p16Ink4, p15Ink4B, p18Ink4C, p19Ink4D

INK4s

the INK4 p16Ink4, etc

CDKN1A (p21)

21-kDa protein

the protein CDKN1A

p21WAFI/CIP1, p27KIP1, p57KIP2

other CDKI; WAFI: wild-type p53-activated protein 1; CIP1: CDK-interacting protein 1; KIP: kinase inhibitor protein

the CDKI p21WAFI/CIP1, etc

TP53 (p53)

53-kDa protein

the protein TP53

CDKN1C (p57)

57-kDa protein

the protein CDKN1C

PE, PPE

protein or gene family named for amino acid sequence motif (PE: Pro-Glu, PPE: Pro-Pro-Glu; see 14.6.1, Nucleic Acids and Amino Acids)

PE and PPE protein families, PE/PPE gene families, etc

P-gp

P-glycoprotein

P-glycoprotein

Pi

inorganic phosphate

inorganic phosphate

PI

phosphatidyl inositol

phosphatidyl inositol

PIP2

phosphatidylinositol 4,5-bisphosphate

phosphatidylinositol 4,5-bisphosphate

Pol

polymerase (eg, DNA, RNA)

polymerase

PPi

inorganic pyrophosphate

inorganic pyrophosphate

pRb

retinoblastoma protein

retinoblastoma protein

PYY3-36

NPY receptor agonist (P: peptide; Y: NPY; Y: Y2 receptor; 3-36: 34 amino acid residue numbers)

peptide YY3-36, the gut hormone PYY3-36

RANKL

receptor-activated nuclear factor—κB ligand

receptor-activated nuclear factor—κB ligand

RecA protein, RecA

recombinase A

recombinase A

RNAi

RNA interference

RNA interference

R point

restriction point (of cell cycle)

R point

RNase

ribonuclease

ribonuclease

rTpo

recombinant thrombopoietin

recombinant thrombopoietin

S

DNA synthesis phase of cell cycle

S phase or DNA synthesis phase

S-cyclin

S-kinase—cyclin complex

S-cyclin

sFlt-1

soluble fms-like tyrosine kinase 1 (fms: McDonough feline sarcoma [oncogene])

soluble fms-like tyrosine kinase 1

S-kinase

synthesis-phase kinase

S-kinase

αSp22

22-kDa glycosylated form of α-synuclein

22-kDa glycosylated α-synuclein

αSyn

α-synuclein

α-synuclein

TAF

TBP-associated factor

TATA-binding protein (TBP)—associated factor

TAFII

a class of TAFs

a class of factors associated with TBP

TATA box

a DNA sequence rich in adenine (A) and thymidine (T)

TATA box

TBP

TATA-binding protein

TATA-binding protein

TFIID

complex of TBP and several TAFIIs

TBP-TAFII complex

UCP-1, UCP-2, UCP-3

uncoupling proteins

uncoupling protein 1, and so on

UDP-Gal

uridine diphosphate galactose

UDP-galactose

UDP-Glc

UDP-glucose

UDP-glucose

uE3

unconjugated estriol

unconjugated E3

Wnt

named for Drosophila melanogaster wingless mutant integration site

the developmental protein Wnt, the Wnt signaling pathway, etc

a Although these gene symbol aliases or nicknames, a result of their discovery before the completion of the Genome Project, may still be used by some, use of the approved gene symbol, not the alias, is strongly preferred. This usage will minimize confusion and make it possible to provide links to genomic databases for online versions of the article and to facilitate data retrieval in a number of databases. If an author insists on using an alias, provide the alias parenthetically after the approved gene symbol at first mention in text and abstract. This will link the two and provide a learning experience for those not yet familiar with the approved gene symbol.

14.10.3 Enzyme Nomenclature.

Enzyme nomenclature was formalized in the 1950s.2 It is formulated by the International Union of Biochemistry (IUB) and the International Union of Pure and Applied Chemistry (IUPAC), more specifically, the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (NC-IUBMB) and the IUPAC-IUB Joint Commission on Biochemical Nomenclature, and “is probably the single largest task of the committee.”2

Supplements of new enzymes are published annually. A complete list is available online.8 This list is searchable and includes the recommended name and number of each enzyme. Officially assigned names and numbers for enzymes are available at the Enzyme Nomenclature database,2 along with rules for enzyme nomenclature.

There are 3 types of enzyme names: recommended name (common, working, or trivial name), systematic name, and Enzyme Commission (EC) number. The recommended name is the name by which the enzyme is commonly known. The systematic name incorporates the reaction the enzyme catalyzes. The EC number is a unique identifier assigned to each enzyme.

Because systematic names can be unwieldy and recommended names are well known, recommended names are used in general medical publications. For unambiguous identification, the EC number, the systematic name, or both may be included at first mention.

The parts of the EC number are as follows:

class

subclass

sub-subclass

serial number within sub-subclass

The enzyme classes are as follows:

EC1

oxidoreductases

EC2

transferases

EC3

hydrolases

EC4

lyases

EC5

isomerases

EC6

ligases

Examples are shown in Table 14.10-3.

Table 14.10-3. Examples of Enzyme Class (EC) Names

EC No.

Recommended name

Systematic name

EC 1.11.1.7

peroxidase

phenolic donor:hydrogen-peroxide oxidoreductase

EC 2.3.3.10 (formerly EC 4.1.3.5)

hydroxymethylglutaryl-CoA synthase

acetyl-CoA:acetoacetyl-CoA C-acetyltransferase

EC 2.7.1.1

hexokinase

ATP:D-hexose 6-phosphotransferase

EC 3.1.1.7

acetylcholinesterase

acetylcholine acetylhydrolase

EC 3.5.2.6

β-lactamase

β-lactam hydrolase

EC 5.4.2.2

phosphoglucomutase

α-D-glucose 1,6-phosphomutase

EC 6.5.1.1

DNA ligase (ATP)

poly(deoxyribonucleotide):poly (deoxyribonucleotide) ligase (AMP-forming)

Principal Author: Cheryl Iverson, MA

Acknowledgment

Thanks to Boris C. Pasche, MD, PhD, Wake Forest Baptist Medical Center, Winston-Salem, North Carolina, and Mary L. (Nora) Disis, MD, JAMA Oncology, and Tumor Vaccine Medical Oncology, University of Washington, Seattle.

References

1.Biochemical Nomenclature Committees: International Union of Pure and Applied Chemistry and International Union of Biochemistry and Molecular Biology: IUPAC-IUBMB Joint Commission on Biochemical Nomenclature (JCBN) website. Updated July 23, 2019. Accessed August 1, 2019. https://www.qmul.ac.uk/sbcs/iubmb/

2.Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (NC-IUBMB). Enzyme Nomenclature database. Updated July 23, 2019. Accessed August 1, 2019. https://www.qmul.ac.uk/sbcs/iubmb/enzyme/

3.National Center for Biotechnology Information website. Accessed August 1, 2019. https://www.ncbi.nlm.nih.gov

4.Medical Subject Headings (MeSH): National Library of Medicine. Accessed August 1, 2019. https://www.ncbi.nlm.nih.gov/mesh

5.Rigden DJ, Fernández-Suárez XM, Galperin MY. The 2016 database issue of Nucleic Acids Research and an updated molecular biology database collection. Nucleic Acids Res. 2016;44(D1):D1-D6. doi:10.1093/nar/gkv1356

6.HUGO Gene Nomenclature Committee (HGNC) website. Accessed August 1, 2019. https://www.genenames.org/

7.ADAMTS13 gene. Published April 20, 2015. Accessed May 8, 2018. https://ghr.nlm.nih.gov/gene/ADAMTS13

8.McDonald AG, Boyce S, Tipton KF. ExporEnz: the primary source of the IUBMB enzyme list. Nucl Acids Res. 2009:37:D593-D597. doi:10.1093/nar/gkn582. https://www.gmul.ac.uk./sbcs/iubmb/enzyme/